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Conserved domains on  [gi|1032291014|gb|OAP05341|]
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hypothetical protein AXX17_AT3G53790 [Arabidopsis thaliana]

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 ...
119-394 1.11e-85

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 cd14066:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 272  Bit Score: 261.82  E-value: 1.11e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKGvqgaqpGPTLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLH 278
Cdd:cd14066    81 LHCHKG------SPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 STRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD-HTMPRGQQSLVTWATPRLSEdKVKQCVDPKLKGE 357
Cdd:cd14066   155 TSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDeNRENASRKDLVEWVESKGKE-ELEDILDKRLVDD 233
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1032291014 358 YP--PKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPL 394
Cdd:cd14066   234 DGveEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
119-394 1.11e-85

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: 261.82  E-value: 1.11e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKGvqgaqpGPTLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLH 278
Cdd:cd14066    81 LHCHKG------SPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 STRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD-HTMPRGQQSLVTWATPRLSEdKVKQCVDPKLKGE 357
Cdd:cd14066   155 TSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDeNRENASRKDLVEWVESKGKE-ELEDILDKRLVDD 233
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1032291014 358 YP--PKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPL 394
Cdd:cd14066   234 DGveEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
119-391 1.29e-44

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: 155.40  E-value: 1.29e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  119 IGEGSYGRAYYATLKDGKA-----VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:smart00221   7 LGEGAFGEVYKGTLKGKGDgkeveVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  194 SLHDILHGRKGvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS-NQSPD 272
Cdd:smart00221  87 DLLDYLRKNRP-------KELSLSDLLSFALQIARGMEYLESK---NFIHRDLAARNCLVGENLVVKISDFGLSrDLYDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  273 MAARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPvdhtmprgqqslvtwaTPRLSEDKVKQCVD 351
Cdd:smart00221 157 DYYKVKGGKL--PIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEP----------------YPGMSNAEVLEYLK 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1032291014  352 pklKGEY---PPKAVAKLAAVAALCVQYESEFRPNMSIVVKAL 391
Cdd:smart00221 219 ---KGYRlpkPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
119-321 3.76e-43

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: 151.50  E-value: 3.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA-----VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:pfam07714   7 LGEGAFGEVYKGTLKGEGEntkikVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHgrkgvqgaQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS-NQSPD 272
Cdd:pfam07714  87 DLLDFLR--------KHKRKLTLKDLLSMALQIAKGMEYLESK---NFVHRDLAARNCLVSENLVVKISDFGLSrDIYDD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 273 MAARLHSTRVLGTFGYhAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:pfam07714 156 DYYRKRGGGKLPIKWM-APESLKDGKFTSKSDVWSFGVLLWEIFTlGEQP 204
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
117-321 2.49e-39

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 146.70  E-value: 2.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKL--DNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:COG0515    13 RLLGRGGMGVVYLARdLRLGRPVALKVLrpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRkgvqgaqpGPtLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnQSPDM 273
Cdd:COG0515    93 SLADLLRRR--------GP-LPPAEALRILAQLAEALAAAHAA---GIVHRDIKPANILLTPDGRVKLIDFGIA-RALGG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 274 AARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:COG0515   160 ATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPP 207
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
116-400 2.01e-19

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 90.68  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYA-TLKDGKAVAVKKL-DNAAEPESnvefltQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:PLN00113  695 ENVISRGKKGASYKGkSIKNGMQFVVKEInDVNSIPSS------EIADMGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGK 768
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGrkgvqgaqpgptLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLfeDFKAKIadfNLSNQSPDM 273
Cdd:PLN00113  769 NLSEVLRN------------LSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIII--DGKDEP---HLRLSLPGL 831
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 274 AARlhSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMpRGQQSLVTWATPRLSEDKVKQCVDPK 353
Cdd:PLN00113  832 LCT--DTKCFISSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEF-GVHGSIVEWARYCYSDCHLDMWIDPS 908
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 354 LKGEYPPKAVAKLAAV--AALCVQYESEFRPNMSIVVKALQPLLRSSTA 400
Cdd:PLN00113  909 IRGDVSVNQNEIVEVMnlALHCTATDPTARPCANDVLKTLESASRSSSS 957
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
210-321 8.56e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 88.31  E-value: 8.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 210 PGPTL-DWIQR---------VRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN----LSNQSpdMAa 275
Cdd:NF033483   90 DGRTLkDYIREhgplspeeaVEIMIQILSALEHAHRN---GIVHRDIKPQNILITKDGRVKVTDFGiaraLSSTT--MT- 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1032291014 276 rlHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:NF033483  164 --QTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPP 207
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
119-394 1.11e-85

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: 261.82  E-value: 1.11e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKGvqgaqpGPTLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLH 278
Cdd:cd14066    81 LHCHKG------SPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 STRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD-HTMPRGQQSLVTWATPRLSEdKVKQCVDPKLKGE 357
Cdd:cd14066   155 TSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDeNRENASRKDLVEWVESKGKE-ELEDILDKRLVDD 233
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1032291014 358 YP--PKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPL 394
Cdd:cd14066   234 DGveEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
119-392 3.05e-71

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: 224.68  E-value: 3.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14664     1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLh 278
Cdd:cd14664    81 LHSR-----PESQPPLDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHV- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 STRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPRLSEDKVKQCVDPKLKGEY 358
Cdd:cd14664   155 MSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDGVDIVDWVRGLLEEKKVEALVDPDLQGVY 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1032291014 359 PPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQ 392
Cdd:cd14664   235 KLEEVEQVFQVALLCTQSSPMERPTMREVVRMLE 268
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
119-333 8.63e-62

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: 199.69  E-value: 8.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESNV-EFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd13999     1 IGSGSFGEVYKGKWR-GTDVAIKKLKVEDDNDELLkEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLS---NQSPDMa 274
Cdd:cd13999    80 LLHKKK--------IPLSWSLRLKIALDIARGMNYLH---SPPIIHRDLKSLNILLDENFTVKIADFGLSrikNSTTEK- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 275 arlhSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHtMPRGQQSL 333
Cdd:cd13999   148 ----MTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKE-LSPIQIAA 201
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
119-394 1.17e-56

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: 188.11  E-value: 1.17e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDgKAVAVKKLDNAAEPESNV---EFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd14159     1 IGEGGFGCVYQAVMRN-TEYAVKRLKEDSELDWSVvknSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHgrkgVQGAqpGPTLDWIQRVRIAVDAARGLEYLHEKvQPAVIHRDIRSSNVLLFEDFKAKIADFNL-----SNQS 270
Cdd:cd14159    80 EDRLH----CQVS--CPCLSWSQRLHVLLGTARAIQYLHSD-SPSLIHGDVKSSNILLDAALNPKLGDFGLarfsrRPKQ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 271 PDMAARL-HSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPV---------------------DHTMPR 328
Cdd:cd14159   153 PGMSSTLaRTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMevdscsptkylkdlvkeeeeaQHTPTT 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 329 GQQSLVTWATPrLSEDKVKQCVDPKLkGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPL 394
Cdd:cd14159   233 MTHSAEAQAAQ-LATSICQKHLDPQA-GPCPPELGIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
103-394 1.73e-56

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: 187.32  E-value: 1.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 103 LDELKEKTDNFGSKSLI------GEGSYGRAYYATLKDgKAVAVKKL---DNAAEPESNVEFLTQVSRVSKLKHDNFVEL 173
Cdd:cd14158     1 FHELKNMTNNFDERPISvggnklGEGGFGVVFKGYIND-KNVAVKKLaamVDISTEDLTKQFEQEIQVMAKCQHENLVEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 174 FGYCVEGNFRILAYEFATMGSLHDILHGRKGVqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLL 253
Cdd:cd14158    80 LGYSCDGPQLCLVYTYMPNGSLLDRLACLNDT------PPLSWHMRCKIAQGTANGINYLHEN---NHIHRDIKSANILL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 254 FEDFKAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEyAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTmpRGQQSL 333
Cdd:cd14158   151 DETFVPKISDFGLARASEKFSQTIMTERIVGTTAYMAPE-ALRGEITPKSDIFSFGVVLLEIITGLPPVDEN--RDPQLL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 334 VTWATPRLSEDK-VKQCVDPKLkGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPL 394
Cdd:cd14158   228 LDIKEEIEDEEKtIEDYVDKKM-GDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
119-321 5.53e-45

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: 156.55  E-value: 5.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGK----AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd00192     3 LGEGAFGEVYKGKLKGGDgktvDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS-NQSPDM 273
Cdd:cd00192    83 LLDFLRKSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASK---KFVHRDLAARNCLVGEDLVVKISDFGLSrDIYDDD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 274 AARLHSTRVLGTFgYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd00192   160 YYRKKTGGKLPIR-WMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATP 207
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
119-391 1.29e-44

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: 155.40  E-value: 1.29e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  119 IGEGSYGRAYYATLKDGKA-----VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:smart00221   7 LGEGAFGEVYKGTLKGKGDgkeveVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  194 SLHDILHGRKGvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS-NQSPD 272
Cdd:smart00221  87 DLLDYLRKNRP-------KELSLSDLLSFALQIARGMEYLESK---NFIHRDLAARNCLVGENLVVKISDFGLSrDLYDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  273 MAARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPvdhtmprgqqslvtwaTPRLSEDKVKQCVD 351
Cdd:smart00221 157 DYYKVKGGKL--PIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEP----------------YPGMSNAEVLEYLK 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1032291014  352 pklKGEY---PPKAVAKLAAVAALCVQYESEFRPNMSIVVKAL 391
Cdd:smart00221 219 ---KGYRlpkPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
119-315 1.34e-44

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: 153.97  E-value: 1.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd00180     1 LGKGSFGKVYKARdKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARL 277
Cdd:cd00180    81 LLKENKG--------PLSEEEALSILRQLLSALEYLHSN---GIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLL 149
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1032291014 278 HSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLEL 315
Cdd:cd00180   150 KTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
119-391 2.46e-44

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 154.61  E-value: 2.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  119 IGEGSYGRAYYATLKDGK-----AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:smart00219   7 LGEGAFGEVYKGKLKGKGgkkkvEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYMEGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  194 SLHDILHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS-NQSPD 272
Cdd:smart00219  87 DLLSYLRKNR--------PKLSLSDLLSFALQIARGMEYLESK---NFIHRDLAARNCLVGENLVVKISDFGLSrDLYDD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  273 MAARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVdhtmprgqqslvtwatPRLSEDKVKQCVD 351
Cdd:smart00219 156 DYYRKRGGKL--PIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPY----------------PGMSNEEVLEYLK 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1032291014  352 pklKGEY---PPKAVAKLAAVAALCVQYESEFRPNMSIVVKAL 391
Cdd:smart00219 218 ---NGYRlpqPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
119-321 3.76e-43

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: 151.50  E-value: 3.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA-----VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:pfam07714   7 LGEGAFGEVYKGTLKGEGEntkikVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHgrkgvqgaQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS-NQSPD 272
Cdd:pfam07714  87 DLLDFLR--------KHKRKLTLKDLLSMALQIAKGMEYLESK---NFVHRDLAARNCLVSENLVVKISDFGLSrDIYDD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 273 MAARLHSTRVLGTFGYhAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:pfam07714 156 DYYRKRGGGKLPIKWM-APESLKDGKFTSKSDVWSFGVLLWEIFTlGEQP 204
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
118-321 9.92e-41

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 144.98  E-value: 9.92e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  118 LIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:smart00220   6 KLGEGSFGKVYLARDKKtGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  197 DILHGRKGVqgaqpgpTLDWIQrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspdMAAR 276
Cdd:smart00220  86 DLLKKRGRL-------SEDEAR--FYLRQILSALEYLHSK---GIVHRDLKPENILLDEDGHVKLADFGLARQ---LDPG 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1032291014  277 LHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPP 195
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
117-327 5.38e-40

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: 143.11  E-value: 5.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKL--DNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd14014     6 RLLGRGGMGEVYRARdTLLGRPVAIKVLrpELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnQSPDM 273
Cdd:cd14014    86 SLADLLRERG---------PLPPREALRILAQIADALAAAHRA---GIVHRDIKPANILLTEDGRVKLTDFGIA-RALGD 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 274 AARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd14014   153 SGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSP 206
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
117-321 2.49e-39

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 146.70  E-value: 2.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKL--DNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:COG0515    13 RLLGRGGMGVVYLARdLRLGRPVALKVLrpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRkgvqgaqpGPtLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnQSPDM 273
Cdd:COG0515    93 SLADLLRRR--------GP-LPPAEALRILAQLAEALAAAHAA---GIVHRDIKPANILLTPDGRVKLIDFGIA-RALGG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 274 AARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:COG0515   160 ATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPP 207
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
119-399 3.52e-37

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: 135.64  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDgKAVAVKKLDNAAEPEsnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14058     1 VGRGSFGVVCKARWRN-QIVAVKIIESESEKK---AFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGrkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKA-KIADFNLSNqspDMAArl 277
Cdd:cd14058    77 LHG------KEPKPIYTAAHAMSWALQCAKGVAYLHSMKPKALIHRDLKPPNLLLTNGGTVlKICDFGTAC---DIST-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 278 HSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTmpRGQQSLVTWATPrlsedkvkqcvdpklKGE 357
Cdd:cd14058   146 HMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHI--GGPAFRIMWAVH---------------NGE 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1032291014 358 YPPKAV---AKLAAVAALCVQYESEFRPNMSIVVKALQPLLRSST 399
Cdd:cd14058   209 RPPLIKncpKPIESLMTRCWSKDPEKRPSMKEIVKIMSHLMQFFP 253
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
118-321 5.88e-37

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: 134.96  E-value: 5.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSRV-SKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd06606     7 LLGKGSFGSVYLALNLDtGELMAVKEVELSGDSEEELEALEREIRIlSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQgaqpgptldwIQRVRI-AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd06606    87 ASLLKKFGKLP----------EPVVRKyTRQILEGLEYLHSN---GIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIA 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 275 ARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06606   154 TGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPP 200
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
119-327 1.74e-35

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: 131.11  E-value: 1.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKdGKAVAVKKL-DNAAEPESNVE-FLTQVSRVSKLKHDNFVELFGYCVE--GNFRILAyEFATMGS 194
Cdd:cd14064     1 IGSGSFGKVYKGRCR-NKIVAIKRYrANTYCSKSDVDmFCREVSILCRLNHPCVIQFVGACLDdpSQFAIVT-QYVSGGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGVqgaqpgptLDWIQRVRIAVDAARGLEYLHEKVQPaVIHRDIRSSNVLLFEDFKAKIADFNLSN--QSPD 272
Cdd:cd14064    79 LFSLLHEQKRV--------IDLQSKLIIAVDVAKGMEYLHNLTQP-IIHRDLNSHNILLYEDGHAVVADFGESRflQSLD 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 273 MAarlHSTRVLGTFGYHAPE-YAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd14064   150 ED---NMTKQPGNLRWMAPEvFTQCTRYSIKADVFSYALCLWELLTGEIPFAHLKP 202
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
116-321 2.30e-35

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: 130.79  E-value: 2.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd05122     5 LEKIGKGGFGVVYKARhKKTGQIVAIKKINLESKEKKE-SILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspdMA 274
Cdd:cd05122    84 LKDLLKNTNK--------TLTEQQIAYVCKEVLKGLEYLHSH---GIIHRDIKAANILLTSDGEVKLIDFGLSAQ---LS 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 275 ARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05122   150 DGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPP 196
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
118-391 5.04e-33

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: 124.76  E-value: 5.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVK--KLDNAAEPESNVEFLTQVSRV-SKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd14146     1 IIGVGGFGKVYRATWK-GQEVAVKaaRQDPDEDIKATAESVRQEAKLfSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFK--------AKIADFNL 266
Cdd:cd14146    80 LNRALAAANAAPGPRRARRIPPHILVNWAVQIARGMLYLHEEAVVPILHRDLKSSNILLLEKIEhddicnktLKITDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 267 snqspdmAARLHSTRVL---GTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVdhtmpRGQQSLVTW---ATPR 340
Cdd:cd14146   160 -------AREWHRTTKMsaaGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY-----RGIDGLAVAygvAVNK 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 341 LSEDKVKQCVDP--KLKGEyppkavaklaavaalCVQYESEFRPNMSIVVKAL 391
Cdd:cd14146   228 LTLPIPSTCPEPfaKLMKE---------------CWEQDPHIRPSFALILEQL 265
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
120-336 7.50e-33

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: 123.53  E-value: 7.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 120 GEGSYGRAYYAT-LKDGKAVAVKKLdNAAEPESNVefltqvsrVSKLKHDNFVELFGYCVEG-NFRILAyEFATMGSLHD 197
Cdd:cd14060     2 GGGSFGSVYRAIwVSQDKEVAVKKL-LKIEKEAEI--------LSVLSHRNIIQFYGAILEApNYGIVT-EYASYGSLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKGVQgaqpgptLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKAKIADFNlsnqspdmAARL 277
Cdd:cd14060    72 YLNSNESEE-------MDMDQIMTWATDIAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFG--------ASRF 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 278 HS----TRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVdhtmpRGQQSL-VTW 336
Cdd:cd14060   137 HShtthMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF-----KGLEGLqVAW 195
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
118-321 2.69e-32

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: 122.50  E-value: 2.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVK--KLDNAAEPESNVEFLTQVSRV-SKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd14061     1 VIGVGGFGKVYRGIWR-GEEVAVKaaRQDPDEDISVTLENVRQEARLfWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKgvqgAQPGPTLDWiqrvriAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKA--------KIADFNL 266
Cdd:cd14061    80 LNRVLAGRK----IPPHVLVDW------AIQIARGMNYLHNEAPVPIIHRDLKSSNILILEAIENedlenktlKITDFGL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 267 snqspdmaAR--LHSTRV--LGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14061   150 --------ARewHKTTRMsaAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVP 200
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
116-321 6.78e-31

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: 118.61  E-value: 6.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKdGKAVAVKKL-DNAAEPESnveFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd05039    11 GELIGKGEFGDVMLGDYR-GQKVAVKCLkDDSTAAQA---FLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDIL--HGRKGVQGAqpgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpd 272
Cdd:cd05039    87 LVDYLrsRGRAVITRK---------DQLGFALDVCEGMEYLESK---KFVHRDLAARNVLVSEDNVAKVSDFGLAKEA-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 273 maarlHSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05039   153 -----SSNQDGGKLpiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVP 199
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
118-321 1.35e-29

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: 115.47  E-value: 1.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVK--KLDNAAEPESNVEFLTQVSRV-SKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd14148     1 IIGVGGFGKVYKGLWR-GEEVAVKaaRQDPDEDIAVTAENVRQEARLfWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKgvqgAQPGPTLDWiqrvriAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFE--------DFKAKIADFNL 266
Cdd:cd14148    80 LNRALAGKK----VPPHVLVNW------AVQIARGMNYLHNEAIVPIIHRDLKSSNILILEpienddlsGKTLKITDFGL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 267 S---NQSPDMAARlhstrvlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14148   150 ArewHKTTKMSAA-------GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVP 200
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
119-330 1.59e-28

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: 112.10  E-value: 1.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDgkAVAVKKLdNAAEP--ESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLH 196
Cdd:cd14062     1 IGSGSFGTVYKGRWHG--DVAVKKL-NVTDPtpSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVT-QWCEGSSLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHgrkgVQGAQpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd14062    77 KHLH----VLETK----FEMLQLIDIARQTAQGMDYLHAK---NIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGS 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 277 LHSTRVLGTFGYHAPEYA-MTGQ--LTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQ 330
Cdd:cd14062   146 QQFEQPTGSILWMAPEVIrMQDEnpYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQ 202
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
96-321 2.02e-28

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: 112.44  E-value: 2.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  96 IDVPALSLDELkektdnfgskslIGEGSYGRAYYAtLKDGKAVAVK--KLDNAAEPESNVEFLTQVSRV-SKLKHDNFVE 172
Cdd:cd14145     3 IDFSELVLEEI------------IGIGGFGKVYRA-IWIGDEVAVKaaRHDPDEDISQTIENVRQEAKLfAMLKHPNIIA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 173 LFGYCVEGNFRILAYEFATMGSLHDILHGRKgvqgAQPGPTLDWiqrvriAVDAARGLEYLHEKVQPAVIHRDIRSSNVL 252
Cdd:cd14145    70 LRGVCLKEPNLCLVMEFARGGPLNRVLSGKR----IPPDILVNW------AVQIARGMNYLHCEAIVPVIHRDLKSSNIL 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 253 LFEDFK--------AKIADFNLSNQspdmAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14145   140 ILEKVEngdlsnkiLKITDFGLARE----WHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVP 212
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
119-321 3.26e-28

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: 111.71  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKdGKAVAVKKL----DNAAEPES-NVEfltqvSRVSKLKHDNFVELFGY---CVEGNFRILAYEFA 190
Cdd:cd13979    11 LGSGGFGSVYKATYK-GETVAVKIVrrrrKNRASRQSfWAE-----LNAARLRHENIVRVLAAetgTDFASLGLIIMEYC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRKGVQGAQpgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ- 269
Cdd:cd13979    85 GNGTLQQLIYEGSEPLPLA--------HRILISLDIARALRFCHSH---GIVHLDVKPANILISEQGVCKLCDFGCSVKl 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 270 -SPDmAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd13979   154 gEGN-EVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELP 205
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
118-360 6.69e-28

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: 110.63  E-value: 6.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEF-LTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd08215     7 VIGKGSFGSAYLVRrKSDGKLYVLKEIDLSNMSEKEREEaLNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQGAQPGPT-LDWIqrvriaVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS---NQSP 271
Cdd:cd08215    87 AQKIKKQKKKGQPFPEEQiLDWF------VQICLALKYLHSR---KILHRDLKTQNIFLTKDGVVKLGDFGISkvlESTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 272 DMAarlhSTrVLGTFGYHAPE------YamtgqlTQKSDVYSFGVVLLELLTGRKPVDHTmprGQQSLVTwatprlsedK 345
Cdd:cd08215   158 DLA----KT-VVGTPYYLSPElcenkpY------NYKSDIWALGCVLYELCTLKHPFEAN---NLPALVY---------K 214
                         250
                  ....*....|....*
gi 1032291014 346 VkqcvdpkLKGEYPP 360
Cdd:cd08215   215 I-------VKGQYPP 222
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
118-321 3.55e-27

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: 109.24  E-value: 3.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVKKL------DNAAEPESNV--------------EFLTQVSRVSKLKHDNFVELFGYC 177
Cdd:cd14000     1 LLGDGGFGSVYRASYK-GEPVAVKIFnkhtssNFANVPADTMlrhlratdamknfrLLRQELTVLSHLHHPSIVYLLGIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 178 VEGnfRILAYEFATMGSLHDIL-HGRKgvQGAQPGPTLdwiqRVRIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLF-- 254
Cdd:cd14000    80 IHP--LMLVLELAPLGSLDHLLqQDSR--SFASLGRTL----QQRIALQVADGLRYLHSAM---IIYRDLKSHNVLVWtl 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 255 ---EDFKAKIADFNLSNQSPDMAARlhstRVLGTFGYHAPEYAMTGQL-TQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14000   149 ypnSAIIIKIADYGISRQCCRMGAK----GSEGTPGFRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGAP 215
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
119-321 3.78e-27

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: 108.69  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA-VAVKKLDNA-AEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGmVAIKCLHSSpNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHgrkgvqgaQPGPTLDWIQRVRIAVDAARGLEYLHeKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLS--NQSPDMA 274
Cdd:cd13978    81 SLLE--------REIQDVPWSLRFRIIHEIALGMNFLH-NMDPPLLHHDLKPENILLDNHFHVKISDFGLSklGMKSISA 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 275 ARLHSTRVL-GTFGYHAPEYAMTGQL--TQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd13978   152 NRRRGTENLgGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEP 201
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
119-321 6.90e-27

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: 107.75  E-value: 6.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAA-EPEsnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd05034     3 LGAGQFGEVWMGVWNGTTKVAVKTLKPGTmSPE---AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgRKGvqgaqPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqspdmaARL 277
Cdd:cd05034    80 YL--RTG-----EGRALRLPQLIDMAAQIASGMAYLESR---NYIHRDLAARNILVGENNVCKVADFGL--------ARL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 278 -----HSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05034   142 ieddeYTAREGAKFpiKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVP 193
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
109-321 1.09e-26

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: 107.94  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 109 KTDNFGSKSLIGEGSYGRAYYATL------KDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNF 182
Cdd:cd05049     3 KRDTIVLKRELGEGAFGKVFLGECynlepeQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 183 RILAYEFATMGSLHDIL--HGRKGVQGAQPGPT---LDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd05049    83 LLMVFEYMEHGDLNKFLrsHGPDAAFLASEDSApgeLTLSQLLHIAVQIASGMVYLASQ---HFVHRDLATRNCLVGTNL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 258 KAKIADFNLSNQspdmaarLHST---RVLGT----FGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05049   160 VVKIGDFGMSRD-------IYSTdyyRVGGHtmlpIRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQP 224
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
119-323 1.17e-26

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 108.00  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATlKDGKAVAVKKL--DNAAEPESNVEFL-TQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd14157     1 ISEGTFADIYKGY-RHGKQYVIKRLkeTECESPKSTERFFqTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAA 275
Cdd:cd14157    80 QDRLQQQGGSH------PLPWEQRLSISLGLLKAVQHLHNF---GILHGNIKSSNVLLDGNLLPKLGHSGLRLCPVDKKS 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 276 R--LHSTRVLGTFGYHAPE-YAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14157   151 VytMMKTKVLQISLAYLPEdFVRHGQLTEKVDIFSCGVVLAEILTGIKAMD 201
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
119-396 1.29e-26

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: 107.18  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVefLTQVSRVSKLKHDNFVELFGYCV-EGNFRILAyEFATMGSLHD 197
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANM--LREVQLMNRLSHPNILRFMGVCVhQGQLHALT-EYINGGNLEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFED---FKAKIADFNLSNQSPDMA 274
Cdd:cd14155    78 LLDSNE---------PLSWTVRVKLALDIARGLSYLHSK---GIFHRDLTSKNCLIKRDengYTAVVGDFGLAEKIPDYS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 275 ARLHSTRVLGTFGYHAPEyAMTGQL-TQKSDVYSFGVVLLELLtGRKPVD-HTMPRGQQSLVTWATPRlsedkvkqcvdp 352
Cdd:cd14155   146 DGKEKLAVVGSPYWMAPE-VLRGEPyNEKADVFSYGIILCEII-ARIQADpDYLPRTEDFGLDYDAFQ------------ 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1032291014 353 KLKGEYPPkavaKLAAVAALCVQYESEFRPNMSIVVKALQPLLR 396
Cdd:cd14155   212 HMVGDCPP----DFLQLAFNCCNMDPKSRPSFHDIVKTLEEILE 251
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
119-394 1.44e-26

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 107.66  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVE-FLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd14160     1 IGEGEIFEVYRVRIGNrSYAVKLFKQEKKMQWKKHWKrFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGrkgVQGAQPgptLDWIQRVRIAVDAARGLEYLHeKVQP-AVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAA 275
Cdd:cd14160    81 DRLQC---HGVTKP---LSWHERINILIGIAKAIHYLH-NSQPcTVICGNISSANILLDDQMQPKLTDFALAHFRPHLED 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 276 RlHSTRVLGT-----FGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPV----DHTMPRGQqslvtwatprLSEDKV 346
Cdd:cd14160   154 Q-SCTINMTTalhkhLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCKVVlddpKHLQLRDL----------LHELME 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 347 KQCVDPKLK------GEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPL 394
Cdd:cd14160   223 KRGLDSCLSfldlkfPPCPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRLEST 276
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
119-321 3.00e-26

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: 105.65  E-value: 3.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKdGKAVAVKKLDNAAEpesnveflTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14059     1 LGSGAQGAVFLGKFR-GEEVAVKKVRDEKE--------TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHgrkgvQGAQPGPTL--DWIQRVriavdaARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd14059    72 LR-----AGREITPSLlvDWSKQI------ASGMNYLH---LHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTK 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1032291014 277 LHSTrvlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14059   138 MSFA---GTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIP 179
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
118-321 4.70e-26

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: 105.38  E-value: 4.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd06627     7 LIGRGAFGSVYKGlNLNTGEFVAIKQISLEKIPKSDLKSVMGeIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGrkgvQGAQPGPTLDW-IQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd06627    87 ASIIKK----FGKFPESLVAVyIYQV------LEGLAYLHEQ---GVIHRDIKGANILTTKDGLVKLADFGVATKLNEVE 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 275 ARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06627   154 KDENS--VVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPP 198
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
116-321 7.08e-26

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: 105.50  E-value: 7.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKdGKAVAVK--KLDNAAEPESNVEFLTQVSRV-SKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd14147     8 EEVIGIGGFGKVYRGSWR-GELVAVKaaRQDPDEDISVTAESVRQEARLfAMLAHPNIIALKAVCLEEPNLCLVMEYAAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKgvqgAQPGPTLDWiqrvriAVDAARGLEYLHEKVQPAVIHRDIRSSNVLL--------FEDFKAKIADF 264
Cdd:cd14147    87 GPLSRALAGRR----VPPHVLVNW------AVQIARGMHYLHCEALVPVIHRDLKSNNILLlqpienddMEHKTLKITDF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 265 NLsnqspdmAARLHSTRVL---GTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14147   157 GL-------AREWHKTTQMsaaGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVP 209
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
119-323 7.89e-26

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: 104.80  E-value: 7.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLD----NAAEPEsnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd08529     8 LGKGSFGVVYKVVRKvDGRVYALKQIDisrmSRKMRE---EAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHgrkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS---NQS 270
Cdd:cd08529    85 DLHSLIK-------SQRGRPLPEDQIWKFFIQTLLGLSHLHSK---KILHRDIKSMNIFLDKGDNVKIGDLGVAkilSDT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 271 PDMAarlhSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd08529   155 TNFA----QT-IVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFE 202
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
119-328 8.30e-26

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: 104.88  E-value: 8.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNaaEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELK--RFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LhgrkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFE---DFKAKIADFNLSNQSPDMAA 275
Cdd:cd14065    79 L--------KSMDEQLPWSQRVSLAKDIASGMAYLHSK---NIIHRDLNSKNCLVREanrGRNAVVADFGLAREMPDEKT 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 276 ----RLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLtGRKPVD-HTMPR 328
Cdd:cd14065   148 kkpdRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVPADpDYLPR 204
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
117-317 1.15e-25

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: 105.16  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYATL-----KDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRI--LAYEF 189
Cdd:cd05038    10 KQLGEGHFGSVELCRYdplgdNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRRSlrLIMEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ 269
Cdd:cd05038    90 LPSGSLRDYLQRHR--------DQIDLKRLLLFASQICKGMEYLGSQ---RYIHRDLAARNILVESEDLVKISDFGLAKV 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 270 SP--DMAARLHSTRVLGTFGYhAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05038   159 LPedKEYYYVKEPGESPIFWY-APECLRESRFSSASDVWSFGVTLYELFT 207
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
118-391 1.18e-25

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: 104.32  E-value: 1.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd05085     3 LLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmaaRL 277
Cdd:cd05085    83 FLRKKKD--------ELKTKQLVKFSLDAAAGMAYLESK---NCIHRDLAARNCLVGENNALKISDFGMSRQEDD---GV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 278 HSTRVLGT--FGYHAPEYAMTGQLTQKSDVYSFGVVLLELLtgrkpvdhtmprgqqSLVTWATPRLSEDKVKQCVDPKLK 355
Cdd:cd05085   149 YSSSGLKQipIKWTAPEALNYGRYSSESDVWSFGILLWETF---------------SLGVCPYPGMTNQQAREQVEKGYR 213
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1032291014 356 GEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKAL 391
Cdd:cd05085   214 MSAPQRCPEDIYKIMQRCWDYNPENRPKFSELQKEL 249
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
118-355 2.86e-25

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: 103.50  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLDNAaepESNVEFLTQVSRVSKLKHDNFVELFG-YCVEGNFRILAyEFATMGSL 195
Cdd:cd06612    10 KLGEGSYGSVYKAIHKEtGQVVAIKVVPVE---EDLQEIIKEISILKQCDSPYIVKYYGsYFKNTDLWIVM-EYCGAGSV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRkgvqgaqpGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAA 275
Cdd:cd06612    86 SDIMKIT--------NKTLTEEEIAAILYQTLKGLEYLHSN---KKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 276 RLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP-RGQQSLVTWATPRLSE---------DK 345
Cdd:cd06612   155 KRNT--VIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPmRAIFMIPNKPPPTLSDpekwspefnDF 232
                         250
                  ....*....|..
gi 1032291014 346 VKQC--VDPKLK 355
Cdd:cd06612   233 VKKClvKDPEER 244
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
119-321 4.27e-25

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 103.61  E-value: 4.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATL----KDGKA--VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05048    13 LGEGAFGKVYKGELlgpsSEESAisVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMAH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDIL-----HGRKGVQGAQPGP--TLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd05048    93 GDLHEFLvrhspHSDVGVSSDDDGTasSLDQSDFLHIAIQIAAGMEYLSSH---HYVHRDLAARNCLVGDGLTVKISDFG 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 266 LSNQ--SPDMaARLHSTRVLgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05048   170 LSRDiySSDY-YRVQSKSLL-PVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQP 226
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
119-321 5.52e-25

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 102.30  E-value: 5.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLD-NAAEPESnveFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLHD 197
Cdd:cd14203     3 LGQGCFGEVWMGTWNGTTKVAIKTLKpGTMSPEA---FLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVT-EFMSKGSLLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKGVQGAQPgptldwiQRVRIAVDAARGLEYLhEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAarl 277
Cdd:cd14203    79 FLKDGEGKYLKLP-------QLVDMAAQIASGMAYI-ERMN--YIHRDLRAANILVGDNLVCKIADFGLARLIEDNE--- 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 278 HSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd14203   146 YTARQGAKFpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVP 192
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
119-321 5.82e-25

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 102.55  E-value: 5.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEflTQVSR----VSKLKHDNFVELFGYcVEGNFRI-LAYEFATM 192
Cdd:cd14007     8 LGKGKFGNVYLAREKKsGFIVALKVISKSQLQKSGLE--HQLRReieiQSHLRHPNILRLYGY-FEDKKRIyLILEYAPN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPd 272
Cdd:cd14007    85 GELYKELKKQK---------RFDEKEAAKYIYQLALALDYLHSK---NIIHRDIKPENILLGSNGELKLADFGWSVHAP- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 273 maarlHSTR--VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14007   152 -----SNRRktFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPP 197
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
119-392 3.99e-24

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: 100.33  E-value: 3.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGrAYYATLKDGKAVAVK--KLDNAAEpesnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLH 196
Cdd:cd05083    14 IGEGEFG-AVLQGEYMGQKVAVKniKCDVTAQ-----AFLEETAVMTKLQHKNLVRLLGVILHNGLYIVM-ELMSKGNLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRkgvqGAQPGPTldwIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPdMAAR 276
Cdd:cd05083    87 NFLRSR----GRALVPV---IQLLQFSLDVAEGMEYLESK---KLVHRDLAARNILVSEDGVAKISDFGLAKVGS-MGVD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 277 LHSTRVLGTfgyhAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVdhtmprgqqslvtwatPRLSEDKVKQCVDPKLK 355
Cdd:cd05083   156 NSRLPVKWT----APEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY----------------PKMSVKEVKEAVEKGYR 215
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1032291014 356 GEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQ 392
Cdd:cd05083   216 MEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
119-321 4.73e-24

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: 100.12  E-value: 4.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYG---RAYYATlKDGK--AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFrILAYEFATMG 193
Cdd:cd05060     3 LGHGNFGsvrKGVYLM-KSGKevEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPL-MLVMELAPLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGVQGAQpgpTLDWIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNqspdm 273
Cdd:cd05060    81 PLLKYLKKRREIPVSD---LKELAHQV------AMGMAYLESK---HFVHRDLAARNVLLVNRHQAKISDFGMSR----- 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 274 AARLHSTRVLGTFG------YHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05060   144 ALGAGSDYYRATTAgrwplkWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKP 198
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
119-328 6.23e-24

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: 100.27  E-value: 6.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEpESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd14154     1 LGKGFFGQAIKVTHREtGEVMVMKELIRFDE-EAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRkgvqgAQPGPtldWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN-------QS 270
Cdd:cd14154    80 VLKDM-----ARPLP---WAQRVRFAKDIASGMAYLHSM---NIIHRDLNSHNCLVREDKTVVVADFGLARliveerlPS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 271 PDMAA--RLHSTR---------VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLtGRKPVD-HTMPR 328
Cdd:cd14154   149 GNMSPseTLRHLKspdrkkrytVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII-GRVEADpDYLPR 217
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
118-326 7.83e-24

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: 100.09  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDgKAVAVKKLdNAAEPESnveFLTQ--VSRVSKLKHDNFVELFGYCVEGNFRILAY----EFAT 191
Cdd:cd14053     2 IKARGRFGAVWKAQYLN-RLVAVKIF-PLQEKQS---WLTEreIYSLPGMKHENILQFIGAEKHGESLEAEYwlitEFHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKV-------QPAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd14053    77 RGSLCDYLKGN----------VISWNELCKIAESMARGLAYLHEDIpatngghKPSIAHRDFKSKNVLLKSDLTACIADF 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 265 NLSNQ-SPDMAARLHSTRVlGTFGYHAPEyAMTG--QLTQKS----DVYSFGVVLLELLT----GRKPVDHTM 326
Cdd:cd14053   147 GLALKfEPGKSCGDTHGQV-GTRRYMAPE-VLEGaiNFTRDAflriDMYAMGLVLWELLSrcsvHDGPVDEYQ 217
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
117-323 9.32e-24

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 99.13  E-value: 9.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSK-LKHDNFVELFG-YCVEGNFrILAYEFATMG 193
Cdd:cd14003     6 KTLGEGSFGKVKLARhKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKlLNHPNIIKLYEvIETENKI-YLVMEYASGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILhgrkgvqgaqpgptldwIQRVRIAVDAAR--------GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd14003    85 ELFDYI-----------------VNNGRLSEDEARrffqqlisAVDYCHSN---GIVHRDLKLENILLDKNGNLKIIDFG 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 266 LSNQSpdMAARLHSTRVlGTFGYHAPE-YAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14003   145 LSNEF--RGGSLLKTFC-GTPAYAAPEvLLGRKYDGPKADVWSLGVILYAMLTGYLPFD 200
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
119-355 1.43e-23

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: 98.82  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVefLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06614     8 IGEGASGEVYKATdRATGKEVAIKKMRLRKQNKELI--INEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGSLTD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqspdmAARL 277
Cdd:cd06614    86 II--------TQNPVRMNESQIAYVCREVLQGLEYLHSQ---NVIHRDIKSDNILLSKDGSVKLADFGF-------AAQL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 278 ---HSTR--VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP-VDHTMPRGQQSLVTWATPRLSE-------- 343
Cdd:cd06614   148 tkeKSKRnsVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPyLEEPPLRALFLITTKGIPPLKNpekwspef 227
                         250
                  ....*....|....*
gi 1032291014 344 -DKVKQC--VDPKLK 355
Cdd:cd06614   228 kDFLNKClvKDPEKR 242
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
117-321 2.42e-23

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: 98.05  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFG-YCVEGNFRIlAYEFATMGS 194
Cdd:cd06623     7 KVLGQGSSGVVYKVRHKpTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGaFYKEGEISI-VLEYMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGVqgaqPGPTLdwiqrVRIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd06623    86 LADLLKKVGKI----PEPVL-----AYIARQILKGLDYLHTKRH--IIHRDIKPSNLLINSKGEVKIADFGISKVLENTL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 275 ARlHSTRVlGTFGYHAPE------YAMtgqltqKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06623   155 DQ-CNTFV-GTVTYMSPEriqgesYSY------AADIWSLGLTLLECALGKFP 199
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
119-318 2.46e-23

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: 97.90  E-value: 2.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA-VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTeVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgRKgvqgaqPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARL 277
Cdd:cd05041    83 FL--RK------KGARLTVKQLLQMCLDAAAGMEYLESK---NCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTV 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1032291014 278 HSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTG 318
Cdd:cd05041   152 SDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSL 192
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
119-327 2.79e-23

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: 98.20  E-value: 2.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06610     9 IGSGATAVVYAAyCLPKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHgRKGVQGAQPGPTLDWIQRvriavDAARGLEYLHEKVQpavIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARL 277
Cdd:cd06610    89 IMK-SSYPRGGLDEAIIATVLK-----EVLKGLEYLHSNGQ---IHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRT 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 278 HSTR--VLGTFGYHAPEyAMTGQ--LTQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd06610   160 RKVRktFVGTPCWMAPE-VMEQVrgYDFKADIWSFGITAIELATGAAPYSKYPP 212
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
100-355 3.74e-23

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: 97.74  E-value: 3.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 100 ALSLDELKektdnfgSKSLIGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESnveFLTQVSRVSKLKHDNFVELFGYCVE 179
Cdd:cd05082     2 ALNMKELK-------LLQTIGKGEFGDVMLGDYR-GNKVAVKCIKNDATAQA---FLAEASVMTQLRHSNLVQLLGVIVE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 180 GNFRI-LAYEFATMGSLHDILHGR-KGVQGaqpGPTLdwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd05082    71 EKGGLyIVTEYMAKGSLVDYLRSRgRSVLG---GDCL-----LKFSLDVCEAMEYLEGN---NFVHRDLAARNVLVSEDN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 258 KAKIADFNLSNQspdmAARLHSTRVLgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT------GRKPVDHTMPR--- 328
Cdd:cd05082   140 VAKVSDFGLTKE----ASSTQDTGKL-PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfgrvpyPRIPLKDVVPRvek 214
                         250       260
                  ....*....|....*....|....*....
gi 1032291014 329 GQQSLVTWATPRLSEDKVKQC--VDPKLK 355
Cdd:cd05082   215 GYKMDAPDGCPPAVYDVMKNCwhLDAAMR 243
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
119-321 5.77e-23

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: 97.73  E-value: 5.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATL------KDGKAVAVKKLDNAAEpESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05092    13 LGEGAFGKVFLAEChnllpeQDKMLVAVKALKEATE-SARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDIL--HGR-----KGVQGAQPGPtLDWIQRVRIAVDAARGLEYLhekVQPAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd05092    92 GDLNRFLrsHGPdakilDGGEGQAPGQ-LTLGQMLQIASQIASGMVYL---ASLHFVHRDLATRNCLVGQGLVVKIGDFG 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 266 LSNQspdmaarLHST-------RVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05092   168 MSRD-------IYSTdyyrvggRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQP 224
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
117-343 7.23e-23

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: 97.41  E-value: 7.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYATLKDGKAVAVKKLDNAAePESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLH 196
Cdd:cd14149    18 TRIGSGSFGTVYKGKWHGDVAVKILKVVDPT-PEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVT-QWCEGSSLY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHgrkgVQGAQpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd14149    96 KHLH----VQETK----FQMFQLIDIARQTAQGMDYLHAK---NIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGS 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 277 LHSTRVLGTFGYHAPEYAM---TGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVT---WATPRLSE 343
Cdd:cd14149   165 QQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVgrgYASPDLSK 237
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
119-321 1.18e-22

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: 96.22  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVK--KLdnaaEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd06613     8 IGSGTYGDVYKArNIATGELAAVKviKL----EPGDDFEIIQQeISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGGGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHgrkgVQGAQPGPTLDWIQRvriavDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ-SPDM 273
Cdd:cd06613    84 LQDIYQ----VTGPLSELQIAYVCR-----ETLKGLAYLHST---GKIHRDIKGANILLTEDGDVKLADFGVSAQlTATI 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 274 AARlhsTRVLGTFGYHAPEYA---MTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06613   152 AKR---KSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPP 199
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
119-397 1.33e-22

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: 96.24  E-value: 1.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAePESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLHDI 198
Cdd:cd14150     8 IGTGSFGTVFRGKWHGDVAVKILKVTEPT-PEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIIT-QWCEGSSLYRH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLH 278
Cdd:cd14150    86 LHVTE--------TRFDTMQLIDVARQTAQGMDYLHAK---NIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 STRVLGTFGYHAPEYAM---TGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVT---WATPRLSedkvkqcvdp 352
Cdd:cd14150   155 VEQPSGSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVgrgYLSPDLS---------- 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1032291014 353 KLKGEYPpkavAKLAAVAALCVQYESEFRPNMSIVVKALQPLLRS 397
Cdd:cd14150   225 KLSSNCP----KAMKRLLIDCLKFKREERPLFPQILVSIELLQRL 265
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
119-317 1.86e-22

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: 95.58  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd05148    14 LGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQ-DFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLLAF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKGvQGAQPGPTLDwiqrvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLH 278
Cdd:cd05148    93 LRSPEG-QVLPVASLID------MACQVAEGMAYLEEQ---NSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYLSS 162
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1032291014 279 STRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05148   163 DKKI--PYKWTAPEAASHGTFSTKSDVWSFGILLYEMFT 199
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
112-321 2.10e-22

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: 95.54  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLD----NAAEPESNVeflTQVSRVSKLKHDNFVELFGYCVEGNFRILA 186
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKrLSDNQVYALKEVNlgslSQKEREDSV---NEIRLLASVNHPNIIRYKEAFLDGNRLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLHDILhgRKGVQGAQPGPTLD-WiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd08530    78 MEYAPFGDLSKLI--SKRKKKRRLFPEDDiW----RIFIQMLRGLKALHDQ---KILHRDLKSANILLSAGDLVKIGDLG 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 266 LSNQSPDMAARlhstRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd08530   149 ISKVLKKNLAK----TQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPP 200
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
118-323 2.43e-22

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: 95.48  E-value: 2.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd14069     8 TLGEGAFGEVFLAvNRNTEEAVAVKFVDMKRAPGDCPENIKKeVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGV--QGAQpgptlDWIQRVrIAvdaarGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ-SPD 272
Cdd:cd14069    88 FDKIEPDVGMpeDVAQ-----FYFQQL-MA-----GLKYLHSC---GITHRDIKPENLLLDENDNLKISDFGLATVfRYK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 273 MAARLhSTRVLGTFGYHAPEyaMTGQLT---QKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14069   154 GKERL-LNKMCGTLPYVAPE--LLAKKKyraEPVDVWSCGIVLFAMLAGELPWD 204
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
118-317 2.52e-22

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: 95.85  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYG---RAYYATLKD--GKAVAVKKLDNAAEpESNVEFLTQVSRVSKLKHDNFVELFGYCVEG---NFRiLAYEF 189
Cdd:cd14205    11 QLGKGNFGsveMCRYDPLQDntGEVVAVKKLQHSTE-EHLRDFEREIEILKSLQHDNIVKYKGVCYSAgrrNLR-LIMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ 269
Cdd:cd14205    89 LPYGSLRDYLQKHK--------ERIDHIKLLQYTSQICKGMEYLGTK---RYIHRDLATRNILVENENRVKIGDFGLTKV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 270 SPDmAARLHSTRVLGT--FGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd14205   158 LPQ-DKEYYKVKEPGEspIFWYAPESLTESKFSVASDVWSFGVVLYELFT 206
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
119-392 2.88e-22

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: 95.00  E-value: 2.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd05084     4 IGRGNFGEVFSGRLRaDNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRkgvqgaqpGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARL 277
Cdd:cd05084    84 FLRTE--------GPRLKVKELIRMVENAAAGMEYLESK---HCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVYAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 278 HSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTgRKPVDHTMPRGQQSlvtwatprlsedkvKQCVDPKLKGE 357
Cdd:cd05084   153 TGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFS-LGAVPYANLSNQQT--------------REAVEQGVRLP 217
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1032291014 358 YPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQ 392
Cdd:cd05084   218 CPENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDLQ 252
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
118-317 3.22e-22

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: 95.95  E-value: 3.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-------GKAVAVKKL-DNAAEPEsnveFLTQVSRVSKLK----HDNFVELFGYCVEGNFRIL 185
Cdd:cd05053    19 PLGEGAFGQVVKAEAVGldnkpneVVTVAVKMLkDDATEKD----LSDLVSEMEMMKmigkHKNIINLLGACTQDGPLYV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILHGR-------KGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK 258
Cdd:cd05053    95 VVEYASKGNLREFLRARrppgeeaSPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASK---KCIHRDLAARNVLVTEDNV 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 259 AKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05053   172 MKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT 230
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
119-321 3.52e-22

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: 94.72  E-value: 3.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYG---RAYYATlKDGKA--VAVKKL--DNAAEPESNVEFLTQVSRVSKLKHDNFVELFGyCVEGNFRILAYEFAT 191
Cdd:cd05040     3 LGDGSFGvvrRGEWTT-PSGKViqVAVKCLksDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYG-VVLSSPLMMVTELAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRkgvQGAQPGPTL-DWiqrvriAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQS 270
Cdd:cd05040    81 LGSLLDRLRKD---QGHFLISTLcDY------AVQIANGMAYLESK---RFIHRDLAARNILLASKDKVKIGDFGLMRAL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 271 PD------MAARLhstRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05040   149 PQnedhyvMQEHR---KV--PFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEP 201
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
118-317 5.95e-22

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 94.72  E-value: 5.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGK--AVAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd05047     2 VIGEGNFGQVLKARIKkDGLrmDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKgVQGAQPG--------PTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd05047    82 NLLDFLRKSR-VLETDPAfaianstaSTLSSQQLLHFAADVARGMDYLSQK---QFIHRDLAARNILVGENYVAKIADFG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 266 LSnqspdmaaRLHSTRVLGTFG-----YHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05047   158 LS--------RGQEVYVKKTMGrlpvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 206
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
118-392 1.02e-21

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 93.64  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD------GKA-VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFA 190
Cdd:cd05044     2 FLGSGAFGEVFEGTAKDilgdgsGETkVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILhgRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFE----DFKAKIADFNL 266
Cdd:cd05044    82 EGGDLLSYL--RAARPTAFTPPLLTLKDLLSICVDVAKGCVYLEDM---HFVHRDLAARNCLVSSkdyrERVVKIGDFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 267 SNQ--SPDM----AARLHSTRvlgtfgYHAPEYAMTGQLTQKSDVYSFGVVLLELLTgrkpvdhtmpRGQQSLvtwatPR 340
Cdd:cd05044   157 ARDiyKNDYyrkeGEGLLPVR------WMAPESLVDGVFTTQSDVWAFGVLMWEILT----------LGQQPY-----PA 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 341 LSEDKVKQCVDPKLKGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQ 392
Cdd:cd05044   216 RNNLEVLHFVRAGGRLDQPDNCPDDLYELMLRCWSTDPEERPSFARILEQLQ 267
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
116-321 1.28e-21

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: 93.63  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKDGKAVAVKKLDN-AAEPEsnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd05068    13 LRKLGSGQFGEVWEGLWNNTTPVAVKTLKPgTMDPE---DFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqspdma 274
Cdd:cd05068    90 LLEYLQGKGR--------SLQLPQLIDMAAQVASGMAYLESQ---NYIHRDLAARNVLVGENNICKVADFGL-------- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 275 ARL------HSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05068   151 ARVikvedeYEAREGAKFpiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIP 206
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
119-391 1.31e-21

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 93.28  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd05059    12 LGSGQFGVVHLGKWRGKIDVAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLLNY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKGVQGAQpgptldWIqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMaarlH 278
Cdd:cd05059    90 LRERRGKFQTE------QL--LEMCKDVCEAMEYLESN---GFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDD----E 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 STRVLGT---FGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKpvdhtMPrgqqslvtwaTPRLSEDKVKQCVDPKLK 355
Cdd:cd05059   155 YTSSVGTkfpVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGK-----MP----------YERFSNSEVVEHISQGYR 219
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1032291014 356 GEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKAL 391
Cdd:cd05059   220 LYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
119-359 1.34e-21

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: 93.56  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYC-VEGNFRIlAYEFATMGSLH 196
Cdd:cd06605     9 LGEGNGGVVSKVRHRpSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFySEGDISI-CMEYMDGGSLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILhgrKGVqGAQPGPTLDwiqrvRIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd06605    88 KIL---KEV-GRIPERILG-----KIAVAVVKGLIYLHEKHK--IIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSLAK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 277 lhsTRVlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP------VDHTMPRGQ-QSLVTWATPRLSEDK---- 345
Cdd:cd06605   157 ---TFV-GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPypppnaKPSMMIFELlSYIVDEPPPLLPSGKfspd 232
                         250       260
                  ....*....|....*....|
gi 1032291014 346 ----VKQCV--DPKLKGEYP 359
Cdd:cd06605   233 fqdfVSQCLqkDPTERPSYK 252
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
109-398 1.42e-21

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: 93.95  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 109 KTDNFGSKSLIGEGSYGRAYYATL------KDGKAVAVKKLDNAAEpESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNF 182
Cdd:cd05093     3 KRHNIVLKRELGEGAFGKVFLAECynlcpeQDKILVAVKTLKDASD-NARKDFHREAELLTNLQHEHIVKFYGVCVEGDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 183 RILAYEFATMGSLHDIL--HGRKGVQGA--QPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK 258
Cdd:cd05093    82 LIMVFEYMKHGDLNKFLraHGPDAVLMAegNRPAELTQSQMLHIAQQIAAGMVYLASQ---HFVHRDLATRNCLVGENLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 259 AKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPvdhtmprgqqslvtWA 337
Cdd:cd05093   159 VKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQP--------------WY 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 338 tpRLSEDKVKQCVDPKLKGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLRSS 398
Cdd:cd05093   225 --QLSNNEVIECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKAS 283
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
117-327 1.42e-21

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: 93.97  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYATLkDGKAVAVKkldnaAEPESNVEFLT---QVSRVSKLKHDNFVELFGYCVEGNFR-----ILAYE 188
Cdd:cd14054     1 QLIGQGRYGTVWKGSL-DERPVAVK-----VFPARHRQNFQnekDIYELPLMEHSNILRFIGADERPTADgrmeyLLVLE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKVQ------PAVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd14054    75 YAPKGSLCSYLREN----------TLDWMSSCRMALSLTRGLAYLHTDLRrgdqykPAIAHRDLNSRNVLVKADGSCVIC 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 263 DFNLSNQSPDM--------AARLHSTRVLGTFGYHAPEyAMTGQLT--------QKSDVYSFGVVLLELLT-------GR 319
Cdd:cd14054   145 DFGLAMVLRGSslvrgrpgAAENASISEVGTLRYMAPE-VLEGAVNlrdcesalKQVDVYALGLVLWEIAMrcsdlypGE 223

                  ....*...
gi 1032291014 320 KPVDHTMP 327
Cdd:cd14054   224 SVPPYQMP 231
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
119-321 1.47e-21

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: 93.60  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLD-NAAEPESnveFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLHD 197
Cdd:cd05069    20 LGQGCFGEVWMGTWNGTTKVAIKTLKpGTMMPEA---FLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVT-EFMGKGSLLD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgRKGvqgaqPGPTLDWIQRVRIAVDAARGLEYLhEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAarl 277
Cdd:cd05069    96 FL--KEG-----DGKYLKLPQLVDMAAQIADGMAYI-ERMN--YIHRDLRAANILVGDNLVCKIADFGLARLIEDNE--- 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 278 HSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05069   163 YTARQGAKFpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVP 209
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
118-315 1.64e-21

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: 93.66  E-value: 1.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHDNfveLFGYCVEGNFRI-------LAYEFA 190
Cdd:cd13998     2 VIGKGRFGEVWKASLK-NEPVAVKIFSSRDKQSWFRE--KEIYRTPMLKHEN---ILQFIAADERDTalrtelwLVTAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKV------QPAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd13998    76 PNGSL*DYLSLH----------TIDWVSLCRLALSVARGLAHLHSEIpgctqgKPAIAHRDLKSKNILVKNDGTCCIADF 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 265 NL------SNQSPDMAArlhSTRVlGTFGYHAPEY---AMTGQLTQ---KSDVYSFGVVLLEL 315
Cdd:cd13998   146 GLavrlspSTGEEDNAN---NGQV-GTKRYMAPEVlegAINLRDFEsfkRVDIYAMGLVLWEM 204
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
119-323 1.65e-21

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: 93.63  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGK----AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVeGNFRILAYEFATMG 193
Cdd:cd05057    15 LGSGAFGTVYKGVWIpEGEkvkiPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICL-SSQVQLITQLMPLG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGVQGAQPgpTLDWiqrvriAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDM 273
Cdd:cd05057    94 CLLDYVRNHRDNIGSQL--LLNW------CVQIAKGMSYLEEK---RLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 274 AARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVD 323
Cdd:cd05057   163 EKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYE 213
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
119-319 1.68e-21

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: 93.78  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPE-SNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFR------ILAYEFA 190
Cdd:cd07840     7 IGEGTYGQVYKArNKKTGELVALKKIRMENEKEgFPITAIREIKLLQKLDHPNVVRLKEIVTSKGSAkykgsiYMVFEYM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TmgslHDI--LHGRKGVQGAQPgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN 268
Cdd:cd07840    87 D----HDLtgLLDNPEVKFTES-------QIKCYMKQLLEGLQYLHSN---GILHRDIKGSNILINNDGVLKLADFGLAR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 269 Q-SPDMAARLhSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07840   153 PyTKENNADY-TNRVI-TLWYRPPELLLgATRYGPEVDMWSVGCILAELFTGK 203
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
119-344 1.83e-21

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: 93.44  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA-VAVK--KLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd14026     5 LSRGAFGTVSRARHADWRVtVAIKclKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVqgaqpgPTLDWIQRVRIAVDAARGLEYLHeKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAA 275
Cdd:cd14026    85 NELLHEKDIY------PDVAWPLRLRILYEIALGVNYLH-NMSPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSIS 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 276 RLHSTRVL---GTFGYHAPEYAMTGQLTQ---KSDVYSFGVVLLELLTGRKPVDHTMPRGQ--QSLVTWATPRLSED 344
Cdd:cd14026   158 QSRSSKSApegGTIIYMPPEEYEPSQKRRasvKHDIYSYAIIMWEVLSRKIPFEEVTNPLQimYSVSQGHRPDTGED 234
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
119-397 2.11e-21

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: 93.20  E-value: 2.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAtlKDGKAVAVKKLD-NAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLHD 197
Cdd:cd14151    16 IGSGSFGTVYKG--KWHGDVAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVT-QWCEGSSLYH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARL 277
Cdd:cd14151    93 HLHIIE--------TKFEMIKLIDIARQTAQGMDYLHAK---SIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 278 HSTRVLGTFGYHAPEYAM---TGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVT---WATPRLSedKVKQCVD 351
Cdd:cd14151   162 QFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVgrgYLSPDLS--KVRSNCP 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1032291014 352 PKLKgeyppkavaklaAVAALCVQYESEFRPNMSIVVKALQPLLRS 397
Cdd:cd14151   240 KAMK------------RLMAECLKKKRDERPLFPQILASIELLARS 273
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
114-328 2.37e-21

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: 92.84  E-value: 2.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 114 GSKSLIGEGSYGRayYATLKDGKAVAVKKLDNAAEPESNVefLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd13992     6 GASSHTGEPKYVK--KVGVYGGRTVAIKHITFSRTEKRTI--LQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILhgrkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEkvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSN----- 268
Cdd:cd13992    82 SLQDVL--------LNREIKMDWMFKSSFIKDIVKGMNYLHS--SSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNlleeq 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 269 ---QSPDMAARlhsTRVLgtfgYHAPE----YAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPR 328
Cdd:cd13992   152 tnhQLDEDAQH---KKLL----WTAPEllrgSLLEVRGTQKGDVYSFAIILYEILFRSDPFALEREV 211
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
119-321 2.56e-21

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: 92.83  E-value: 2.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLD-NAAEPESnveFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLHD 197
Cdd:cd05071    17 LGQGCFGEVWMGTWNGTTRVAIKTLKpGTMSPEA---FLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVT-EYMSKGSLLD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGrkgvqgaQPGPTLDWIQRVRIAVDAARGLEYLhEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAarl 277
Cdd:cd05071    93 FLKG-------EMGKYLRLPQLVDMAAQIASGMAYV-ERMN--YVHRDLRAANILVGENLVCKVADFGLARLIEDNE--- 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 278 HSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05071   160 YTARQGAKFpiKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVP 206
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
116-317 2.58e-21

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 93.14  E-value: 2.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLK-DGKAV--AVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFRILAYEFAT 191
Cdd:cd05089     7 EDVIGEGNFGQVIKAMIKkDGLKMnaAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAIEYAP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKgVQGAQP--------GPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd05089    87 YGNLLDFLRKSR-VLETDPafakehgtASTLTSQQLLQFASDVAKGMQYLSEK---QFIHRDLAARNVLVGENLVSKIAD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 264 FNLSNqspdmAARLHSTRVLGTFG--YHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05089   163 FGLSR-----GEEVYVKKTMGRLPvrWMAIESLNYSVYTTKSDVWSFGVLLWEIVS 213
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
118-318 3.32e-21

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 91.94  E-value: 3.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVKKLDNaaepESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGnfRILAYEFATMGSLH 196
Cdd:cd14068     1 LLGDGGFGSVYRAVYR-GEDVAVKIFNK----HTSFRLLRQeLVVLSHLHHPSLVALLAAGTAP--RMLVMELAPKGSLD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFK-----AKIADFNLSNQSP 271
Cdd:cd14068    74 ALLQQDNA--------SLTRTLQHRIALHVADGLRYLHSAM---IIYRDLKPHNVLLFTLYPncaiiAKIADYGIAQYCC 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 272 DMAARLHStrvlGTFGYHAPEYAMTGQL-TQKSDVYSFGVVLLELLTG 318
Cdd:cd14068   143 RMGIKTSE----GTPGFRAPEVARGNVIyNQQADVYSFGLLLYDILTC 186
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
119-324 3.38e-21

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 91.94  E-value: 3.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd05112    12 IGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEE--DFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKGVQGAQpgpTLdwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN-QSPDMAARL 277
Cdd:cd05112    90 LRTQRGLFSAE---TL-----LGMCLDVCEGMAYLEEA---SVIHRDLAARNCLVGENQVVKVSDFGMTRfVLDDQYTSS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 278 HSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVDH 324
Cdd:cd05112   159 TGTKF--PVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYEN 204
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
106-321 3.83e-21

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: 92.37  E-value: 3.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 106 LKEKTDNFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRvsKL-KHDNFVELFGYCVEGNFR 183
Cdd:cd06608     1 LPDPAGIFELVEVIGEGTYGKVYKARhKKTGQLAAIKIMDIIEDEEEEIKLEINILR--KFsNHPNIATFYGAFIKKDPP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 184 I------LAYEFATMGSLHDILHGRKGVQGAQPGPTLDWIQRvriavDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd06608    79 GgddqlwLVMEYCGGGSVTDLVKGLRKKGKRLKEEWIAYILR-----ETLRGLAYLHEN---KVIHRDIKGQNILLTEEA 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 258 KAKIADFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQ-----LTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06608   151 EVKLVDFGVSAQLDSTLGRRNT--FIGTPYWMAPEVIACDQqpdasYDARCDVWSLGITAIELADGKPP 217
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
119-321 3.86e-21

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 92.44  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLD-NAAEPESnveFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLHD 197
Cdd:cd05070    17 LGNGQFGEVWMGTWNGNTKVAIKTLKpGTMSPES---FLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVT-EYMSKGSLLD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgRKGVQGAQPGPTLdwiqrVRIAVDAARGLEYLhEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAarl 277
Cdd:cd05070    93 FL--KDGEGRALKLPNL-----VDMAAQVAAGMAYI-ERMN--YIHRDLRSANILVGNGLICKIADFGLARLIEDNE--- 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 278 HSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05070   160 YTARQGAKFpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVP 206
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
116-321 6.35e-21

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: 91.64  E-value: 6.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAEpESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd14063     5 KEVIGKGRFGRVHRGRWHGDVAIKLLNIDYLNE-EQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCKGRTL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLfEDFKAKIADFNLSNqspdMAA 275
Cdd:cd14063    84 YSLIHERK--------EKFDFNKTVQIAQQICQGMGYLHAK---GIIHKDLKSKNIFL-ENGRVVITDFGLFS----LSG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 276 RLHSTRVLGTFG-------YHAPEY--AMT------GQL--TQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14063   148 LLQPGRREDTLVipngwlcYLAPEIirALSpdldfeESLpfTKASDVYAFGTVWYELLAGRWP 210
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
119-317 6.54e-21

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: 91.64  E-value: 6.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD------GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05032    14 LGQGSFGMVYEGLAKGvvkgepETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMAK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHG-RKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS---N 268
Cdd:cd05032    94 GDLKSYLRSrRPEAENNPGLGPPTLQKFIQMAAEIADGMAYLAAK---KFVHRDLAARNCMVAEDLTVKIGDFGMTrdiY 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 269 QS----PDMAARLhSTRvlgtfgYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05032   171 ETdyyrKGGKGLL-PVR------WMAPESLKDGVFTTKSDVWSFGVVLWEMAT 216
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
111-334 7.09e-21

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: 91.72  E-value: 7.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAA-EPESNVEFLTQVSRVSKLKHDNFVELFGYCV---EGNFRIlA 186
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDpNPDVQKQILRELEINKSCASPYIVKYYGAFLdeqDSSIGI-A 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLhDILHGRKGVQGAQPGptldwiQRV--RIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd06621    80 MEYCEGGSL-DSIYKKVKKKGGRIG------EKVlgKIAESVLKGLSYLHSR---KIIHRDIKPSNILLTRKGQVKLCDF 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 265 NLSNQspdMAARLHSTRVlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDhtmPRGQQSLV 334
Cdd:cd06621   150 GVSGE---LVNSLAGTFT-GTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFP---PEGEPPLG 212
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
119-392 1.44e-20

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 90.91  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK--DGKA----VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05036    14 LGQGAFGEVYEGTVSgmPGDPsplqVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILLELMAG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDIL-HGRKGVQGAQPGPTLDWIQrvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLF---EDFKAKIADFNlsn 268
Cdd:cd05036    94 GDLKSFLrENRPRPEQPSSLTMLDLLQ---LAQDVAKGCRYLEEN---HFIHRDIAARNCLLTckgPGRVAKIGDFG--- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 269 qspdMAARLHST-------RVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRkpvdhtMP---RGQQSLVTWA 337
Cdd:cd05036   165 ----MARDIYRAdyyrkggKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGY------MPypgKSNQEVMEFV 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 338 TPRLSEDKVKQCVDPKLKgeyppkavaklaaVAALCVQYESEFRPNMSIVVKALQ 392
Cdd:cd05036   235 TSGGRMDPPKNCPGPVYR-------------IMTQCWQHIPEDRPNFSTILERLN 276
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
119-321 1.54e-20

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: 90.57  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELF-GYCVEGNFRILaYEFATMGSLHD 197
Cdd:cd06611    13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYeAYFYENKLWIL-IEFCDGGALDS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 IlhgrkgVQGAQPGPTLDWIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARL 277
Cdd:cd06611    92 I------MLELERGLTEPQIRYVCRQM--LEALNFLHSH---KVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 278 HStrVLGTFGYHAPEYAMTGQLTQ-----KSDVYSFGVVLLELLTGRKP 321
Cdd:cd06611   161 DT--FIGTPYWMAPEVVACETFKDnpydyKADIWSLGITLIELAQMEPP 207
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
119-321 2.55e-20

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: 90.07  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATL-----KDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd05090    13 LGECAFGKIYKGHLylpgmDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDIL-----HGRKGVQGAQPG---PTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd05090    93 DLHEFLimrspHSDVGCSSDEDGtvkSSLDHGDFLHIAIQIAAGMEYLSSH---FFVHKDLAARNILVGEQLHVKISDLG 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 266 LSNQ--SPDMaARLHSTRVLgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05090   170 LSREiySSDY-YRVQNKSLL-PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQP 226
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
119-351 2.57e-20

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: 89.55  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK---DGKAVAVKKLDNAAEPESNVE-FLT-QVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd14080     8 IGEGSYSKVKLAEYTksgLKEKVACKIIDKKKAPKDFLEkFLPrELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLhdilhgrkgvqgaqpgptLDWIQRvRIAVDAAR----------GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd14080    88 DL------------------LEYIQK-RGALSESQariwfrqlalAVQYLHSL---DIAHRDLKCENILLDSNNNVKLSD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 264 FNLSNQSPDMAARLHSTRVLGTFGYHAPEyAMTGQ--LTQKSDVYSFGVVLLELLTGRKPVDHT----MPRGQQSlVTWA 337
Cdd:cd14080   146 FGFARLCPDDDGDVLSKTFCGSAAYAAPE-ILQGIpyDPKKYDIWSLGVILYIMLCGSMPFDDSnikkMLKDQQN-RKVR 223
                         250
                  ....*....|....
gi 1032291014 338 TPRLSEDKVKQCVD 351
Cdd:cd14080   224 FPSSVKKLSPECKD 237
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
119-398 3.11e-20

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: 90.03  E-value: 3.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD---GKA---VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05061    14 LGQGSFGMVYEGNARDiikGEAetrVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGAQPG---PTLDwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ 269
Cdd:cd05061    94 GDLKSYLRSLRPEAENNPGrppPTLQ--EMIQMAAEIADGMAYLNAK---KFVHRDLAARNCMVAHDFTVKIGDFGMTRD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 270 SPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELltgrkpvdhtmprgqQSLVTWATPRLSEDKVKQC 349
Cdd:cd05061   169 IYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEI---------------TSLAEQPYQGLSNEQVLKF 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 350 VdpkLKGEY---PPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLRSS 398
Cdd:cd05061   234 V---MDGGYldqPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPS 282
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
119-344 3.93e-20

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


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 89.28  E-value: 3.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYG---RAYYATLKdgKAVAVKKLDNAAEPEsnvEFLT-----QVSRVSKLKHDNFVELFgYCVEGNFRI-LAYEF 189
Cdd:cd14162     8 LGHGSYAvvkKAYSTKHK--CKVAIKIVSKKKAPE---DYLQkflprEIEVIKGLKHPNLICFY-EAIETTSRVyIIMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLhdilhgrkgvqgaqpgptLDWIQRvRIAVDAAR----------GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA 259
Cdd:cd14162    82 AENGDL------------------LDYIRK-NGALPEPQarrwfrqlvaGVEYCHSK---GVVHRDLKCENLLLDKNNNL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 260 KIADFNL--SNQSPDMAARLHSTRVLGTFGYHAPEY----AMTGQLtqkSDVYSFGVVLLELLTGRKPVDHT-----MPR 328
Cdd:cd14162   140 KITDFGFarGVMKTKDGKPKLSETYCGSYAYASPEIlrgiPYDPFL---SDIWSMGVVLYTMVYGRLPFDDSnlkvlLKQ 216
                         250
                  ....*....|....*.
gi 1032291014 329 GQQSLVTWATPRLSED 344
Cdd:cd14162   217 VQRRVVFPKNPTVSEE 232
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
119-321 3.95e-20

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: 89.89  E-value: 3.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATL------KDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05050    13 IGQGAFGRVFQARApgllpyEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYMAY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGR-------------KGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA 259
Cdd:cd05050    93 GDLNEFLRHRspraqcslshstsSARKCGLNPLPLSCTEQLCIAKQVAAGMAYLSER---KFVHRDLATRNCLVGENMVV 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 260 KIADFNLSNQ--SPDMaARLHSTRVLgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05050   170 KIADFGLSRNiySADY-YKASENDAI-PIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQP 232
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
119-330 5.02e-20

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: 88.73  E-value: 5.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEfltQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd14156     1 IGSGFFSKVYKVTHGaTGKVMVVKIYKNDVDQHKIVR---EISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFED---FKAKIADFNLSNQSPDMA 274
Cdd:cd14156    78 LL--------AREELPLSWREKVELACDISRGMVYLHSK---NIYHRDLNSKNCLIRVTprgREAVVTDFGLAREVGEMP 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 275 ARLHSTR--VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLtGRKPVD-HTMPRGQ 330
Cdd:cd14156   147 ANDPERKlsLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIPADpEVLPRTG 204
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
119-321 7.06e-20

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: 88.56  E-value: 7.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLdnaaEPES-NVE-FLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd05072    15 LGAGQFGEVWMGYYNNSTKVAVKTL----KPGTmSVQaFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKGVQGAQPgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAar 276
Cdd:cd05072    91 DFLKSDEGGKVLLP-------KLIDFSAQIAEGMAYIERK---NYIHRDLRAANVLVSESLMCKIADFGLARVIEDNE-- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 277 lHSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05072   159 -YTAREGAKFpiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIP 205
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
221-359 8.36e-20

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: 88.64  E-value: 8.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 221 RIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARlhsTRVLGTFGYHAPEyAMTGQLT 300
Cdd:cd06617   107 KIAVSIVKALEYLHSKLS--VIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVAK---TIDAGCKPYMAPE-RINPELN 180
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 301 Q-----KSDVYSFGVVLLELLTGRKPVD--HTMPRGQQSLVTWATPRLSEDK--------VKQCV--DPKLKGEYP 359
Cdd:cd06617   181 QkgydvKSDVWSLGITMIELATGRFPYDswKTPFQQLKQVVEEPSPQLPAEKfspefqdfVNKCLkkNYKERPNYP 256
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
119-321 1.21e-19

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 88.94  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEP--ESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAtMGSL 195
Cdd:cd06633    29 IGHGSFGAVYFATnSHTNEVVAIKKMSYSGKQtnEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYC-LGSA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKgvqgaQPgptldwIQRVRIAV---DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF-NLSNQSP 271
Cdd:cd06633   108 SDLLEVHK-----KP------LQEVEIAAithGALQGLAYLHSH---NMIHRDIKAGNILLTEPGQVKLADFgSASIASP 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 272 dmaarlhSTRVLGTFGYHAPEYAMT---GQLTQKSDVYSFGVVLLElLTGRKP 321
Cdd:cd06633   174 -------ANSFVGTPYWMAPEVILAmdeGQYDGKVDIWSLGITCIE-LAERKP 218
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
101-327 1.24e-19

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 88.51  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 101 LSLDELKEKTDNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRvSKLKHDNFVELFG---- 175
Cdd:cd06639    12 LGLESLADPSDTWDIIETIGKGTYGKVYKVTNKkDGSLAAVKILDPISDVDEEIEAEYNILR-SLPNHPNVVKFYGmfyk 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 176 --YCVEGNFrILAYEFATMGSLHDILHGRkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLL 253
Cdd:cd06639    91 adQYVGGQL-WLVLELCNGGSVTELVKGL-----LKCGQRLDEAMISYILYGALLGLQHLHNN---RIIHRDVKGNNILL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 254 FEDFKAKIADFNLSNQSpdMAARLHSTRVLGTFGYHAPEYAMTGQLTQKS-----DVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd06639   162 TTEGGVKLVDFGVSAQL--TSARLRRNTSVGTPFWMAPEVIACEQQYDYSydarcDVWSLGITAIELADGDPPLFDMHP 238
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
151-354 1.63e-19

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: 87.42  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 151 SNVEflTQVSRVSKLKHDNFVELFGYCVE-------GNFRILAyEFATMGSLHDILhgrkgvqgaQPGPTLDWIQRVRIA 223
Cdd:cd14012    43 QLLE--KELESLKKLRHPNLVSYLAFSIErrgrsdgWKVYLLT-EYAPGGSLSELL---------DSVGSVPLDTARRWT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 224 VDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF---KAKIADFNLSNQSPDMAARLHSTRVLGTFgYHAPEYA-MTGQL 299
Cdd:cd14012   111 LQLLEALEYLHRN---GVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTLLDMCSRGSLDEFKQTY-WLPPELAqGSKSP 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 300 TQKSDVYSFGVVLLELLTGrKPVDHTMPRGQQSLVTWATPRLSEDKVKQCV--DPKL 354
Cdd:cd14012   187 TRKTDVWDLGLLFLQMLFG-LDVLEKYTSPNPVLVSLDLSASLQDFLSKCLslDPKK 242
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
116-400 2.01e-19

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 90.68  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYA-TLKDGKAVAVKKL-DNAAEPESnvefltQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:PLN00113  695 ENVISRGKKGASYKGkSIKNGMQFVVKEInDVNSIPSS------EIADMGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGK 768
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGrkgvqgaqpgptLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLfeDFKAKIadfNLSNQSPDM 273
Cdd:PLN00113  769 NLSEVLRN------------LSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIII--DGKDEP---HLRLSLPGL 831
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 274 AARlhSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMpRGQQSLVTWATPRLSEDKVKQCVDPK 353
Cdd:PLN00113  832 LCT--DTKCFISSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEF-GVHGSIVEWARYCYSDCHLDMWIDPS 908
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 354 LKGEYPPKAVAKLAAV--AALCVQYESEFRPNMSIVVKALQPLLRSSTA 400
Cdd:PLN00113  909 IRGDVSVNQNEIVEVMnlALHCTATDPTARPCANDVLKTLESASRSSSS 957
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
119-321 2.02e-19

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: 87.12  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEP--ESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAtMGSL 195
Cdd:cd06607     9 IGHGSFGAVYYARnKRTSEVVAIKKMSYSGKQstEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYC-LGSA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKgvqgaqpgptlDWIQRVRIAV---DAARGLEYLHEKVQpavIHRDIRSSNVLLFEDFKAKIADFNlsnqspd 272
Cdd:cd06607    88 SDIVEVHK-----------KPLQEVEIAAichGALQGLAYLHSHNR---IHRDVKAGNILLTEPGTVKLADFG------- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 273 mAARLHS--TRVLGTFGYHAPE--YAM-TGQLTQKSDVYSFGVVLLElLTGRKP 321
Cdd:cd06607   147 -SASLVCpaNSFVGTPYWMAPEviLAMdEGQYDGKVDVWSLGITCIE-LAERKP 198
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
118-317 2.63e-19

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 87.13  E-value: 2.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK------DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAT 191
Cdd:cd05046    12 TLGRGEFGEVFLAKAKgieeegGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYTD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNqSP 271
Cdd:cd05046    92 LGDLKQFLRATKSKDEKLKPPPLSTKQKVALCTQIALGMDHLSNA---RFVHRDLAARNCLVSSQREVKVSLLSLSK-DV 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1032291014 272 DMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05046   168 YNSEYYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFT 213
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
116-317 2.67e-19

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 86.71  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKD-GKAVAVKKLdnaAEPESNV-EFLTQVSRVSKLKHDNFVELFGYCV-EGNFRILAyEFATM 192
Cdd:cd05052    11 KHKLGGGQYGEVYEGVWKKyNLTVAVKTL---KEDTMEVeEFLKEAAVMKEIKHPNLVQLLGVCTrEPPFYIIT-EFMPY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspd 272
Cdd:cd05052    87 GNLLDYLRECNRE-------ELNAVVLLYMATQIASAMEYLEKK---NFIHRDLAARNCLVGENHLVKVADFGLSRL--- 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 273 MAARLHSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05052   154 MTGDTYTAHAGAKFpiKWTAPESLAYNKFSIKSDVWAFGVLLWEIAT 200
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
111-321 3.10e-19

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: 86.54  E-value: 3.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYE 188
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKyTGQVVALKFIPKRGKSEKELRNLRQeIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATmGSLHDILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsn 268
Cdd:cd14002    81 YAQ-GELFQILEDDG---------TLPEEEVRSIAKQLVSALHYLHSN---RIIHRDMKPQNILIGKGGVVKLCDFGF-- 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 269 qspdmaARLHS--TRVL----GTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14002   146 ------ARAMScnTLVLtsikGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPP 198
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
119-397 3.57e-19

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 86.55  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYG---RAYYATLKDGKAVAVKKLDNAA-EPESNVEFLTQVSRVSKLKHDNFVELFGYCvEGNFRILAYEFATMGS 194
Cdd:cd05116     3 LGSGNFGtvkKGYYQMKKVVKTVAVKILKNEAnDPALKDELLREANVMQQLDNPYIVRMIGIC-EAESWMLVMEMAELGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGVQGAQpgpTLDWIQRVRIavdaarGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ-SPDM 273
Cdd:cd05116    82 LNKFLQKNRHVTEKN---ITELVHQVSM------GMKYLEES---NFVHRDLAARNVLLVTQHYAKISDFGLSKAlRADE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 274 AARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVDhtmprgqqslvtwatpRLSEDKVKQCVDP 352
Cdd:cd05116   150 NYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYK----------------GMKGNEVTQMIEK 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1032291014 353 KLKGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVvkalQPLLRS 397
Cdd:cd05116   214 GERMECPAGCPPEMYDLMKLCWTYDVDERPGFAAV----ELRLRN 254
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
119-349 5.39e-19

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: 86.23  E-value: 5.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLHDI 198
Cdd:cd05073    19 LGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVE--AFLAEANVMKTLQHDKLVKLHAVVTKEPIYIIT-EFMAKGSLLDF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKGvqGAQPGPTLdwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAarlH 278
Cdd:cd05073    96 LKSDEG--SKQPLPKL-----IDFSAQIAEGMAFIEQR---NYIHRDLRAANILVSASLVCKIADFGLARVIEDNE---Y 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 STRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP--------VDHTMPRGQQSLVTWATPRLSEDKVK 347
Cdd:cd05073   163 TAREGAKFpiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPypgmsnpeVIRALERGYRMPRPENCPEELYNIMM 242

                  ..
gi 1032291014 348 QC 349
Cdd:cd05073   243 RC 244
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
119-389 5.69e-19

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: 86.28  E-value: 5.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDnAAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd06641    12 IGKGSFGEVFKGIdNRTQKVVAIKIID-LEEAEDEIEDIQQeITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILhgrkgvqgaQPGPtLDWIQRVRIAVDAARGLEYLHEKVQpavIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmaAR 276
Cdd:cd06641    91 DLL---------EPGP-LDETQIATILREILKGLDYLHSEKK---IHRDIKAANVLLSEHGEVKLADFGVAGQLTD--TQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 277 LHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPrlsedkvkqcvdPKLKG 356
Cdd:cd06641   156 IKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNP------------PTLEG 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1032291014 357 EYppkaVAKLAAVAALCVQYESEFRPNMSIVVK 389
Cdd:cd06641   224 NY----SKPLKEFVEACLNKEPSFRPTAKELLK 252
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
119-321 5.73e-19

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: 86.09  E-value: 5.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAA-EPESnveFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATMGSLHD 197
Cdd:cd05067    15 LGAGQFGEVWMGYYNGHTKVAIKSLKQGSmSPDA---FLAEANLMKQLQHQRLVRLYAVVTQEPIYIIT-EYMENGSLVD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKGVQgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqspdmaARL 277
Cdd:cd05067    91 FLKTPSGIK-------LTINKLLDMAAQIAEGMAFIEER---NYIHRDLRAANILVSDTLSCKIADFGL--------ARL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 278 -----HSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05067   153 iedneYTAREGAKFpiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIP 204
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
118-321 5.82e-19

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: 86.14  E-value: 5.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLDnAAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEG-NFRILAyEFATMGS 194
Cdd:cd06609     8 RIGKGSFGEVYKGIDKRtNQVVAIKVID-LEEAEDEIEDIQQeIQFLSQCDSPYITKYYGSFLKGsKLWIIM-EYCGGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILhgrkgvqgaQPGPtLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd06609    86 VLDLL---------KPGP-LDETYIAFILREVLLGLEYLHSE---GKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTM 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 275 ARLHSTrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06609   153 SKRNTF--VGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPP 197
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
117-321 6.85e-19

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: 85.66  E-value: 6.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYA-TLKDGKAVAVKKLD-------NAAEPESNVEFLT-QVSRVSKLKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd06628     6 ALIGSGSFGSVYLGmNASSGELMAVKQVElpsvsaeNKDRKKSMLDALQrEIALLRELQHENIVQYLGSSSDANHLNIFL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGrkgvQGAQPGPTL-DWIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd06628    86 EYVPGGSVATLLNN----YGAFEESLVrNFVRQI------LKGLNYLHNR---GIIHRDIKGANILVDNKGGIKISDFGI 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 267 SNQ----SPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06628   153 SKKleanSLSTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHP 211
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
118-321 7.46e-19

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: 85.90  E-value: 7.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKLD-NAAEPESNVEflTQVSRVSKLK----------HDNFVELFGYCVEGNFRIL 185
Cdd:cd06629     8 LIGKGTYGRVYLAmNATTGEMLAVKQVElPKTSSDRADS--RQKTVVDALKseidtlkdldHPNIVQYLGFEETEDYFSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILhgRKgvqgaqPGPTLDWIQR--VRIAVDaarGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd06629    86 FLEYVPGGSIGSCL--RK------YGKFEEDLVRffTRQILD---GLAYLHSK---GILHRDLKADNILVDLEGICKISD 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 264 FNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQ--LTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06629   152 FGISKKSDDIYGNNGATSMQGSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRRP 211
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
210-321 8.56e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 88.31  E-value: 8.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 210 PGPTL-DWIQR---------VRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN----LSNQSpdMAa 275
Cdd:NF033483   90 DGRTLkDYIREhgplspeeaVEIMIQILSALEHAHRN---GIVHRDIKPQNILITKDGRVKVTDFGiaraLSSTT--MT- 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1032291014 276 rlHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:NF033483  164 --QTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPP 207
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
111-323 8.67e-19

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 85.39  E-value: 8.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKDGKAV-AVKKLDNAAEPESNVE--FLTQVSRVSKLKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYLAREKQSKFIlALKVLFKAQLEKAGVEhqLRREVEIQSHLRHPNILRLYGYFHDATRVYLIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILhgrkgvqgaQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS 267
Cdd:cd14116    85 EYAPLGTVYREL---------QKLSKFDEQRTATYITELANALSYCHSK---RVIHRDIKPENLLLGSAGELKIADFGWS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 268 NQSPdmAARlhSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14116   153 VHAP--SSR--RTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFE 204
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
107-321 9.10e-19

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


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 85.19  E-value: 9.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 107 KEKTDNFGSkslIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFlTQVSRVSKLKHDNFVELFGYCVEGNFRIL 185
Cdd:cd06648     6 RSDLDNFVK---IGEGSTGIVCIATDKStGRQVAVKKMDLRKQQRRELLF-NEVVIMRDYQHPNIVEMYSSYLVGDELWV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDIL-HGRkgvqgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd06648    82 VMEFLEGGALTDIVtHTR-----------MNEEQIATVCRAVLKALSFLHSQ---GVIHRDIKSDSILLTSDGRVKLSDF 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 265 NLSNQ-SPDMAARlhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06648   148 GFCAQvSKEVPRR---KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPP 202
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
116-317 1.30e-18

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


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 85.82  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATL-KDGKAV--AVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFRILAYEFAT 191
Cdd:cd05088    12 QDVIGEGNFGQVLKARIkKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGVQ-------GAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd05088    92 HGNLLDFLRKSRVLEtdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQK---QFIHRDLAARNILVGENYVAKIADF 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 265 NLSNqspdmAARLHSTRVLGTFG--YHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05088   169 GLSR-----GQEVYVKKTMGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 218
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
119-317 1.32e-18

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 85.40  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD--GKA----VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05045     8 LGEGEFGKVVKATAFRlkGRAgyttVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILH-GRK------GVQGAQPGPTLDWIQR--------VRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd05045    88 GSLRSFLReSRKvgpsylGSDGNRNSSYLDNPDEraltmgdlISFAWQISRGMQYLAEM---KLVHRDLAARNVLVAEGR 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 258 KAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05045   165 KMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVT 224
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
111-323 1.33e-18

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: 84.91  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNV--EFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRArSLHTGLEVAIKMIDKKAMQKAGMvqRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGRKgvqgaQPgptldwiqrvrIAVDAAR--------GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA 259
Cdd:cd14186    81 EMCHNGEMSRYLKNRK-----KP-----------FTEDEARhfmhqivtGMLYLHSH---GILHRDLTLSNLLLTRNMNI 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 260 KIADFNLSNQSpDMAARLHSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14186   142 KIADFGLATQL-KMPHEKHFT-MCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFD 203
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
119-317 1.62e-18

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 85.40  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAY----YATLKDGK----AVAVKKLDNAAEPESNVEFLTQVsRVSKL--KHDNFVELFGYCVEGNFRILAYE 188
Cdd:cd05099    20 LGEGCFGQVVraeaYGIDKSRPdqtvTVAVKMLKDNATDKDLADLISEM-ELMKLigKHKNIINLLGVCTQEGPLYVIVE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHDILHGRKgvqgaQPGP------------TLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFED 256
Cdd:cd05099    99 YAAKGNLREFLRARR-----PPGPdytfditkvpeeQLSFKDLVSCAYQVARGMEYLESR---RCIHRDLAARNVLVTED 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 257 FKAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05099   171 NVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFT 231
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
119-341 1.73e-18

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: 85.00  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKD--GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd14206     5 IGNGWFGKVILGeIFSDytPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGDL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQGAQPG-PTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd14206    85 KRYLRAQRKADGMTPDlPTRDLRTLQRMAYEITLGLLHLHKN---NYIHSDLALRNCLLTSDLTVRIGDYGLSHNNYKED 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 275 ARLHSTRVLGTFGYHAPEY--AMTGQL-----TQKSDVYSFGVVLLELLT-GRKPVDHT--------MPRGQQslVTWAT 338
Cdd:cd14206   162 YYLTPDRLWIPLRWVAPELldELHGNLivvdqSKESNVWSLGVTIWELFEfGAQPYRHLsdeevltfVVREQQ--MKLAK 239

                  ...
gi 1032291014 339 PRL 341
Cdd:cd14206   240 PRL 242
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
119-317 3.03e-18

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: 85.07  E-value: 3.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATL------KDGKA--VAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd05100    20 LGEGCFGQVVMAEAigidkdKPNKPvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRK--GVQGA-----QPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd05100   100 ASKGNLREYLRARRppGMDYSfdtckLPEEQLTFKDLVSCAYQVARGMEYLASQ---KCIHRDLAARNVLVTEDNVMKIA 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 263 DFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05100   177 DFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT 231
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
118-321 3.25e-18

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: 83.61  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVEFLTQVSR----VSKLKHDNFVELFGY-CVEGNFRILaYEFAT 191
Cdd:cd06632     7 LLGSGSFGSVYEGfNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQeialLSKLRHPNIVQYYGTeREEDNLYIF-LEYVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGrkgvQGAQPGPTLDWIQRVRIAvdaarGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSP 271
Cdd:cd06632    86 GGSIHKLLQR----YGAFEEPVIRLYTRQILS-----GLAYLHSR---NTVHRDIKGANILVDTNGVVKLADFGMAKHVE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 272 DMAarlHSTRVLGTFGYHAPEYAMT--GQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06632   154 AFS---FAKSFKGSPYWMAPEVIMQknSGYGLAVDIWSLGCTVLEMATGKPP 202
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
119-316 3.47e-18

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 83.84  E-value: 3.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEpESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd14222     1 LGKGFFGQAIKVTHKaTGKVMVMKELIRCDE-ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvQGAQPGPtldWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN--------Q 269
Cdd:cd14222    80 FL------RADDPFP---WQQKVSFAKGIASGMAYLHSM---SIIHRDLNSHNCLIKLDKTVVVADFGLSRliveekkkP 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 270 SPDMAA----------RLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELL 316
Cdd:cd14222   148 PPDKPTtkkrtlrkndRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
119-321 3.78e-18

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: 83.29  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVE-FLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd05117     8 LGRGSFGVVRLAVHKkTGEEYAVKIIDKKKLKSEDEEmLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGGELF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLF---EDFKAKIADFNLS---NQS 270
Cdd:cd05117    88 DRIVKKG---------SFSEREAAKIMKQILSAVAYLHSQ---GIVHRDLKPENILLAskdPDSPIKIIDFGLAkifEEG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 271 PDMaarlhSTRVlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05117   156 EKL-----KTVC-GTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPP 200
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
119-321 4.06e-18

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: 83.58  E-value: 4.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKA---VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd05033    12 IGGGEFGEVCSGSLKlPGKKeidVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMENGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd05033    92 LDKFLRENDG--------KFTVTQLVGMLRGIASGMKYLSEMN---YVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 275 ARlHSTR-----VLGTfgyhAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05033   161 AT-YTTKggkipIRWT----APEAIAYRKFTSASDVWSFGIVMWEVMSyGERP 208
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
116-321 4.52e-18

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: 83.37  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKD-GKAVAVK--KLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd14099     6 GKFLGKGGFAKCYEVTDMStGKVYAGKvvPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGAQpgptldwiqrVR-IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqsp 271
Cdd:cd14099    86 GSLMELLKRRKALTEPE----------VRyFMRQILSGVKYLHSN---RIIHRDLKLGNLFLDENMNVKIGDFGL----- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 272 dmAARLHS-----TRVLGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14099   148 --AARLEYdgerkKTLCGTPNYIAPEVLEKKKgHSFEVDIWSLGVILYTLLVGKPP 201
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
116-398 5.27e-18

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 83.52  E-value: 5.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYAT------LKDGKAVAVKKLDNAaEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd05094    10 KRELGEGAFGKVFLAEcynlspTKDKMLVAVKTLKDP-TLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDIL--HGRKGV-----QGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd05094    89 MKHGDLNKFLraHGPDAMilvdgQPRQAKGELGLSQMLHIATQIASGMVYLASQ---HFVHRDLATRNCLVGANLLVKIG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 263 DFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPvdhtmprgqqslvtWAtpRL 341
Cdd:cd05094   166 DFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQP--------------WF--QL 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 342 SEDKVKQCVDPKLKGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLRSS 398
Cdd:cd05094   230 SNTEVIECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKAT 286
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
119-323 5.37e-18

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: 83.08  E-value: 5.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEF-LTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd08225     8 IGEGSFGKIYLAKAKsDSEHCVIKEIDLTKMPVKEKEAsKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGDLM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKGVQGAQpGPTLDWIqrVRIAVdaarGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK-AKIADFNLSNQSPDmAA 275
Cdd:cd08225    88 KRINRQRGVLFSE-DQILSWF--VQISL----GLKHIHDR---KILHRDIKSQNIFLSKNGMvAKLGDFGIARQLND-SM 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 276 RLHSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd08225   157 ELAYT-CVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFE 203
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
119-322 5.72e-18

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: 83.48  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKK--------------------LDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCV 178
Cdd:cd14067     1 LGQGGSGTVIYRARYQGQPVAVKRfhikkckkrtdgsadtmlkhLRAADAMKNFSEFRQEASMLHSLQHPCIVYLIGISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 179 EGnfRILAYEFATMGSLHDILHGRKGVQGAQPgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLF---- 254
Cdd:cd14067    81 HP--LCFALELAPLGSLNTVLEENHKGSSFMP---LGHMLTFKIAYQIAAGLAYLHKK---NIIFCDLKSDNILVWsldv 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 255 -EDFKAKIADFNLSNQSPDMAArlhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPV 322
Cdd:cd14067   153 qEHINIKLSDYGISRQSFHEGA----LGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPS 217
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
111-317 7.10e-18

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 83.27  E-value: 7.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKDGK----AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVE-GNFRIL 185
Cdd:cd05043     6 ERVTLSDLLQEGTFGRIFHGILRDEKgkeeEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEdGEKPMV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILHGRKGVqGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd05043    86 LYPYMNWGNLKLFLQQCRLS-EANNPQALSTQQLVHMALQIACGMSYLHRR---GVIHKDIAARNCVIDDELQVKITDNA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 266 LSnqspdmaarlhstRVLGTFGYH-------------APEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05043   162 LS-------------RDLFPMDYHclgdnenrpikwmSLESLVNKEYSSASDVWSFGVLLWELMT 213
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
119-389 7.85e-18

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: 82.80  E-value: 7.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06642    12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQeITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSALD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgaQPGPtLDWIQRVRIAVDAARGLEYLHEKVQpavIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmaARL 277
Cdd:cd06642    92 LL---------KPGP-LEETYIATILREILKGLDYLHSERK---IHRDIKAANVLLSEQGDVKLADFGVAGQLTD--TQI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 278 HSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPrlsedkvkqcvdPKLKGE 357
Cdd:cd06642   157 KRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSP------------PTLEGQ 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1032291014 358 YppkaVAKLAAVAALCVQYESEFRPNMSIVVK 389
Cdd:cd06642   225 H----SKPFKEFVEACLNKDPRFRPTAKELLK 252
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
118-328 9.62e-18

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 82.48  E-value: 9.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKAVAVKKLD------NAAEPESNvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAT 191
Cdd:cd06631     8 VLGKGAYGTVYCGLTSTGQLIAVKQVEldtsdkEKAEKEYE-KLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILhgrkgvqgAQPGPtLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF------- 264
Cdd:cd06631    87 GGSIASIL--------ARFGA-LEEPVFCRYTKQILEGVAYLHNN---NVIHRDIKGNNIMLMPNGVIKLIDFgcakrlc 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 265 -NLSNQSpdMAARLHSTRvlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHtMPR 328
Cdd:cd06631   155 iNLSSGS--QSQLLKSMR--GTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWAD-MNP 214
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
138-316 9.75e-18

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: 83.06  E-value: 9.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 138 VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDIL----------HGRKGVQG 207
Cdd:cd05096    49 VAVKILRPDANKNARNDFLKEVKILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLsshhlddkeeNGNDAVPP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 208 AQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS-NQSPDMAARLHSTRVLgTF 286
Cdd:cd05096   129 AHCLPAISYSSLLHVALQIASGMKYLSSL---NFVHRDLATRNCLVGENLTIKIADFGMSrNLYAGDYYRIQGRAVL-PI 204
                         170       180       190
                  ....*....|....*....|....*....|
gi 1032291014 287 GYHAPEYAMTGQLTQKSDVYSFGVVLLELL 316
Cdd:cd05096   205 RWMAWECILMGKFTTASDVWAFGVTLWEIL 234
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
118-321 1.01e-17

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 82.54  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPE--SNVEFLTQVSRVSKLKHDNFVELFGYCVEGnfRILAYEFATMGSL 195
Cdd:cd14025     3 KVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDdsERMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHeKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSN---QSPD 272
Cdd:cd14025    81 EKLLASE----------PLPWELRFRIIHETAVGMNFLH-CMKPPLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHS 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 273 MaaRLHSTRVLGTFGYHAPEYAMTGQ--LTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14025   150 H--DLSRDGLRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKP 198
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
118-321 1.05e-17

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 82.58  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK--DGKA--VAVK--KLDNAAEPESNvEFLTQVSRVSKLKHDNFVELFGYCVEGNFR------IL 185
Cdd:cd05035     6 ILGEGEFGSVMEAQLKqdDGSQlkVAVKtmKVDIHTYSEIE-EFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppspMV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHD-ILHGRKGVQGAQ-PGPTLdwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd05035    85 ILPFMKHGDLHSyLLYSRLGGLPEKlPLQTL-----LKFMVDIAKGMEYLSNR---NFIHRDLAARNCMLDENMTVCVAD 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 264 FNLSNQ--SPDMAARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05035   157 FGLSRKiySGDYYRQGRISKM--PVKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTP 215
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
113-328 1.15e-17

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: 82.37  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRAYYATLKDGK--AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFA 190
Cdd:cd14202     4 FSRKDLIGHGAFAVVFKGRHKEKHdlEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRKGVQGaqpgptldwiQRVRIAVDAARG-LEYLHEKvqpAVIHRDIRSSNVLLF---------EDFKAK 260
Cdd:cd14202    84 NGGDLADYLHTMRTLSE----------DTIRLFLQQIAGaMKMLHSK---GIIHRDLKPQNILLSysggrksnpNNIRIK 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 261 IADFNLSN--QSPDMAARLhstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPR 328
Cdd:cd14202   151 IADFGFARylQNNMMAATL-----CGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQ 215
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
119-351 1.17e-17

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: 82.28  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVeFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06647    15 IGQGASGTVYTAIdVATGQEVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgaqPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ-SPDMAAR 276
Cdd:cd06647    94 VV----------TETCMDEGQIAAVCRECLQALEFLHSN---QVIHRDIKSDNILLGMDGSVKLTDFGFCAQiTPEQSKR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 277 lhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP-RGQQSLVTWATPRLSE---------DKV 346
Cdd:cd06647   161 ---STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNpeklsaifrDFL 237

                  ....*
gi 1032291014 347 KQCVD 351
Cdd:cd06647   238 NRCLE 242
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
119-317 1.25e-17

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 82.75  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT---LKDGK-----AVAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd05098    21 LGEGCFGQVVLAEaigLDKDKpnrvtKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRK--GVQ-----GAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd05098   101 ASKGNLREYLQARRppGMEycynpSHNPEEQLSSKDLVSCAYQVARGMEYLASK---KCIHRDLAARNVLVTEDNVMKIA 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 263 DFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05098   178 DFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFT 232
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
132-323 1.49e-17

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 82.10  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 132 LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCV-EGNFRILAYEFATMGSLHDILhgRKGvqgaqp 210
Cdd:cd06620    27 IPTGTIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLnENNNIIICMEYMDCGSLDKIL--KKK------ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 211 GP-TLDWIQRVRIAVdaARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAArlhSTRVlGTFGYH 289
Cdd:cd06620    99 GPfPEEVLGKIAVAV--LEGLTYLYNVHR--IIHRDIKPSNILVNSKGQIKLCDFGVSGELINSIA---DTFV-GTSTYM 170
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1032291014 290 APEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd06620   171 SPERIQGGKYSVKSDVWSLGLSIIELALGEFPFA 204
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
119-317 1.67e-17

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 82.76  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATL--------KDGKAVAVKKL-DNAAEPE-----SNVEFLTQVSrvsklKHDNFVELFGYCVEGNFRI 184
Cdd:cd05101    32 LGEGCFGQVVMAEAvgidkdkpKEAVTVAVKMLkDDATEKDlsdlvSEMEMMKMIG-----KHKNIINLLGACTQDGPLY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYEFATMGSLHDILHGRK--GVQGAQ-----PGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd05101   107 VIVEYASKGNLREYLRARRppGMEYSYdinrvPEEQMTFKDLVSCTYQLARGMEYLASQ---KCIHRDLAARNVLVTENN 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 258 KAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05101   184 VMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFT 243
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
119-341 1.70e-17

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: 82.46  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVeFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06655    27 IGQGASGTVFTAIdVATGQEVAIKQINLQKQPKKEL-IINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSLTD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgaqPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ-SPDMAAR 276
Cdd:cd06655   106 VV----------TETCMDEAQIAAVCRECLQALEFLHAN---QVIHRDIKSDNVLLGMDGSVKLTDFGFCAQiTPEQSKR 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 277 lhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP-RGQQSLVTWATPRL 341
Cdd:cd06655   173 ---STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPEL 235
Pkinase pfam00069
Protein kinase domain;
116-321 1.87e-17

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 80.37  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKD-GKAVAVKKLDNA-AEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:pfam00069   4 LRKLGSGSFGTVYKAKHRDtGKIVAIKKIKKEkIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGVQGAqpgptldwiQRVRIAVDAARGLEYLHEKvqpavihrdirssnvllfedfkakiadfnlsnqspdm 273
Cdd:pfam00069  84 SLFDLLSEKGAFSER---------EAKFIMKQILEGLESGSSL------------------------------------- 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 274 aarlhSTRVlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:pfam00069 118 -----TTFV-GTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPP 159
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
111-320 2.07e-17

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: 81.57  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKK--LDNAAEPESNVefLTQVSRVSKLKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd13996     6 NDFEEIELLGSGGFGSVYKVRNKvDGVTYAIKKirLTEKSSASEKV--LREVKALAKLNHPNIVRYYTAWVEEPPLYIQM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGRKGVqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK-AKIADFNL 266
Cdd:cd13996    84 ELCEGGTLRDWIDRRNSS------SKNDRKLALELFKQILKGVSYIHSK---GIVHRDLKPSNIFLDNDDLqVKIGDFGL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 267 S-------NQSPDMAARL------HSTRVlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRK 320
Cdd:cd13996   155 AtsignqkRELNNLNNNNngntsnNSVGI-GTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFK 220
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
118-323 2.10e-17

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: 81.30  E-value: 2.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNveFLTQVSR----VSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd14663     7 TLGEGTFAKVKFArNTKTGESVAIKIIDKEQVAREG--MVEQIKReiaiMKLLRHPNIVELHEVMATKTKIFFVMELVTG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILhgrkgvqgAQPGPTLDWIQRvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS--NQS 270
Cdd:cd14663    85 GELFSKI--------AKNGRLKEDKAR-KYFQQLIDAVDYCHSR---GVFHRDLKPENLLLDEDGNLKISDFGLSalSEQ 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 271 PDMAARLHSTrvLGTFGYHAPE-YAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14663   153 FRQDGLLHTT--CGTPNYVAPEvLARRGYDGAKADIWSCGVILFVLLAGYLPFD 204
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
118-344 2.21e-17

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: 81.75  E-value: 2.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKH---DNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd06917     8 LVGRGSYGAVYRGYhVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILhgrkgvqgaQPGPtldwIQRVRIAV---DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqs 270
Cdd:cd06917    88 SIRTLM---------RAGP----IAERYIAVimrEVLVALKFIHKD---GIIHRDIKAANILVTNTGNVKLCDFGV---- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 271 pdmAARLHSTR-----VLGTFGYHAPEYAMTGQL-TQKSDVYSFGVVLLELLTGRKPV-DHTMPRGQQSLVTWATPRLSE 343
Cdd:cd06917   148 ---AASLNQNSskrstFVGTPYWMAPEVITEGKYyDTKADIWSLGITTYEMATGNPPYsDVDALRAVMLIPKSKPPRLEG 224

                  .
gi 1032291014 344 D 344
Cdd:cd06917   225 N 225
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
119-392 2.33e-17

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: 81.87  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAY---YATLKD--GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRI--LAYEFAT 191
Cdd:cd05080    12 LGEGHFGKVSlycYDPTNDgtGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGKSlqLIMEYVP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILhgrkgvqgaqPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSP 271
Cdd:cd05080    92 LGSLRDYL----------PKHSIGLAQLLLFAQQICEGMAYLHSQ---HYIHRDLAARNVLLDNDRLVKIGDFGLAKAVP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 272 D--MAARLHSTRVLGTFGYhAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPvDHTMPRGQQSLVTWATPRLSEDKVKQC 349
Cdd:cd05080   159 EghEYYRVREDGDSPVFWY-APECLKEYKFYYASDVWSFGVTLYELLTHCDS-SQSPPTKFLEMIGIAQGQMTVVRLIEL 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1032291014 350 VDPKLKGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQ 392
Cdd:cd05080   237 LERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILK 279
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
150-353 2.40e-17

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: 81.39  E-value: 2.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 150 ESNVEFLTQVSRVSKLKHDNFVELFGYCVE-GNFRiLAYEFATMGSLHDILHGRK---GVQGaqpgptldwiqrvRIAVD 225
Cdd:cd14027    33 EHNEALLEEGKMMNRLRHSRVVKLLGVILEeGKYS-LVMEYMEKGNLMHVLKKVSvplSVKG-------------RIILE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 226 AARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF---------NLSNQSPDMAARLHST--RVLGTFGYHAPEY- 293
Cdd:cd14027    99 IIEGMAYLHGK---GVIHKDLKPENILVDNDFHIKIADLglasfkmwsKLTKEEHNEQREVDGTakKNAGTLYYMAPEHl 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 294 -AMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQ------------QSLVTWATPRLSEDKVKQCVDPK 353
Cdd:cd14027   176 nDVNAKPTEKSDVYSFAIVLWAIFANKEPYENAINEDQiimciksgnrpdVDDITEYCPREIIDLMKLCWEAN 248
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
119-321 2.54e-17

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: 81.19  E-value: 2.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKL---DNaaEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd06626     8 IGEGTFGKVYTAvNLDTGELMAMKEIrfqDN--DPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDIL-HGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN-----LSN 268
Cdd:cd06626    86 LEELLrHGR----------ILDEAVIRVYTLQLLEGLAYLHEN---GIVHRDIKPANIFLDSNGLIKLGDFGsavklKNN 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 269 QSPDMAARLHSTRvlGTFGYHAPEYAMTGQLTQK---SDVYSFGVVLLELLTGRKP 321
Cdd:cd06626   153 TTTMAPGEVNSLV--GTPAYMAPEVITGNKGEGHgraADIWSLGCVVLEMATGKRP 206
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
119-317 2.55e-17

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: 81.62  E-value: 2.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD------GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05062    14 LGQGSFGMVYEGIAKGvvkdepETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGAQPGPTLDWIQR-VRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSP 271
Cdd:cd05062    94 GDLKSYLRSLRPEMENNPVQAPPSLKKmIQMAGEIADGMAYLNAN---KFVHRDLAARNCMVAEDFTVKIGDFGMTRDIY 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1032291014 272 DMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05062   171 ETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIAT 216
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
119-321 2.61e-17

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: 80.73  E-value: 2.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFL-TQVSRVSKLKHDNFVELFGyCVEGNFRI-LAYEFATMGSL 195
Cdd:cd14009     1 IGRGSFATVWKGRHKQtGEVVAIKEISRKKLNKKLQENLeSEIAILKSIKHPNIVRLYD-VQKTEDFIyLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQGAqpgptldwIQRvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA---KIADFNL--SNQS 270
Cdd:cd14009    80 SQYIRKRGRLPEA--------VAR-HFMQQLASGLKFLRSK---NIIHRDLKPQNLLLSTSGDDpvlKIADFGFarSLQP 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 271 PDMAARLhstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14009   148 ASMAETL-----CGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPP 193
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
119-321 2.73e-17

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: 81.12  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVA--VKKLDNAAEPESNvEFLTQVSRVSKLKHDNFVELFGYCVEGNFR--ILAYEFATMG 193
Cdd:cd13983     9 LGRGSFKTVYRAfDTEEGIEVAwnEIKLRKLPKAERQ-RFKQEIEILKSLKHPNIIKFYDSWESKSKKevIFITELMTSG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILhgRKgvqgaqpgptldwIQRVRIAV------DAARGLEYLHeKVQPAVIHRDIRSSNVllfedF------KAKI 261
Cdd:cd13983    88 TLKQYL--KR-------------FKRLKLKVikswcrQILEGLNYLH-TRDPPIIHRDLKCDNI-----FingntgEVKI 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 262 ADFNLSnqspdmAARLHSTR--VLGTFGYHAPE-YamTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd13983   147 GDLGLA------TLLRQSFAksVIGTPEFMAPEmY--EEHYDEKVDIYAFGMCLLEMATGEYP 201
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
119-328 3.15e-17

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: 81.16  E-value: 3.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LhgrKGVQGAQPgptldWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS-------NQSP 271
Cdd:cd14221    81 I---KSMDSHYP-----WSQRVSFAKDIASGMAYLHSM---NIIHRDLNSHNCLVRENKSVVVADFGLArlmvdekTQPE 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 272 DMAARLHSTR-----VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLtGRKPVD-HTMPR 328
Cdd:cd14221   150 GLRSLKKPDRkkrytVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII-GRVNADpDYLPR 211
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
83-321 3.58e-17

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: 81.64  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  83 AAVKPDALKEPpsiDVPALSLDELKEKTdnFGSKSLIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEP--ESNVEFLTQV 159
Cdd:cd06635     2 STSRAGSLKDP---DIAELFFKEDPEKL--FSDLREIGHGSFGAVYFArDVRTSEVVAIKKMSYSGKQsnEKWQDIIKEV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 160 SRVSKLKHDNFVELFGYCVEGNFRILAYEFAtMGSLHDILHGRKgvqgaQPgptLDWIQRVRIAVDAARGLEYLHEKvqp 239
Cdd:cd06635    77 KFLQRIKHPNSIEYKGCYLREHTAWLVMEYC-LGSASDLLEVHK-----KP---LQEIEIAAITHGALQGLAYLHSH--- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 240 AVIHRDIRSSNVLLFEDFKAKIADFNlsnqSPDMAARLHStrVLGTFGYHAPEYAMT---GQLTQKSDVYSFGVVLLElL 316
Cdd:cd06635   145 NMIHRDIKAGNILLTEPGQVKLADFG----SASIASPANS--FVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIE-L 217

                  ....*
gi 1032291014 317 TGRKP 321
Cdd:cd06635   218 AERKP 222
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
119-323 3.95e-17

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: 80.51  E-value: 3.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVK--KLDNAAEPESNVEFLTQVSRVSKLKHDNFV---ELFgycvEGNFRI-LAYEFAT 191
Cdd:cd14073     9 LGKGTYGKVKLAIERAtGREVAIKsiKKDKIEDEQDMVRIRREIEIMSSLNHPHIIriyEVF----ENKDKIvIVMEYAS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGVQGAQpgptldwIQRV-RIAVDAARgleYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQs 270
Cdd:cd14073    85 GGELYDYISERRRLPERE-------ARRIfRQIVSAVH---YCHKN---GVVHRDLKLENILLDQNGNAKIADFGLSNL- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 271 pdmaarLHSTRVLGTFG----YHAPEyAMTGQLTQ--KSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14073   151 ------YSKDKLLQTFCgsplYASPE-IVNGTPYQgpEVDCWSLGVLLYTLVYGTMPFD 202
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
119-316 4.72e-17

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 80.78  E-value: 4.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHDN---FVELFGYCVEGNFR-ILAYEFATMGS 194
Cdd:cd14056     3 IGKGRYGEVWLGKYR-GEKVAVKIFSSRDEDSWFRE--TEIYQTVMLRHENilgFIAADIKSTGSWTQlWLITEYHEHGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKV-----QPAVIHRDIRSSNVLLFEDFKAKIADFNL--- 266
Cdd:cd14056    80 LYDYLQRN----------TLDTEEALRLAYSAASGLAHLHTEIvgtqgKPAIAHRDLKSKNILVKRDGTCCIADLGLavr 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 267 -SNQSPDMAARLHStRVlGTFGYHAPEyAMTGQLTQKS-------DVYSFGVVLLELL 316
Cdd:cd14056   150 yDSDTNTIDIPPNP-RV-GTKRYMAPE-VLDDSINPKSfesfkmaDIYSFGLVLWEIA 204
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
118-317 4.98e-17

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 80.21  E-value: 4.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATL--KDGKAV--AVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCvegnfriLAYEFATMG 193
Cdd:cd05058     2 VIGKGHFGCVYHGTLidSDGQKIhcAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGIC-------LPSEGSPLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHG--RKGVQGAQPGPTLDwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSP 271
Cdd:cd05058    75 VLPYMKHGdlRNFIRSETHNPTVK--DLIGFGLQVAKGMEYLASK---KFVHRDLAARNCMLDESFTVKVADFGLARDIY 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 272 D---------MAARLhstrvlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05058   150 DkeyysvhnhTGAKL-------PVKWMALESLQTQKFTTKSDVWSFGVLLWELMT 197
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
112-316 5.21e-17

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: 80.23  E-value: 5.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKL---DNAAEPEsnvefltqVSRVSKLKHDNFVELFG------YCVEGN 181
Cdd:cd14047     7 DFKEIELIGSGGFGQVFKAKHRiDGKTYAIKRVklnNEKAERE--------VKALAKLDHPNIVRYNGcwdgfdYDPETS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 182 FR----------ILAYEFATMGSLHDILHGRKGVQgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNV 251
Cdd:cd14047    79 SSnssrsktkclFIQMEFCEKGTLESWIEKRNGEK-------LDKVLALEIFEQITKGVEYIHSK---KLIHRDLKPSNI 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 252 LLFEDFKAKIADFNLSNQspdMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELL 316
Cdd:cd14047   149 FLVDTGKVKIGDFGLVTS---LKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
119-331 6.81e-17

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 79.90  E-value: 6.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA-VAVKKLDNA-AEPESNVEFLT-QVSRVSKLKHDNFVELFgYCVEgnfrilayefATMGSL 195
Cdd:cd14164     8 IGEGSFSKVKLATSQKYCCkVAIKIVDRRrASPDFVQKFLPrELSILRRVNHPNIVQMF-ECIE----------VANGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHgrkgvqgAQPGPTLDWIQRV-RIAVDAARGL--------EYLHEKvqpAVIHRDIRSSNVLLF-EDFKAKIADFN 265
Cdd:cd14164    77 YIVME-------AAATDLLQKIQEVhHIPKDLARDMfaqmvgavNYLHDM---NIVHRDLKCENILLSaDDRKIKIADFG 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 266 LSNQS---PDMaarlhSTRVLGTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGRKPVDHT---MPRGQQ 331
Cdd:cd14164   147 FARFVedyPEL-----STTFCGSRAYTPPEVILgTPYDPKKYDVWSLGVVLYVMVTGTMPFDETnvrRLRLQQ 214
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
119-319 9.53e-17

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: 79.83  E-value: 9.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKK--LDNAAE--PESNvefLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMg 193
Cdd:cd07829     7 LGEGTYGVVYKAKdKKTGEIVALKKirLDNEEEgiPSTA---LREISLLKELKHPNIVKLLDVIHTENKLYLVFEYCDQ- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRkgvqgaQPGPTLDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqspdm 273
Cdd:cd07829    83 DLKKYLDKR------PGPLPPNLIKS--IMYQLLRGLAYCHSH---RILHRDLKPQNLLINRDGVLKLADFGL------- 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 274 aARLHS------TRVLGTFGYHAPEYAMtGQLTQKS--DVYSFGVVLLELLTGR 319
Cdd:cd07829   145 -ARAFGiplrtyTHEVVTLWYRAPEILL-GSKHYSTavDIWSVGCIFAELITGK 196
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
119-360 1.10e-16

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: 79.08  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLD-NAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVE-GNFRILAyEFATMGSL 195
Cdd:cd08218     8 IGEGSFGKALLVKSKeDGKQYVIKEINiSKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEEnGNLYIVM-DYCDGGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQgAQPGPTLDWIqrvriaVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqspdmAA 275
Cdd:cd08218    87 YKRINAQRGVL-FPEDQILDWF------VQLCLALKHVHDR---KILHRDIKSQNIFLTKDGIIKLGDFGI-------AR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 276 RLHSTRVL-----GTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTgrkpVDHTMPRGQqslvtwatprlsedkVKQCV 350
Cdd:cd08218   150 VLNSTVELartciGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCT----LKHAFEAGN---------------MKNLV 210
                         250
                  ....*....|
gi 1032291014 351 DPKLKGEYPP 360
Cdd:cd08218   211 LKIIRGSYPP 220
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
112-340 1.12e-16

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: 78.96  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNA-AEPESNVEFLTQVSRVSKLK-HDNFVELFGYCVEGNFRILAYE 188
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKvDGCLYAVKKSKKPfRGPKERARALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHDILhgrkgvQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNlsn 268
Cdd:cd13997    81 LCENGSLQDAL------EELSPISKLSEAEVWDLLLQVALGLAFIHSK---GIVHLDIKPDNIFISNKGTCKIGDFG--- 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 269 qspdMAARLHSTRVL--GTFGYHAPEY-AMTGQLTQKSDVYSFGVVLLELLTGRKpvdhtMPRGQQSlvtWATPR 340
Cdd:cd13997   149 ----LATRLETSGDVeeGDSRYLAPELlNENYTHLPKADIFSLGVTVYEAATGEP-----LPRNGQQ---WQQLR 211
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
119-356 1.12e-16

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 79.68  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFlTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06657    28 IGEGSTGIVCIATVKSsGKLVAVKKMDLRKQQRRELLF-NEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 IL-HGRKGVQgaqpgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd06657   107 IVtHTRMNEE-----------QIAAVCLAVLKALSVLHAQ---GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 277 LHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP-RGQQSLVTWATPRLsedKVKQCVDPKLK 355
Cdd:cd06657   173 RKS--LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPlKAMKMIRDNLPPKL---KNLHKVSPSLK 247

                  .
gi 1032291014 356 G 356
Cdd:cd06657   248 G 248
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
106-345 1.37e-16

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 79.76  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 106 LKEKTDNFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHD-NFVELFGYCVEGN-- 181
Cdd:cd06637     1 LRDPAGIFELVELVGNGTYGQVYKGRhVKTGQLAAIKVMDVTGDEEEEIK--QEINMLKKYSHHrNIATYYGAFIKKNpp 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 182 ----FRILAYEFATMGSLHDILHGRKGVQGAQpgptlDWIqrVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDF 257
Cdd:cd06637    79 gmddQLWLVMEFCGAGSVTDLIKNTKGNTLKE-----EWI--AYICREILRGLSHLH---QHKVIHRDIKGQNVLLTENA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 258 KAKIADFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQ-----KSDVYSFGVVLLELLTGRKPVDHTMPRGQQS 332
Cdd:cd06637   149 EVKLVDFGVSAQLDRTVGRRNT--FIGTPYWMAPEVIACDENPDatydfKSDLWSLGITAIEMAEGAPPLCDMHPMRALF 226
                         250
                  ....*....|....
gi 1032291014 333 LVTW-ATPRLSEDK 345
Cdd:cd06637   227 LIPRnPAPRLKSKK 240
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
111-321 1.53e-16

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: 79.18  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNaaepesnvEFLTQ------VSR----VSKLKHDNFVELFgYCVE 179
Cdd:cd05581     1 NDFKFGKPLGEGSYSTVVLAKEKeTGKEYAIKVLDK--------RHIIKekkvkyVTIekevLSRLAHPGIVKLY-YTFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 180 GNFRI-LAYEFATMGSLHDILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK 258
Cdd:cd05581    72 DESKLyFVLEYAPNGDLLEYIRKYG---------SLDEKCTRFYTAEIVLALEYLHSK---GIIHRDLKPENILLDEDMH 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 259 AKIADF--------NLSNQSPDMAA-------RLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05581   140 IKITDFgtakvlgpDSSPESTKGDAdsqiaynQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPP 217
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
119-323 1.61e-16

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 78.72  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSK-LKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd14072     8 IGKGNFAKVKLARhVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKiLNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DIL--HGRKGVQGAQpgptldwiQRVRIAVDAargLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ-SPDM 273
Cdd:cd14072    88 DYLvaHGRMKEKEAR--------AKFRQIVSA---VQYCHQK---RIVHRDLKAENLLLDADMNIKIADFGFSNEfTPGN 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 274 AarlhstrvLGTF----GYHAPEyamtgqLTQ-------KSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14072   154 K--------LDTFcgspPYAAPE------LFQgkkydgpEVDVWSLGVILYTLVSGSLPFD 200
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
101-351 1.83e-16

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: 79.38  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 101 LSLDELKEKTDNFGSkslIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVeFLTQVSRVSKLKHDNFVELFGYCVE 179
Cdd:cd06654    13 VSVGDPKKKYTRFEK---IGQGASGTVYTAMdVATGQEVAIRQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 180 GNFRILAYEFATMGSLHDILhgrkgvqgaqPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA 259
Cdd:cd06654    89 GDELWVVMEYLAGGSLTDVV----------TETCMDEGQIAAVCRECLQALEFLHSN---QVIHRDIKSDNILLGMDGSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 260 KIADFNLSNQ-SPDMAARlhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP-RGQQSLVTWA 337
Cdd:cd06654   156 KLTDFGFCAQiTPEQSKR---STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNG 232
                         250       260
                  ....*....|....*....|...
gi 1032291014 338 TPRLS---------EDKVKQCVD 351
Cdd:cd06654   233 TPELQnpeklsaifRDFLNRCLE 255
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
134-322 2.08e-16

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: 78.75  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 134 DGKAVAVKKLDNAAEPESNVeFLTQVSRVSKLKHDNFVELFGYCVE-GNFRILAyEFATMGSLHDILHGRKgvqgaqpgP 212
Cdd:cd14045    29 DGRTVAIKKIAKKSFTLSKR-IRKEVKQVRELDHPNLCKFIGGCIEvPNVAIIT-EYCPKGSLNDVLLNED--------I 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 213 TLDWIQRVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSnqspdMAARLHSTRVLGTFG----- 287
Cdd:cd14045    99 PLNWGFRFSFATDIARGMAYLH---QHKIYHGRLKSSNCVIDDRWVCKIADYGLT-----TYRKEDGSENASGYQqrlmq 170
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1032291014 288 -YHAPEYAMT--GQLTQKSDVYSFGVVLLELLTGRKPV 322
Cdd:cd14045   171 vYLPPENHSNtdTEPTQATDVYSYAIILLEIATRNDPV 208
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
119-354 2.10e-16

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 78.49  E-value: 2.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVE-FLT-QVSRVSKLKHDNFVELFGYCVEGNFRI-LAYEFATMGS 194
Cdd:cd14163     8 IGEGTYSKVKEAfSKKHQRKVAIKIIDKSGGPEEFIQrFLPrELQIVERLDHKNIIHVYEMLESADGKIyLVMELAEDGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHD-ILHGrkgvqgaqpGPTLDWIQRV--RIAVDAARgleYLHekvQPAVIHRDIRSSNVLLfEDFKAKIADFNLSNQSP 271
Cdd:cd14163    88 VFDcVLHG---------GPLPEHRAKAlfRQLVEAIR---YCH---GCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 272 DMAARLHSTrVLGTFGYHAPEyAMTG--QLTQKSDVYSFGVVLLELLTGRKPVDHT-MPR---GQQSLVTWAT----PRL 341
Cdd:cd14163   152 KGGRELSQT-FCGSTAYAAPE-VLQGvpHDSRKGDIWSMGVVLYVMLCAQLPFDDTdIPKmlcQQQKGVSLPGhlgvSRT 229
                         250
                  ....*....|...
gi 1032291014 342 SEDKVKQCVDPKL 354
Cdd:cd14163   230 CQDLLKRLLEPDM 242
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
116-321 2.22e-16

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: 78.62  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKDGK----AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILaYEFAT 191
Cdd:cd05056    11 GRCIGEGQFGDVYQGVYMSPEnekiAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENPVWIV-MELAP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKgvqgaqpgptlDWIQRVRI---AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN 268
Cdd:cd05056    90 LGELRSYLQVNK-----------YSLDLASLilyAYQLSTALAYLESK---RFVHRDIAARNVLVSSPDCVKLGDFGLSR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 269 QSPDmAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05056   156 YMED-ESYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKP 208
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
119-347 2.29e-16

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 78.55  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDnaAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd06645    19 IGSGTYGDVYKArNVNTGELAAIKVIK--LEPGEDFAVVQQeIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSLQ 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHgrkgvqgaQPGPtLDWIQRVRIAVDAARGLEYLHEKVQpavIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd06645    97 DIYH--------VTGP-LSESQIAYVSRETLQGLYYLHSKGK---MHRDIKGANILLTDNGHVKLADFGVSAQITATIAK 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 277 LHStrVLGTFGYHAPEYAMT---GQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVT---WATPRLsEDKVK 347
Cdd:cd06645   165 RKS--FIGTPYWMAPEVAAVerkGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTksnFQPPKL-KDKMK 238
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
119-321 2.69e-16

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: 78.36  E-value: 2.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVK-----KLDNAAE-PESNVEFLTQVSRVS-------KLKHDNFVELFGycV----EG 180
Cdd:cd14008     1 LGRGSFGKVKLALdTETGQLYAIKifnksRLRKRREgKNDRGKIKNALDDVRreiaimkKLDHPNIVRLYE--ViddpES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 181 NFRILAYEFATMGSLHDILHGrkgvqgaQPGPTLDwIQRVR-IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA 259
Cdd:cd14008    79 DKLYLVLEYCEGGPVMELDSG-------DRVPPLP-EETARkYFRDLVLGLEYLHEN---GIVHRDIKPENLLLTADGTV 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 260 KIADFNLSNQSPDMAARLhsTRVLGTFGYHAPEyAMTGQLTQKS----DVYSFGVVLLELLTGRKP 321
Cdd:cd14008   148 KISDFGVSEMFEDGNDTL--QKTAGTPAFLAPE-LCDGDSKTYSgkaaDIWALGVTLYCLVFGRLP 210
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
101-321 2.78e-16

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: 78.57  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 101 LSLDELKEKTD--NFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKlKHD--NFVELFG 175
Cdd:cd06618     3 LTIDGKKYKADlnDLENLGEIGSGTCGQVYKMRhKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLK-SHDcpYIVKCYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 176 YCV-EGNFRIlAYEFatMGSLHDILHGRkgVQGAQPGPTLDwiqrvRIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLLF 254
Cdd:cd06618    82 YFItDSDVFI-CMEL--MSTCLDKLLKR--IQGPIPEDILG-----KMTVSIVKALHYLKEKHG--VIHRDVKPSNILLD 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 255 EDFKAKIADFNLSNQSPDMAARlhsTRVLGTFGYHAPEY---AMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06618   150 ESGNVKLCDFGISGRLVDSKAK---TRSAGCAAYMAPERidpPDNPKYDIRADVWSLGISLVELATGQFP 216
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
119-321 3.21e-16

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: 77.56  E-value: 3.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSR--VSKLKHDNFVELFgycvegnfrilaYEFATMGSL 195
Cdd:cd05123     1 LGKGSFGKVLLVRKKDtGKLYAMKVLRKKEIIKRKEVEHTLNERniLERVNHPFIVKLH------------YAFQTEEKL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILhgrkgvQGAQPGPTLDWIQRV-RIAVDAAR--------GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd05123    69 YLVL------DYVPGGELFSHLSKEgRFPEERARfyaaeivlALEYLHSL---GIIYRDLKPENILLDSDGHIKLTDFGL 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 267 SNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05123   140 AKELSSDGDRTYT--FCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPP 192
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
109-323 3.43e-16

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: 78.91  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 109 KTDNFGSKSLIGEGSYGRAYYAT-LKDGKA----VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFR 183
Cdd:cd05108     5 KETEFKKIKVLGSGAFGTVYKGLwIPEGEKvkipVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 184 ILAyEFATMGSLHDILHGRKGVQGAQpgPTLDWiqrvriAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd05108    85 LIT-QLMPFGCLLDYVREHKDNIGSQ--YLLNW------CVQIAKGMNYLEDR---RLVHRDLAARNVLVKTPQHVKITD 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 264 FNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVD 323
Cdd:cd05108   153 FGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYD 213
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
119-324 3.71e-16

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: 78.11  E-value: 3.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDG---KAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd05087     5 IGHGWFGKVFLGEVNSGlssTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLGDL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQGAQPGP-TLDwiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd05087    85 KGYLRSCRAAESMAPDPlTLQ-----RMACEVACGLLHLHRN---NFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKED 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 275 ARLHSTRVLGTFGYHAPEYA--MTGQL-----TQKSDVYSFGVVLLELLT-GRKPVDH 324
Cdd:cd05087   157 YFVTADQLWVPLRWIAPELVdeVHGNLlvvdqTKQSNVWSLGVTIWELFElGNQPYRH 214
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
119-321 3.90e-16

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 78.14  E-value: 3.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATL------KDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd05091    14 LGEDRFGKVYKGHLfgtapgEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCSH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDIL-----HGRKGVQGAQP--GPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd05091    94 GDLHEFLvmrspHSDVGSTDDDKtvKSTLEPADFLHIVTQIAAGMEYLSSH---HVVHKDLATRNVLVFDKLNVKISDLG 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 266 LSNQ--SPD----MAARLHSTRvlgtfgYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05091   171 LFREvyAADyyklMGNSLLPIR------WMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQP 227
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
119-327 3.93e-16

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: 78.17  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06640    12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQeITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSALD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgaQPGPtLDWIQRVRIAVDAARGLEYLHEKVQpavIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmaARL 277
Cdd:cd06640    92 LL---------RAGP-FDEFQIATMLKEILKGLDYLHSEKK---IHRDIKAANVLLSEQGDVKLADFGVAGQLTD--TQI 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 278 HSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd06640   157 KRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHP 206
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
119-321 3.93e-16

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: 77.72  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDG-KAVAVKKLDNAAEPEsnvefLTQVSRVS-KLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTiEFVAIKCVDKSKRPE-----VLNEVRLThELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILhgrkgvqgAQPG--PTldwiQRVR-IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDM 273
Cdd:cd14010    83 TLL--------RQDGnlPE----SSVRkFGRDLVRGLHYIHSK---GIIYCDLKPSNILLDGNGTLKLSDFGLARREGEI 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 274 AARLHS--------------TRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14010   148 LKELFGqfsdegnvnkvskkQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPP 209
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
119-343 4.22e-16

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: 78.16  E-value: 4.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFlTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06658    30 IGEGSTGIVCIATEKhTGKQVAVKKMDLRKQQRRELLF-NEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 IL-HGRKGVQgaqpgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd06658   109 IVtHTRMNEE-----------QIATVCLSVLRALSYLHNQ---GVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPK 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 277 LHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP-RGQQSLVTWATPRLSE 343
Cdd:cd06658   175 RKS--LVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPlQAMRRIRDNLPPRVKD 240
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
116-317 5.02e-16

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 78.09  E-value: 5.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYY-------------ATLKDGKA--VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEG 180
Cdd:cd05097    10 KEKLGEGQFGEVHLceaeglaeflgegAPEFDGQPvlVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 181 NFRILAYEFATMGSLHDILHGRK---GVQGAQPGPTLDWIQRVRIAVDAARGLEYLhekVQPAVIHRDIRSSNVLLFEDF 257
Cdd:cd05097    90 DPLCMITEYMENGDLNQFLSQREiesTFTHANNIPSVSIANLLYMAVQIASGMKYL---ASLNFVHRDLATRNCLVGNHY 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 258 KAKIADFNLSNQ--SPDMaARLHSTRVLgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05097   167 TIKIADFGMSRNlySGDY-YRIQGRAVL-PIRWMAWESILLGKFTTASDVWAFGVTLWEMFT 226
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
103-327 5.61e-16

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 77.74  E-value: 5.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 103 LDELKEKTDNFGSKSLIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKlKHDNFVELFGY----- 176
Cdd:cd06638    10 FDSFPDPSDTWEIIETIGKGTYGKVFKVlNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALS-DHPNVVKFYGMyykkd 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 177 CVEGNFRILAYEFATMGSLHDILHG--RKGVQGAQPgpTLDWIQRvriavDAARGLEYLHEKvqpAVIHRDIRSSNVLLF 254
Cdd:cd06638    89 VKNGDQLWLVLELCNGGSVTDLVKGflKRGERMEEP--IIAYILH-----EALMGLQHLHVN---KTIHRDVKGNNILLT 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 255 EDFKAKIADFNLSNQSpdMAARLHSTRVLGTFGYHAPEY-AMTGQL----TQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd06638   159 TEGGVKLVDFGVSAQL--TSTRLRRNTSVGTPFWMAPEViACEQQLdstyDARCDVWSLGITAIELGDGDPPLADLHP 234
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
118-321 6.58e-16

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: 77.01  E-value: 6.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLD---NAAEPESNVEFL-TQVSRVSKLKHDNFVELFGyCVEGNFRILAY-EFAT 191
Cdd:cd06625     7 LLGQGAFGQVYLCYDADtGRELAVKQVEidpINTEASKEVKALeCEIQLLKNLQHERIVQYYG-CLQDEKSLSIFmEYMP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILhgrkgvqgAQPGPTLDWIQRvRIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNLSN--Q 269
Cdd:cd06625    86 GGSVKDEI--------KAYGALTENVTR-KYTRQILEGLAYLHSNM---IVHRDIKGANILRDSNGNVKLGDFGASKrlQ 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 270 SPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06625   154 TICSSTGMKS--VTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPP 203
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
119-322 7.77e-16

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 76.99  E-value: 7.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDnaAEPESNVEFLTQ-VSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd06646    17 VGSGTYGDVYKArNLHTGELAAVKIIK--LEPGDDFSLIQQeIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQ 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHgrkgvqgaQPGPtLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd06646    95 DIYH--------VTGP-LSELQIAYVCRETLQGLAYLHSK---GKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 277 LHStrVLGTFGYHAPEYAM---TGQLTQKSDVYSFGVVLLELLTGRKPV 322
Cdd:cd06646   163 RKS--FIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIELAELQPPM 209
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
118-323 7.77e-16

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: 77.41  E-value: 7.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGKAV----AVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAyEFATM 192
Cdd:cd05110    14 VLGSGAFGTVYKGIwVPEGETVkipvAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVT-QLMPH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGAQpgPTLDWiqrvriAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPD 272
Cdd:cd05110    93 GCLLDYVHEHKDNIGSQ--LLLNW------CVQIAKGMMYLEER---RLVHRDLAARNVLVKSPNHVKITDFGLARLLEG 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 273 MAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVD 323
Cdd:cd05110   162 DEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYD 213
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
101-327 7.80e-16

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 77.35  E-value: 7.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 101 LSLDELKEKTDNFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFltQVSRVSKLKHD-NFVELFGYCV 178
Cdd:cd06636     6 IDLSALRDPAGIFELVEVVGNGTYGQVYKGRhVKTGQLAAIKVMDVTEDEEEEIKL--EINMLKKYSHHrNIATYYGAFI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 179 E------GNFRILAYEFATMGSLHDILHGRKGVQGAQpgptlDWIqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVL 252
Cdd:cd06636    84 KksppghDDQLWLVMEFCGAGSVTDLVKNTKGNALKE-----DWI--AYICREILRGLAHLHAH---KVIHRDIKGQNVL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 253 LFEDFKAKIADFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQ-----LTQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd06636   154 LTENAEVKLVDFGVSAQLDRTVGRRNT--FIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHP 231
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
101-341 7.82e-16

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: 77.45  E-value: 7.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 101 LSLDELKEKTDNFGSkslIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVeFLTQVSRVSKLKHDNFVELFGYCVE 179
Cdd:cd06656    12 VSVGDPKKKYTRFEK---IGQGASGTVYTAiDIATGQEVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 180 GNFRILAYEFATMGSLHDILhgrkgvqgaqPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA 259
Cdd:cd06656    88 GDELWVVMEYLAGGSLTDVV----------TETCMDEGQIAAVCRECLQALDFLHSN---QVIHRDIKSDNILLGMDGSV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 260 KIADFNLSNQ-SPDMAARlhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP-RGQQSLVTWA 337
Cdd:cd06656   155 KLTDFGFCAQiTPEQSKR---STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNG 231

                  ....
gi 1032291014 338 TPRL 341
Cdd:cd06656   232 TPEL 235
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
118-321 8.57e-16

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: 76.70  E-value: 8.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGKAVAVKKL----DNAAEPESNVEFLT-QVSRVSKLKHDNFVELFGYCVEG-NFRILAyEFA 190
Cdd:cd06630     7 LLGTGAFSSCYQARdVKTGTLMAVKQVsfcrNSSSEQEEVVEAIReEIRMMARLNHPNIVRMLGATQHKsHFNIFV-EWM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHgrkgvqgaQPGPTLDWIQrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLfeDF---KAKIADFNls 267
Cdd:cd06630    86 AGGSVASLLS--------KYGAFSENVI-INYTLQILRGLAYLHDN---QIIHRDLKGANLLV--DStgqRLRIADFG-- 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 268 nqspdMAARLHS--TRV-------LGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06630   150 -----AAARLASkgTGAgefqgqlLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPP 207
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
116-395 9.40e-16

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: 76.94  E-value: 9.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLK-DGK---AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAT 191
Cdd:cd05063    10 QKVIGAGEFGEVFRGILKmPGRkevAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYME 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSP 271
Cdd:cd05063    90 NGALDKYLRDHDG--------EFSSYQLVGMLRGIAAGMKYLSDM---NYVHRDLAARNILVNSNLECKVSDFGLSRVLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 272 DMAARLHSTrvlgTFG-----YHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVdhtmprgqqslvtWatpRLSEDK 345
Cdd:cd05063   159 DDPEGTYTT----SGGkipirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPY-------------W---DMSNHE 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 346 VKQCVDPKLKGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPLL 395
Cdd:cd05063   219 VMKAINDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL 268
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
118-315 1.17e-15

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 76.75  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHDNFVELFGYCVEGNFR----ILAYEFATMG 193
Cdd:cd14144     2 SVGKGRYGEVWKGKWR-GEKVAVKIFFTTEEASWFRE--TEIYQTVLMRHENILGFIAADIKGTGSwtqlYLITDYHENG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKV-----QPAVIHRDIRSSNVLLFEDFKAKIADFNLsn 268
Cdd:cd14144    79 SLYDFLRGN----------TLDTQSMLKLAYSAACGLAHLHTEIfgtqgKPAIAHRDIKSKNILVKKNGTCCIADLGL-- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 269 qspdmAARLHS----------TRVlGTFGYHAPEyAMTGQLTQKS-------DVYSFGVVLLEL 315
Cdd:cd14144   147 -----AVKFISetnevdlppnTRV-GTKRYMAPE-VLDESLNRNHfdaykmaDMYSFGLVLWEI 203
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
138-324 1.81e-15

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 76.22  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 138 VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGV-QGAQP--GPTL 214
Cdd:cd05051    49 VAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAEtQGASAtnSKTL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 215 DWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ--SPDMAaRLHSTRVLgTFGYHAPE 292
Cdd:cd05051   129 SYGTLLYMATQIASGMKYLESL---NFVHRDLATRNCLVGPNYTIKIADFGMSRNlySGDYY-RIEGRAVL-PIRWMAWE 203
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1032291014 293 YAMTGQLTQKSDVYSFGVVLLELLT--GRKPVDH 324
Cdd:cd05051   204 SILLGKFTTKSDVWAFGVTLWEILTlcKEQPYEH 237
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
119-321 1.97e-15

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: 76.18  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFlTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd06659    29 IGEGSTGVVCIAREKhSGRQVAVKMMDLRKQQRRELLF-NEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgAQPGPTLDWIQRVRIAVDAArgLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ-SPDMAAR 276
Cdd:cd06659   108 IV--------SQTRLNEEQIATVCEAVLQA--LAYLHSQ---GVIHRDIKSDSILLTLDGRVKLSDFGFCAQiSKDVPKR 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1032291014 277 lhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06659   175 ---KSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPP 216
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
165-326 2.03e-15

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: 76.22  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 165 LKHDNFVELFGYCVEG-NFRI---LAYEFATMGSLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKV--- 237
Cdd:cd14140    46 MKHENLLQFIAAEKRGsNLEMelwLITAFHDKGSLTDYLKGN----------IVSWNELCHIAETMARGLSYLHEDVprc 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 238 -----QPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEyAMTGQLT-QKS-----DVY 306
Cdd:cd14140   116 kgeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPE-VLEGAINfQRDsflriDMY 194
                         170       180
                  ....*....|....*....|....
gi 1032291014 307 SFGVVLLELLTGRK----PVDHTM 326
Cdd:cd14140   195 AMGLVLWELVSRCKaadgPVDEYM 218
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
118-395 2.19e-15

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: 75.68  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGKA---VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd05065    11 VIGAGEFGEVCRGRLKlPGKReifVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDM 273
Cdd:cd05065    91 ALDSFLRQNDG--------QFTVIQLVGMLRGIAAGMKYLSEM---NYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 274 AARLHSTRVLG---TFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVdhtmprgqqslvtWatpRLSEDKVKQC 349
Cdd:cd05065   160 TSDPTYTSSLGgkiPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY-------------W---DMSNQDVINA 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1032291014 350 VDPKLKGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPLL 395
Cdd:cd05065   224 IEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
219-321 2.26e-15

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: 75.37  E-value: 2.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 219 RVRI-AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmaaRLHSTRVLGTFGYHAPEYAMTG 297
Cdd:cd05578   101 TVKFyICEIVLALDYLHSK---NIIHRDIKPDNILLDEQGHVHITDFNIATKLTD---GTLATSTSGTKPYMAPEVFMRA 174
                          90       100
                  ....*....|....*....|....
gi 1032291014 298 QLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05578   175 GYSFAVDWWSLGVTAYEMLRGKRP 198
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
119-323 2.27e-15

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 75.30  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd05113    12 LGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSED--EFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LhgRKGVQGAQPgptldwIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAarlH 278
Cdd:cd05113    90 L--REMRKRFQT------QQLLEMCKDVCEAMEYLESK---QFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDE---Y 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 279 STRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVD 323
Cdd:cd05113   156 TSSVGSKFpvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYE 203
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
119-321 2.35e-15

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 75.81  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA---VAVKKLDNAAEPESNVE-FLTQVSRVSKLKHDNFVELFGYCVEGNFR------ILAYE 188
Cdd:cd05075     8 LGEGEFGSVMEGQLNQDDSvlkVAVKTMKIAICTRSEMEdFLSEAVCMKEFDHPNVMRLIGVCLQNTESegypspVVILP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHD-ILHGRKGVQGAQ-PGPTLdwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd05075    88 FMKHGDLHSfLLYSRLGDCPVYlPTQML-----VKFMTDIASGMEYLSSK---NFIHRDLAARNCMLNENMNVCVADFGL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 267 S----NQSPDMAARLHSTRVlgtfGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05075   160 SkkiyNGDYYRQGRISKMPV----KWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTP 215
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
119-327 2.37e-15

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: 75.59  E-value: 2.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLdnaaePESNVEFLTQVSRV--------SKLKHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd05611     4 ISKGAFGSVYLAKKRsTGDYFAIKVL-----KKSDMIAKNQVTNVkaeraimmIQGESPYVAKLYYSFQSKDYLYLVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHgrkgVQGAQPgptLDWIQRVriAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ 269
Cdd:cd05611    79 LNGGDCASLIK----TLGGLP---EDWAKQY--IAEVVLGVEDLH---QRGIIHRDIKPENLLIDQTGHLKLTDFGLSRN 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 270 SpdmAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd05611   147 G---LEKRHNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETP 201
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
119-315 2.48e-15

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 75.84  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFG-YCVEGNFRILAyEFATMGSLHD 197
Cdd:cd06644    20 LGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGaFYWDGKLWIMI-EFCPGGAVDA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 I-LHGRKGVQGAQpgptldwIQRV-RIAVDAargLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAA 275
Cdd:cd06644    99 ImLELDRGLTEPQ-------IQVIcRQMLEA---LQYLHSM---KIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQ 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1032291014 276 RLHStrVLGTFGYHAPEYAMTGQLTQ-----KSDVYSFGVVLLEL 315
Cdd:cd06644   166 RRDS--FIGTPYWMAPEVVMCETMKDtpydyKADIWSLGITLIEM 208
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
221-322 2.94e-15

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 75.94  E-value: 2.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 221 RIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPD-MAarlhsTRVLGTFGYHAPEYAMTGQL 299
Cdd:cd06615   103 KISIAVLRGLTYLREKHK--IMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDsMA-----NSFVGTRSYMSPERLQGTHY 175
                          90       100
                  ....*....|....*....|...
gi 1032291014 300 TQKSDVYSFGVVLLELLTGRKPV 322
Cdd:cd06615   176 TVQSDIWSLGLSLVEMAIGRYPI 198
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
119-324 3.33e-15

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: 75.32  E-value: 3.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVA---VKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd05042     3 IGNGWFGKVLLGEIYSGTSVAqvvVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILhgRKGVQGAQPGPTLDWIQrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAA 275
Cdd:cd05042    83 KAYL--RSEREHERGDSDTRTLQ--RMACEVAAGLAHLHKL---NFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKEDY 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 276 RLHSTRVLGTFGYHAPEYA-------MTGQLTQKSDVYSFGVVLLELLT-GRKPVDH 324
Cdd:cd05042   156 IETDDKLWFPLRWTAPELVtefhdrlLVVDQTKYSNIWSLGVTLWELFEnGAQPYSN 212
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
135-317 3.44e-15

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: 75.32  E-value: 3.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 135 GKAVAVKKLD-NAAEPESNVefLTQVSRVSKLKHDNFVELFGYCVE-GNFRILAyEFATMGSLHDILhgrkgvqgAQPGP 212
Cdd:cd14042    30 GNLVAIKKVNkKRIDLTREV--LKELKHMRDLQHDNLTRFIGACVDpPNICILT-EYCPKGSLQDIL--------ENEDI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 213 TLDWIQRVRIAVDAARGLEYLHEKVqpAVIHRDIRSSNVLLFEDFKAKIADFNL----SNQSPDMAARLHSTRVLGTfgy 288
Cdd:cd14042    99 KLDWMFRYSLIHDIVKGMHYLHDSE--IKSHGNLKSSNCVVDSRFVLKITDFGLhsfrSGQEPPDDSHAYYAKLLWT--- 173
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1032291014 289 hAPEY----AMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd14042   174 -APELlrdpNPPPPGTQKGDVYSFGIILQEIAT 205
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
112-316 3.46e-15

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: 75.30  E-value: 3.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEG------NFRI 184
Cdd:cd14048     7 DFEPIQCLGRGGFGVVFEAKNKvDDCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERppegwqEKMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYEFATMG-----SLHDILHGRKGVQGAQPGPTLDWIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA 259
Cdd:cd14048    87 EVYLYIQMQlcrkeNLKDWMNRRCTMESRELFVCLNIFKQI------ASAVEYLHSK---GLIHRDLKPSNVFFSLDDVV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 260 KIADFNLSN------------QSPDMAARlHSTRVlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELL 316
Cdd:cd14048   158 KVGDFGLVTamdqgepeqtvlTPMPAYAK-HTGQV-GTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
119-327 4.32e-15

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: 74.77  E-value: 4.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRA-YYATLKDGKAVAVKKLD--NAAEPESNvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd08221     8 LGRGAFGEAvLYRKTEDNSLVVWKEVNlsRLSEKERR-DALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HD-ILHgrkgvqgaQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpDMA 274
Cdd:cd08221    87 HDkIAQ--------QKNQLFPEEVVLWYLYQIVSAVSHIHKA---GILHRDIKTLNIFLTKADLVKLGDFGISKVL-DSE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 275 ARLHSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd08221   155 SSMAES-IVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNP 206
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
118-317 4.36e-15

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 74.97  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK--DG--KAVAVK--KLDNAAEPESNvEFLTQVSRVSKLKHDNFVELFGYCVE-GNFRI----LA 186
Cdd:cd14204    14 VLGEGEFGSVMEGELQqpDGtnHKVAVKtmKLDNFSQREIE-EFLSEAACMKDFNHPNVIRLLGVCLEvGSQRIpkpmVI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLHDILHGRKGVQGAQ--PGPTLdwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd14204    93 LPFMKYGDLHSFLLRSRLGSGPQhvPLQTL-----LKFMIDIALGMEYLSSR---NFLHRDLAARNCMLRDDMTVCVADF 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 265 NLSNQ--SPDM--AARLHSTRVlgtfGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd14204   165 GLSKKiySGDYyrQGRIAKMPV----KWIAVESLADRVYTVKSDVWAFGVTMWEIAT 217
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
119-318 4.92e-15

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 74.62  E-value: 4.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLdnaaepesNVEFLTQVSR-VSKLK----HDNFVELFgyCVE--GNFRILAYEFAT 191
Cdd:cd13982     9 LGYGSEGTIVFRGTFDGRPVAVKRL--------LPEFFDFADReVQLLResdeHPNVIRYF--CTEkdRQFLYIALELCA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MgSLHDILH-GRKGVQGAQPGPtldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLL-----FEDFKAKIADFN 265
Cdd:cd13982    79 A-SLQDLVEsPRESKLFLRPGL-----EPVRLLRQIASGLAHLHSL---NIVHRDLKPQNILIstpnaHGNVRAMISDFG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 266 LSNQSPDMAARLHSTR-VLGTFGYHAPEYAMTG---QLTQKSDVYSFGVVLLELLTG 318
Cdd:cd13982   150 LCKKLDVGRSSFSRRSgVAGTSGWIAPEMLSGStkrRQTRAVDIFSLGCVFYYVLSG 206
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
119-319 5.03e-15

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: 75.10  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKK--LDNAAE--PESNvefLTQVSRVSKLKHDNFVEL----FGYCVEGNFRILAYEF 189
Cdd:cd07845    15 IGEGTYGIVYRArDTTSGEIVALKKvrMDNERDgiPISS---LREITLLLNLRHPNIVELkevvVGKHLDSIFLVMEYCE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILhgrkgvqgaqpgPTLDWIQRVR-IAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNLSN 268
Cdd:cd07845    92 QDLASLLDNM------------PTPFSESQVKcLMLQLLRGLQYLHENF---IIHRDLKVSNLLLTDKGCLKIADFGLAR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 269 QSPDMAArlHSTRVLGTFGYHAPE--YAMTGQlTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07845   157 TYGLPAK--PMTPKVVTLWYRAPEllLGCTTY-TTAIDMWAVGCILAELLAHK 206
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
119-315 5.36e-15

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: 74.68  E-value: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELF-GYCVEGNFRILAyEFATMGSLHD 197
Cdd:cd06643    13 LGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLdAFYYENNLWILI-EFCAGGAVDA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgVQGAQPgPTLDWIQRV-RIAVDAargLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd06643    92 VM-----LELERP-LTEPQIRVVcKQTLEA---LVYLHEN---KIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1032291014 277 LHStrVLGTFGYHAPEYAMTGQLTQ-----KSDVYSFGVVLLEL 315
Cdd:cd06643   160 RDS--FIGTPYWMAPEVVMCETSKDrpydyKADVWSLGVTLIEM 201
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
119-317 5.76e-15

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: 74.58  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRA---YYATLKD--GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVE--GNFRILAYEFAT 191
Cdd:cd05079    12 LGEGHFGKVelcRYDPEGDntGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEFLP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN--Q 269
Cdd:cd05079    92 SGSLKEYLPRNKN--------KINLKQQLKYAVQICKGMDYLGSR---QYVHRDLAARNVLVESEHQVKIGDFGLTKaiE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 270 SPDMAARLHSTRVLGTFGYhAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05079   161 TDKEYYTVKDDLDSPVFWY-APECLIQSKFYIASDVWSFGVTLYELLT 207
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
139-317 5.78e-15

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: 74.74  E-value: 5.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 139 AVKKLDNAAEPESNVEF---LTQVSRVSK-LKHDNFVELFGYCVEGNFRI-LAYEFATMgSLHDILHGRKGVqGAQPGPT 213
Cdd:cd14001    32 AVKKINSKCDKGQRSLYqerLKEEAKILKsLNHPNIVGFRAFTKSEDGSLcLAMEYGGK-SLNDLIEERYEA-GLGPFPA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 214 LDwIQRVriAVDAARGLEYLH-EKvqpAVIHRDIRSSNVLLFEDFKA-KIADFNLSNQ-SPDMAARLHST-RVLGTFGYH 289
Cdd:cd14001   110 AT-ILKV--ALSIARALEYLHnEK---KILHGDIKSGNVLIKGDFESvKLCDFGVSLPlTENLEVDSDPKaQYVGTEPWK 183
                         170       180
                  ....*....|....*....|....*....
gi 1032291014 290 APEYAMTGQL-TQKSDVYSFGVVLLELLT 317
Cdd:cd14001   184 AKEALEEGGViTDKADIFAYGLVLWEMMT 212
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
101-321 5.90e-15

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 74.60  E-value: 5.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 101 LSLDELKEKTDNFGSKSligegsygRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCvEG 180
Cdd:cd05115     5 LLIDEVELGSGNFGCVK--------KGVYKMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVC-EA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 181 NFRILAYEFATMGSLHDILHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAK 260
Cdd:cd05115    76 EALMLVMEMASGGPLNKFLSGKK--------DEITVSNVVELMHQVSMGMKYLEEK---NFVHRDLAARNVLLVNQHYAK 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 261 IADFNLSNQspdMAA--RLHSTRVLGTF--GYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05115   145 ISDFGLSKA---LGAddSYYKARSAGKWplKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKP 207
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
113-314 5.97e-15

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: 74.38  E-value: 5.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRAYYATLKD--GKAVAVKKLD-NAAEPESNVEFLTQVS---RVSKLKHDNFVELFGYCVEGNFRILA 186
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERVptGKVYAVKKLKpNYAGAKDRLRRLEEVSilrELTLDGHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLHDIL--HGRKGVqgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd14052    82 TELCENGSLDVFLseLGLLGR--------LDEFRVWKILVELSLGLRFIHDH---HFVHLDLKPANVLITFEGTLKIGDF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 265 NLSNQSPD-MAARLHSTRVlgtfgYHAPEYAMTGQLTQKSDVYSFGVVLLE 314
Cdd:cd14052   151 GMATVWPLiRGIEREGDRE-----YIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
119-321 6.04e-15

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: 74.28  E-value: 6.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLdnaaePESNV---EFLTQVSRVSKLK-HDNFVELFGYCVEGN-FRILAYEFATM 192
Cdd:cd13987     1 LGEGTYGKVLLAVHKgSGTKMALKFV-----PKPSTklkDFLREYNISLELSvHPHIIKTYDVAFETEdYYVFAQEYAPY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILhgrkgvqGAQPGPTLDWIQRVRIAVDAArgLEYLHEKvqpAVIHRDIRSSNVLLFE-DF-KAKIADFNLSNqs 270
Cdd:cd13987    76 GDLFSII-------PPQVGLPEERVKRCAAQLASA--LDFMHSK---NLVHRDIKPENVLLFDkDCrRVKLCDFGLTR-- 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 271 pdmaaRLHST--RVLGTFGYHAPEYAMTG-----QLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd13987   142 -----RVGSTvkRVSGTIPYTAPEVCEAKknegfVVDPSIDVWAFGVLLFCCLTGNFP 194
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
118-396 6.06e-15

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: 74.68  E-value: 6.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGK----AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRiLAYEFATM 192
Cdd:cd05109    14 VLGSGAFGTVYKGIwIPDGEnvkiPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQ-LVTQLMPY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGAQPgpTLDWiqrvriAVDAARGLEYLhEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPD 272
Cdd:cd05109    93 GCLLDYVRENKDRIGSQD--LLNW------CVQIAKGMSYL-EEVR--LVHRDLAARNVLVKSPNHVKITDFGLARLLDI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 273 MAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKPVDHTMPRGQQSLVTwATPRLSEdkvkqcvd 351
Cdd:cd05109   162 DETEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPAREIPDLLE-KGERLPQ-------- 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1032291014 352 pklkgeyPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLR 396
Cdd:cd05109   233 -------PPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRMAR 270
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
116-321 7.64e-15

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: 73.92  E-value: 7.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYAT-LKDGKAVAVKKL--DNAAEPESN----------VEFLTQVSRvsklkHDNFVELFGYCVEGNF 182
Cdd:cd13993     5 ISPIGEGAYGVVYLAVdLRTGRKYAIKCLykSGPNSKDGNdfqklpqlreIDLHRRVSR-----HPNIITLHDVFETEVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 183 RILAYEFATMGSLHDILHGRKGVQGAQpgpTLDWiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF-KAKI 261
Cdd:cd13993    80 IYIVLEYCPNGDLFEAITENRIYVGKT---ELIK----NVFLQLIDAVKHCHSL---GIYHRDIKPENILLSQDEgTVKL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 262 ADFNLSNQSP-DMAARLHSTRvlgtfgYHAPE------YAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd13993   150 CDFGLATTEKiSMDFGVGSEF------YMAPEcfdevgRSLKGYPCAAGDIWSLGIILLNLTFGRNP 210
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
118-317 9.27e-15

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: 74.34  E-value: 9.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKA-----VAVK--KLDNAAEPESNVEFLTQVSrvskLKHDNFVELFGYCVEGNFRILAY--- 187
Cdd:cd14055     2 LVGKGRFAEVWKAKLKQNASgqyetVAVKifPYEEYASWKNEKDIFTDAS----LKHENILQFLTAEERGVGLDRQYwli 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 -EFATMGSLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKVQP------AVIHRDIRSSNVLLFEDFKAK 260
Cdd:cd14055    78 tAYHENGSLQDYLTRH----------ILSWEDLCKMAGSLARGLAHLHSDRTPcgrpkiPIAHRDLKSSNILVKNDGTCV 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 261 IADFNLS-----NQSPDMAArlHSTRVlGTFGYHAPEyAMTGQLT-------QKSDVYSFGVVLLELLT 317
Cdd:cd14055   148 LADFGLAlrldpSLSVDELA--NSGQV-GTARYMAPE-ALESRVNledlesfKQIDVYSMALVLWEMAS 212
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
112-321 9.56e-15

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: 73.84  E-value: 9.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKK--LDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYE 188
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARcLLDGRLVALKKvqIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSL-HDILHGRKGVQGAqPGPTLdWIQRVRIAvdaaRGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS 267
Cdd:cd08224    81 LADAGDLsRLIKHFKKQKRLI-PERTI-WKYFVQLC----SALEHMHSK---RIMHRDIKPANVFITANGVVKLGDLGLG 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 268 NQ--SPDMAArlHSTrvLGTFGYHAPE------YAMtgqltqKSDVYSFGVVLLELLTGRKP 321
Cdd:cd08224   152 RFfsSKTTAA--HSL--VGTPYYMSPErireqgYDF------KSDIWSLGCLLYEMAALQSP 203
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
119-324 1.01e-14

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: 73.42  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDN------AAEPEsnVEFLTQVSRVSKlkHDNFVELFG--YCVEGNFRILAYEF 189
Cdd:cd05118     7 IGEGAFGTVWLArDKVTGEKVAIKKIKNdfrhpkAALRE--IKLLKHLNDVEG--HPNIVKLLDvfEHRGGNHLCLVFEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 atMG-SLHDILhgrkgvQGAQPGPTLDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLL-FEDFKAKIADFNLS 267
Cdd:cd05118    83 --MGmNLYELI------KDYPRGLPLDLIKS--YLYQLLQALDFLHSN---GIIHRDLKPENILInLELGQLKLADFGLA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 268 NQSPDmaaRLHSTRVlGTFGYHAPE--YAMTGqLTQKSDVYSFGVVLLELLTGR------KPVDH 324
Cdd:cd05118   150 RSFTS---PPYTPYV-ATRWYRAPEvlLGAKP-YGSSIDIWSLGCILAELLTGRplfpgdSEVDQ 209
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
113-328 1.27e-14

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: 73.50  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRAYYAT--LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFA 190
Cdd:cd14201     8 YSRKDLVGHGAFAVVFKGRhrKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRkgvqGAQPGPTLdwiqRVRIAVDAArGLEYLHEKvqpAVIHRDIRSSNVLL---------FEDFKAKI 261
Cdd:cd14201    88 NGGDLADYLQAK----GTLSEDTI----RVFLQQIAA-AMRILHSK---GIIHRDLKPQNILLsyasrkkssVSGIRIKI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 262 ADFNLSN--QSPDMAARLhstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPR 328
Cdd:cd14201   156 ADFGFARylQSNMMAATL-----CGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQ 219
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
118-321 1.42e-14

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: 73.45  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGKA----VAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRiLAYEFATM 192
Cdd:cd05111    14 VLGSGVFGTVHKGIwIPEGDSikipVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGASLQ-LVTQLLPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGaqPGPTLDWiqrvriAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPD 272
Cdd:cd05111    93 GSLLDHVRQHRGSLG--PQLLLNW------CVQIAKGMYYLEEH---RMVHRNLAARNVLLKSPSQVQVADFGVADLLYP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 273 MAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05111   162 DDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEP 211
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
110-321 1.58e-14

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 73.17  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 110 TDNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDNAA--EPESNVEflTQVSRVSKLKHDNFVELFGYCVEGNFRILA 186
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEVVLAEDKAtGKLVAIKCIDKKAlkGKEDSLE--NEIAVLRKIKHPNIVQLLDIYESKSHLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLHD-ILhgRKGVQGAQPGPTLdwIQRVRIAVDaargleYLHEKvqpAVIHRDIRSSNVLLF---EDFKAKIA 262
Cdd:cd14083    80 MELVTGGELFDrIV--EKGSYTEKDASHL--IRQVLEAVD------YLHSL---GIVHRDLKPENLLYYspdEDSKIMIS 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 263 DFNLS--NQSPDMAArlhstrVLGTFGYHAPEYamtgqLTQKS-----DVYSFGVVLLELLTGRKP 321
Cdd:cd14083   147 DFGLSkmEDSGVMST------ACGTPGYVAPEV-----LAQKPygkavDCWSIGVISYILLCGYPP 201
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
119-321 1.65e-14

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: 73.90  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEP--ESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAtMGSL 195
Cdd:cd06634    23 IGHGSFGAVYFArDVRNNEVVAIKKMSYSGKQsnEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYC-LGSA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKgvqgaQPgptldwIQRVRIAV---DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF-NLSNQSP 271
Cdd:cd06634   102 SDLLEVHK-----KP------LQEVEIAAithGALQGLAYLHSH---NMIHRDVKAGNILLTEPGLVKLGDFgSASIMAP 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 272 dmaarlhSTRVLGTFGYHAPEYAMT---GQLTQKSDVYSFGVVLLElLTGRKP 321
Cdd:cd06634   168 -------ANSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIE-LAERKP 212
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
105-321 1.95e-14

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 72.83  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 105 ELKEKTDNFGSKSLIGEGSYGRAYYA-TLKDGKAVAVKKLdnaaePE---SNVEFL-TQVSRVSKLKHDNFVELFGYCVE 179
Cdd:cd06624     2 EYEYEYDESGERVVLGKGTFGVVYAArDLSTQVRIAIKEI-----PErdsREVQPLhEEIALHSRLSHKNIVQYLGSVSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 180 GNFRILAYEFATMGSLHDILHGRKGVQGAQPGPTLDWIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLfEDFKA 259
Cdd:cd06624    77 DGFFKIFMEQVPGGSLSALLRSKWGPLKDNENTIGYYTKQI------LEGLKYLHDN---KIVHRDIKGDNVLV-NTYSG 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 260 --KIADFNLSNQspdmAARLH--STRVLGTFGYHAPEYAMTGQ--LTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06624   147 vvKISDFGTSKR----LAGINpcTETFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPP 210
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
111-323 2.08e-14

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


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 72.97  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKDGK-AVAVKKLDNAAEPESNVE--FLTQVSRVSKLKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd14117     6 DDFDIGRPLGKGKFGNVYLAREKQSKfIVALKVLFKSQIEKEGVEhqLRREIEIQSHLRHPNILRLYNYFHDRKRIYLIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILhgrkgvqgaQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS 267
Cdd:cd14117    86 EYAPRGELYKEL---------QKHGRFDEQRTATFMEELADALHYCHEK---KVIHRDIKPENLLMGYKGELKIADFGWS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 268 NQSPDMAARlhstRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14117   154 VHAPSLRRR----TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFE 205
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
119-321 2.12e-14

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: 72.78  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYG----------RAYYATlkdgKAVAVKKL-------------DNAAEPESNVEFLTQVSR----VSKLKHDNFV 171
Cdd:cd14118     2 IGKGSYGivklayneedNTLYAM----KILSKKKLlkqagffrrppprRKPGALGKPLDPLDRVYReiaiLKKLDHPNVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 172 ELFGYC---VEGNFrILAYEFATMGSLHDIlhgrkgvqgaqPGP-TLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIR 247
Cdd:cd14118    78 KLVEVLddpNEDNL-YMVFELVDKGAVMEV-----------PTDnPLSEETARSYFRDIVLGIEYLHYQ---KIIHRDIK 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 248 SSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTrvLGTFGYHAPEyAMTGQLTQKS----DVYSFGVVLLELLTGRKP 321
Cdd:cd14118   143 PSNLLLGDDGHVKIADFGVSNEFEGDDALLSST--AGTPAFMAPE-ALSESRKKFSgkalDIWAMGVTLYCFVFGRCP 217
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
112-328 2.20e-14

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 72.73  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSkSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLtqvsrvSKLKHDNFVELFGYCVEGNFRILAYEFA 190
Cdd:cd13995     6 NIGS-DFIPRGAFGKVYLAQdTKTKKRMACKLIPVEQFKPSDVEIQ------ACFRHENIAELYGALLWEETVHLFMEAG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHgrkgvqgaQPGPTLDWiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLlFEDFKAKIADFNLSNQs 270
Cdd:cd13995    79 EGGSVLEKLE--------SCGPMREF-EIIWVTKHVLKGLDFLHSK---NIIHHDIKPSNIV-FMSTKAVLVDFGLSVQ- 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 271 pdMAARLHSTRVL-GTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPR 328
Cdd:cd13995   145 --MTEDVYVPKDLrGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPR 201
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
119-317 2.27e-14

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: 73.47  E-value: 2.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK---DGKAVAVKKLdnaaepESNVEFLTQVSR--------VSKLKHDNFVELFGYCVEGNFRI--L 185
Cdd:cd07842     8 IGRGTYGRVYKAKRKngkDGKEYAIKKF------KGDKEQYTGISQsacreialLRELKHENVVSLVEVFLEHADKSvyL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILHGRKGVQGAQPGPTLDwiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLL----FEDFKAKI 261
Cdd:cd07842    82 LFDYAEHDLWQIIKFHRQAKRVSIPPSMVK-----SLLWQILNGIHYLHSN---WVLHRDLKPANILVmgegPERGVVKI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 262 ADFNLSN--QSPdMAARLHSTRVLGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLT 317
Cdd:cd07842   154 GDLGLARlfNAP-LKPLADLDPVVVTIWYRAPELLLGARhYTKAIDIWAIGCIFAELLT 211
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
117-321 2.34e-14

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: 72.99  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPES----NVEFLTQVSRVSKLKHDNFVELFG-YCVEGNFRiLAYEFA 190
Cdd:cd07841     6 KKLGEGTYAVVYKARdKETGRIVAIKKIKLGERKEAkdgiNFTALREIKLLQELKHPNIIGLLDvFGHKSNIN-LVFEFM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TmGSLHDILHGRKGVqgAQPGPTLDWIQRvriavdAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ- 269
Cdd:cd07841    85 E-TDLEKVIKDKSIV--LTPADIKSYMLM------TLRGLEYLHSN---WILHRDLKPNNLLIASDGVLKLADFGLARSf 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 270 -SPDmaaRLHSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTgRKP 321
Cdd:cd07841   153 gSPN---RKMTHQVV-TRWYRAPELLFgARHYGVGVDMWSVGCIFAELLL-RVP 201
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
118-321 4.21e-14

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: 71.82  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGK---AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd05066    11 VIGAGEFGEVCSGRLKlPGKreiPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS---NQS 270
Cdd:cd05066    91 SLDAFLRKHDG--------QFTVIQLVGMLRGIASGMKYLSDM---GYVHRDLAARNILVNSNLVCKVSDFGLSrvlEDD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 271 PDMAARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05066   160 PEAAYTTRGGKI--PIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERP 209
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
108-317 4.53e-14

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 72.33  E-value: 4.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 108 EKTDNFGSKSLIGEGSYGRAYYatlkdgkaVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd05095    27 EGMEKFMDKDFALEVSENQPVL--------VAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITDDPLCMIT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILhGRKGVQGAQPGP----TLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd05095    99 EYMENGDLNQFL-SRQQPEGQLALPsnalTVSYSDLRFMAAQIASGMKYLSSL---NFVHRDLATRNCLVGKNYTIKIAD 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 264 FNLSNQ--SPDMaARLHSTRVLgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05095   175 FGMSRNlySGDY-YRIQGRAVL-PIRWMSWESILLGKFTTASDVWAFGVTLWETLT 228
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
119-321 4.61e-14

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: 71.55  E-value: 4.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGK--AVAVKKLDNAAEPESNVE-FLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd14121     3 LGSGTYATVYKAYRKSGAreVVAVKCVSKSSLNKASTEnLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA--KIADFNLSNQspdM 273
Cdd:cd14121    83 SRFIRSRR---------TLPESTVRRFLQQLASALQFLREH---NISHMDLKPQNLLLSSRYNPvlKLADFGFAQH---L 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 274 AARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14121   148 KPNDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAP 195
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
117-321 4.65e-14

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: 71.92  E-value: 4.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKK----LDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYC----VEGNFRI-LA 186
Cdd:cd07838     5 AEIGEGAYGTVYKARdLQDGRFVALKKvrvpLSEEGIPLSTIREIALLKQLESFEHPNVVRLLDVChgprTDRELKLtLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMgSLHDILhgRKGVQGAQPGPTLDWIQRvriavDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd07838    85 FEHVDQ-DLATYL--DKCPKPGLPPETIKDLMR-----QLLRGLDFLHSH---RIVHRDLKPQNILVTSDGQVKLADFGL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 267 snqspdmaARLHS-----TRVLGTFGYHAPEYamtgqLTQKS-----DVYSFGVVLLELLTgRKP 321
Cdd:cd07838   154 --------ARIYSfemalTSVVVTLWYRAPEV-----LLQSSyatpvDMWSVGCIFAELFN-RRP 204
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
165-321 5.02e-14

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: 71.63  E-value: 5.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 165 LKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHgRKGvqgaqpgpTL--DWIQRVRIAVDAArgLEYLHEKvqpAVI 242
Cdd:cd14120    49 LSHENVVALLDCQETSSSVYLVMEYCNGGDLADYLQ-AKG--------TLseDTIRVFLQQIAAA--MKALHSK---GIV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 243 HRDIRSSNVLL---------FEDFKAKIADFNLSN--QSPDMAARLhstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVV 311
Cdd:cd14120   115 HRDLKPQNILLshnsgrkpsPNDIRLKIADFGFARflQDGMMAATL-----CGSPMYMAPEVIMSLQYDAKADLWSIGTI 189
                         170
                  ....*....|
gi 1032291014 312 LLELLTGRKP 321
Cdd:cd14120   190 VYQCLTGKAP 199
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
119-330 6.35e-14

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


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 71.77  E-value: 6.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNV-EFLTQVSRVSKLKHDNFVelfGYCVEGNFRILAYEFATMG--- 193
Cdd:cd14049    14 LGKGGYGKVYKVRNKlDGQYYAIKKILIKKVTKRDCmKVLREVKVLAGLQHPNIV---GYHTAWMEHVQLMLYIQMQlce 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 -SLHDIL-----HGRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLF-EDFKAKIADFNL 266
Cdd:cd14049    91 lSLWDWIvernkRPCEEEFKSAPYTPVDVDVTTKILQQLLEGVTYIHSM---GIVHRDLKPRNIFLHgSDIHVRIGDFGL 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 267 S-----NQSPDMAAR-----LHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLtgrKPVDHTMPRGQ 330
Cdd:cd14049   168 AcpdilQDGNDSTTMsrlngLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---QPFGTEMERAE 238
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
113-344 6.90e-14

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: 71.63  E-value: 6.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRAYYATL------KDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKH-DNFVELFGYCV-EGNFRI 184
Cdd:cd06616     3 FTAEDLKDLGEIGRGAFGTVnkmlhkPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDcPYIVKFYGALFrEGDCWI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 lAYEFAT--MGSLHDILHGRKgvQGAQPGPTLDwiqrvRIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd06616    83 -CMELMDisLDKFYKYVYEVL--DSVIPEEILG-----KIAVATVKALNYLKEELK--IIHRDVKPSNILLDRNGNIKLC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 263 DFNLSNQSPDMAARlhsTRVLGTFGYHAPEYAMTGQLTQ----KSDVYSFGVVLLELLTGRKPVDHTMPRGQQ--SLVTW 336
Cdd:cd06616   153 DFGISGQLVDSIAK---TRDAGCRPYMAPERIDPSASRDgydvRSDVWSLGITLYEVATGKFPYPKWNSVFDQltQVVKG 229

                  ....*...
gi 1032291014 337 ATPRLSED 344
Cdd:cd06616   230 DPPILSNS 237
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
111-317 7.31e-14

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 71.75  E-value: 7.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATL----KDGKA--VAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFR 183
Cdd:cd05055    35 NNLSFGKTLGAGAFGKVVEATAyglsKSDAVmkVAVKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 184 ILAYEFATMGSLHDILHGRKGVqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd05055   115 LVITEYCCYGDLLNFLRRKRES-------FLTLEDLLSFSYQVAKGMAFLASK---NCIHRDLAARNVLLTHGKIVKICD 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 264 FNL-------SNQSPDMAARLhstrvlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05055   185 FGLardimndSNYVVKGNARL-------PVKWMAPESIFNCVYTFESDVWSYGILLWEIFS 238
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
107-321 7.40e-14

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 71.88  E-value: 7.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 107 KEKTDNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLD-NAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCvegNFRI 184
Cdd:cd05619     1 KLTIEDFVLHKMLGKGSFGKVFLAELKgTNQFFAIKALKkDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFC---TFQT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYEFATMgslhDILHGRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd05619    78 KENLFFVM----EYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSK---GIVYRDLKLDNILLDKDGHIKIADF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 265 NLSNQSpdMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05619   151 GMCKEN--MLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSP 205
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
158-326 1.12e-13

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: 70.84  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 158 QVSRVSKLKHDNFVELFGYCVEG-NFRI---LAYEFATMGSLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYL 233
Cdd:cd14141    39 EIYSLPGMKHENILQFIGAEKRGtNLDVdlwLITAFHEKGSLTDYLKAN----------VVSWNELCHIAQTMARGLAYL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 234 HEKV-------QPAVIHRDIRSSNVLLFEDFKAKIADFNLS--NQSPDMAARLHSTrvLGTFGYHAPEyAMTGQLT---- 300
Cdd:cd14141   109 HEDIpglkdghKPAIAHRDIKSKNVLLKNNLTACIADFGLAlkFEAGKSAGDTHGQ--VGTRRYMAPE-VLEGAINfqrd 185
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1032291014 301 --QKSDVYSFGVVLLELLT----GRKPVDHTM 326
Cdd:cd14141   186 afLRIDMYAMGLVLWELASrctaSDGPVDEYM 217
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
119-317 1.15e-13

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: 70.54  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLD---------NAAEPESNVefltqvsrVSKLKHDNFV---ELFGYcvEGNFRIL 185
Cdd:cd08223     8 IGKGSYGEVWLVRHKrDRKQYVIKKLNlknaskrerKAAEQEAKL--------LSKLKHPNIVsykESFEG--EDGFLYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILHGRKGVqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd08223    78 VMGFCEGGDLYTRLKEQKGV-------LLEERQVVEWFVQIAMALQYMHER---NILHRDLKTQNIFLTKSNIIKVGDLG 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 266 ----LSNQSpDMAARLhstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd08223   148 iarvLESSS-DMATTL-----IGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMAT 197
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
117-317 1.26e-13

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: 70.69  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRA---YYATLKD--GKAVAVKKLDNAAePESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFR--ILAYEF 189
Cdd:cd05081    10 SQLGKGNFGSVelcRYDPLGDntGALVAVKQLQHSG-PDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRRslRLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRKGVqgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ 269
Cdd:cd05081    89 LPSGCLRDFLQRHRAR--------LDASRLLLYSSQICKGMEYLGSR---RCVHRDLAARNILVESEAHVKIADFGLAKL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 270 SP-DMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05081   158 LPlDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
118-315 1.28e-13

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: 70.93  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHDNFVELFGY-------CVEgnfRILAYEFA 190
Cdd:cd14142    12 CIGKGRYGEVWRGQWQ-GESVAVKIFSSRDEKSWFRE--TEIYNTVLLRHENILGFIASdmtsrnsCTQ---LWLITHYH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKV-----QPAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd14142    86 ENGSLYDYLQRT----------TLDHQEMLRLALSAASGLVHLHTEIfgtqgKPAIAHRDLKSKNILVKSNGQCCIADLG 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 266 LS---NQSPDMAARLHSTRVlGTFGYHAPEyAMTGQLT-------QKSDVYSFGVVLLEL 315
Cdd:cd14142   156 LAvthSQETNQLDVGNNPRV-GTKRYMAPE-VLDETINtdcfesyKRVDIYAFGLVLWEV 213
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
112-387 1.63e-13

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: 70.06  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLD--NAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYE 188
Cdd:cd08228     3 NFQIEKKIGRGQFSEVYRATcLLDRKPVALKKVQifEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHDILHGRKGVQGAQPGPTLdWiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN 268
Cdd:cd08228    83 LADAGDLSQMIKYFKKQKRLIPERTV-W----KYFVQLCSAVEHMHSR---RVMHRDIKPANVFITATGVVKLGDLGLGR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 269 QSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPvdhtMPRGQQSLVTWAtprlseDKVKQ 348
Cdd:cd08228   155 FFSSKTTAAHS--LVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSP----FYGDKMNLFSLC------QKIEQ 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1032291014 349 CVDPKLKGEYppkAVAKLAAVAALCVQYESEFRPNMSIV 387
Cdd:cd08228   223 CDYPPLPTEH---YSEKLRELVSMCIYPDPDQRPDIGYV 258
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
119-323 1.70e-13

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 70.17  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVK------------KLDNAAEPESNVEFLTQ--VSRVSKLKHDNFVELFGYCVEGNFR 183
Cdd:cd14077     9 IGAGSMGKVKLAKhIRTGEKCAIKiiprasnaglkkEREKRLEKEISRDIRTIreAALSSLLNHPHICRLRDFLRTPNHY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 184 ILAYEFATMGSLHDIL--HGRkgvqgaqpgptLDWIQRVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKI 261
Cdd:cd14077    89 YMLFEYVDGGQLLDYIisHGK-----------LKEKQARKFARQIASALDYLH---RNSIVHRDLKIENILISKSGNIKI 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 262 ADFNLSN-QSPDmaARLHStrVLGTFGYHAPEYAMTGQLT-QKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14077   155 IDFGLSNlYDPR--RLLRT--FCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFD 214
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
116-321 2.72e-13

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 69.52  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFG-YCVEGNFRILAyEFATMG 193
Cdd:cd06619     6 QEILGHGNGGTVYKAYhLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGaFFVENRISICT-EFMDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHdilhgrkgVQGAQPGPTLDwiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDM 273
Cdd:cd06619    85 SLD--------VYRKIPEHVLG-----RIAVAVVKGLTYLWSL---KILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNS 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 274 AARLHstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06619   149 IAKTY----VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFP 192
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
119-321 2.74e-13

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 69.21  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA----TLKdgkAVAVK-----KLDNAAEPESNVEflTQVSRVSKLKHDNFVEL---------------F 174
Cdd:cd14119     1 LGEGSYGKVKEVldteTLC---RRAVKilkkrKLRRIPNGEANVK--REIQILRRLNHRNVIKLvdvlyneekqklymvM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 175 GYCVegnfrilayefatmGSLHDILHgrkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLF 254
Cdd:cd14119    76 EYCV--------------GGLQEMLD-------SAPDKRLPIWQAHGYFVQLIDGLEYLHSQ---GIIHKDIKPGNLLLT 131
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 255 EDFKAKIADFNLSNQSpDMAARLHS-TRVLGTFGYHAPEYAmTGQLT---QKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14119   132 TDGTLKISDFGVAEAL-DLFAEDDTcTTSQGSPAFQPPEIA-NGQDSfsgFKVDIWSAGVTLYNMTTGKYP 200
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
118-321 3.88e-13

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: 68.85  E-value: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEfltqVSR-----VSKLKHDNFVElFGYCVEGNFRI-LAYEFAT 191
Cdd:cd08219     7 VVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVE----DSRkeavlLAKMKHPNIVA-FKESFEADGHLyIVMEYCD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGVQGAQPgPTLDWIQRVRIAVdaarglEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNlsnqsp 271
Cdd:cd08219    82 GGDLMQKIKLQRGKLFPED-TILQWFVQMCLGV------QHIHEK---RVLHRDIKSKNIFLTQNGKVKLGDFG------ 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 272 dmAARLHSTRV------LGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd08219   146 --SARLLTSPGayactyVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHP 199
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
118-315 4.04e-13

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: 68.99  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGKAVAVKKLD-NAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd08220     7 VVGRGAYGTVYLCRRKdDNKLVIIKQIPvEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK-AKIADFNLSNQspdMA 274
Cdd:cd08220    87 FEYIQQRKGS-------LLSEEEILHFFVQILLALHHVHSK---QILHRDLKTQNILLNKKRTvVKIGDFGISKI---LS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1032291014 275 ARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLEL 315
Cdd:cd08220   154 SKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYEL 194
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
119-315 4.77e-13

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: 68.91  E-value: 4.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHDNFVELFGYCVEGNFR----ILAYEFATMGS 194
Cdd:cd14220     3 IGKGRYGEVWMGKWR-GEKVAVKVFFTTEEASWFRE--TEIYQTVLMRHENILGFIAADIKGTGSwtqlYLITDYHENGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGrkgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKV-----QPAVIHRDIRSSNVLLFEDFKAKIADFNLS-- 267
Cdd:cd14220    80 LYDFLKC----------TTLDTRALLKLAYSAACGLCHLHTEIygtqgKPAIAHRDLKSKNILIKKNGTCCIADLGLAvk 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 268 -NQSPDMAARLHSTRVlGTFGYHAPEyAMTGQLTQK-------SDVYSFGVVLLEL 315
Cdd:cd14220   150 fNSDTNEVDVPLNTRV-GTKRYMAPE-VLDESLNKNhfqayimADIYSFGLIIWEM 203
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
118-321 4.85e-13

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 69.18  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK----DGKAVAVKKLDNAAEPESNVE-FLTQVSRVSKLKHDNFVELFGYCVEGNFR------ILA 186
Cdd:cd05074    16 MLGKGEFGSVREAQLKsedgSFQKVAVKMLKADIFSSSDIEeFLREAACMKEFDHPNVIKLIGVSLRSRAKgrlpipMVI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLHDILHGRKgvQGAQPGpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd05074    96 LPFMKHGDLHTFLLMSR--IGEEPF-TLPLQTLVRFMIDIASGMEYLSSK---NFIHRDLAARNCMLNENMTVCVADFGL 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 267 SNQ--SPDMAARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05074   170 SKKiySGDYYRQGCASKL--PVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTP 225
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
118-321 5.15e-13

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


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 69.20  E-value: 5.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGKAVAVKKLD-NAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCvegNFRILAYEFATMgsl 195
Cdd:cd05620     2 VLGKGSFGKVLLAELKgKGEYFAVKALKkDVVLIDDDVECTMVEKRVLALAWENPFLTHLYC---TFQTKEHLFFVM--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 hDILHGRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspDMAA 275
Cdd:cd05620    76 -EFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSK---GIIYRDLKLDNVMLDRDGHIKIADFGMCKE--NVFG 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1032291014 276 RLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05620   150 DNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSP 195
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
118-321 5.29e-13

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: 68.68  E-value: 5.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKA--VAVKKLD--NAA----EPESNVEFLTQVSRVS----KLKHDNFVELFGYCVEGNFRIL 185
Cdd:cd08528     7 LLGSGAFGCVYKVRKKSNGQtlLALKEINmtNPAfgrtEQERDKSVGDIISEVNiikeQLRHPNIVRYYKTFLENDRLYI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILHGRKGVQGAQPGPTLdWiqrvRIAVDAARGLEYLHEkvQPAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd08528    87 VMELIEGAPLGEHFSSLKEKNEHFTEDRI-W----NIFVQMVLALRYLHK--EKQIVHRDLKPNNIMLGEDDKVTITDFG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 266 LSNQSPDMAARLhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd08528   160 LAKQKGPESSKM--TSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPP 213
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
116-319 5.37e-13

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: 69.48  E-value: 5.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNaaePESNVEFLTQVSRVSK----LKHDNFVEL---FGYCVEGNFR--IL 185
Cdd:cd07834     5 LKPIGSGAYGVVCSAYdKRTGRKVAIKKISN---VFDDLIDAKRILREIKilrhLKHENIIGLldiLRPPSPEEFNdvYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFatMGS-LHDILHgrkgvqgaQPGP-TLDWIQRvrIAVDAARGLEYLHEkvqpA-VIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd07834    82 VTEL--METdLHKVIK--------SPQPlTDDHIQY--FLYQILRGLKYLHS----AgVIHRDLKPSNILVNSNCDLKIC 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 263 DFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07834   146 DFGLARGVDPDEDKGFLTEYVVTRWYRAPELLLSSKkYTKAIDIWSVGCIFAELLTRK 203
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
119-318 5.54e-13

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: 68.89  E-value: 5.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLdnaAEPESNVEFLTQVSRVSKL-----KHDNFVELFGYCVEGNFRILAYEFaTM 192
Cdd:cd07832     8 IGEGAHGIVFKAKdRETGETVALKKV---ALRKLEGGIPNQALREIKAlqacqGHPYVVKLRDVFPHGTGFVLVFEY-ML 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKgvqgaQPGPTldwIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPD 272
Cdd:cd07832    84 SSLSEVLRDEE-----RPLTE---AQVKRYMRMLLKGVAYMHAN---RIMHRDLKPANLLISSTGVLKIADFGLARLFSE 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 273 MAARLHSTRVlGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLTG 318
Cdd:cd07832   153 EDPRLYSHQV-ATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNG 198
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
166-318 6.48e-13

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: 68.29  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 166 KHDNFVELFGycvegnfRILAYEFATMGS-----LHDILHgRKGVQGAQPGptLDWIQRVRIAVDAARGLEYLHEKvqpA 240
Cdd:cd13975    56 KHERIVSLHG-------SVIDYSYGGGSSiavllIMERLH-RDLYTGIKAG--LSLEERLQIALDVVEGIRFLHSQ---G 122
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 241 VIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMaarlhSTRVLGTFGYHAPEYaMTGQLTQKSDVYSFGVVLLELLTG 318
Cdd:cd13975   123 LVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMM-----SGSIVGTPIHMAPEL-FSGKYDNSVDVYAFGILFWYLCAG 194
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-321 1.13e-12

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: 67.75  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKDG-KAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTqKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHgRKGVQGAQPGPTLdwIQRVRIAVdaarglEYLHEKvqpAVIHRDIRSSNVLLF---EDFKAKIADFNL 266
Cdd:cd14167    83 VSGGELFDRIV-EKGFYTERDASKL--IFQILDAV------KYLHDM---GIVHRDLKPENLLYYsldEDSKIMISDFGL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 267 SNQspDMAARLHSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14167   151 SKI--EGSGSVMST-ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP 202
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
105-322 1.24e-12

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: 68.16  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 105 ELKEktDNFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDN-AAEPESNVEFLTQVSRVSKLKHDNFVELFG-YCVEGNF 182
Cdd:cd06650     1 ELKD--DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHlEIKPAIRNQIIRELQVLHECNSPYIVGFYGaFYSDGEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 183 RIlAYEFATMGSLHDILhgRKGvqGAQPGPTLDwiqRVRIAVdaARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd06650    79 SI-CMEHMDGGSLDQVL--KKA--GRIPEQILG---KVSIAV--IKGLTYLREKHK--IMHRDVKPSNILVNSRGEIKLC 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 263 DFNLSNQSPDMAArlhsTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPV 322
Cdd:cd06650   147 DFGVSGQLIDSMA----NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPI 202
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
108-319 1.25e-12

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 68.53  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 108 EKTDNFGSKSLIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSK-LKHDNFVELFGYCVEGN---- 181
Cdd:cd07877    14 EVPERYQNLSPVGSGAYGSVCAAfDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKhMKHENVIGLLDVFTPARslee 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 182 FRILAYEFATMGS-LHDILHGRKgvqgaqpgPTLDWIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAK 260
Cdd:cd07877    94 FNDVYLVTHLMGAdLNNIVKCQK--------LTDDHVQFLIYQI--LRGLKYIHSA---DIIHRDLKPSNLAVNEDCELK 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 261 IADFNLSNQSPDmaarlHSTRVLGTFGYHAPEYAMTG-QLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07877   161 ILDFGLARHTDD-----EMTGYVATRWYRAPEIMLNWmHYNQTVDIWSVGCIMAELLTGR 215
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
119-321 1.47e-12

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 67.19  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd05114    12 LGSGLFGVVRLGKWRAQYKVAIKAIREGAMSEE--DFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LHGRKGVqgAQPGPTLDWIQrvriavDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNlsnqspdMAARLH 278
Cdd:cd05114    90 LRQRRGK--LSRDMLLSMCQ------DVCEGMEYLE---RNNFIHRDLAARNCLVNDTGVVKVSDFG-------MTRYVL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 STRVLGTFG------YHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05114   152 DDQYTSSSGakfpvkWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMP 201
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
119-317 1.51e-12

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: 67.06  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYatLKDGKAVAVKKLDNAAE-------PESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAT 191
Cdd:cd08222     8 LGSGNFGTVYL--VSDLKATADEELKVLKEisvgelqPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHD-ILHGRKGVQGAQPGPTLDWIQRVRIAVDaargleYLHEKvqpAVIHRDIRSSNVLLFEDFkAKIADFNLSN-- 268
Cdd:cd08222    86 GGDLDDkISEYKKSGTTIDENQILDWFIQLLLAVQ------YMHER---RILHRDLKAKNIFLKNNV-IKVGDFGISRil 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 269 -QSPDMAarlhsTRVLGTFGYHAPEyAMTGQ-LTQKSDVYSFGVVLLELLT 317
Cdd:cd08222   156 mGTSDLA-----TTFTGTPYYMSPE-VLKHEgYNSKSDIWSLGCILYEMCC 200
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
117-319 1.80e-12

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 68.09  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYATLKDGKA-VAVKKLdnaAEPESNVEFLTQVSRVSKL----KHDNFVELF-----GYCVEgNFR--I 184
Cdd:cd07851    21 SPVGSGAYGQVCSAFDTKTGRkVAIKKL---SRPFQSAIHAKRTYRELRLlkhmKHENVIGLLdvftpASSLE-DFQdvY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYEFatMGS-LHDILHGRKgvqgaqpgPTLDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd07851    97 LVTHL--MGAdLNNIVKCQK--------LSDDHIQF--LVYQILRGLKYIHSA---GIIHRDLKPSNLAVNEDCELKILD 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 264 FNLSNQSPD-MaarlhsTRVLGTFGYHAPEYAMT-GQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07851   162 FGLARHTDDeM------TGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGK 213
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
118-315 2.00e-12

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: 67.01  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd14046    13 VLGKGAFGQVVKVRNKlDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCEKSTLR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGrkgvqgaqpGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS--------- 267
Cdd:cd14046    93 DLIDS---------GLFQDTDRLWRLFRQILEGLAYIHSQ---GIIHRDLKPVNIFLDSNGNVKIGDFGLAtsnklnvel 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 268 ----NQSPDMAARLHS---TRVLGTFGYHAPEYA--MTGQLTQKSDVYSFGVVLLEL 315
Cdd:cd14046   161 atqdINKSTSAALGSSgdlTGNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEM 217
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
118-325 2.03e-12

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 66.73  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLDNA--AEPESNVEFLTQVSRVSK-LKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd14098     7 RLGSGTFAEVKKAVEVEtGKMRAIKQIVKRkvAGNDKNLQLFQREINILKsLEHPGIVRLIDWYEDDQHIYLVMEYVEGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDIL--HGRKGVQGAQPgptldwiqrvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFED--FKAKIADFNLsnq 269
Cdd:cd14098    87 DLMDFImaWGAIPEQHARE-----------LTKQILEAMAYTHSM---GITHRDLKPENILITQDdpVIVKISDFGL--- 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 270 spdmAARLHSTRVL----GTFGYHAPEYAMT------GQLTQKSDVYSFGVVLLELLTGRKPVDHT 325
Cdd:cd14098   150 ----AKVIHTGTFLvtfcGTMAYLAPEILMSkeqnlqGGYSNLVDMWSVGCLVYVMLTGALPFDGS 211
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
119-322 2.04e-12

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: 67.78  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNA-AEPESNVEFLTQVSRVSKLKHDNFV---ELFGYCVEGN-FRILAYEFATM 192
Cdd:cd07855    13 IGSGAYGVVCSAIdTKSGQKVAIKKIPNAfDVVTTAKRTLRELKILRHFKHDNIIairDILRPKVPYAdFKDVYVVLDLM 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GS-LHDILHGrkgvqgAQPgPTLDWIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN----LS 267
Cdd:cd07855    93 ESdLHHIIHS------DQP-LTLEHIRYFLYQL--LRGLKYIHSA---NVIHRDLKPSNLLVNENCELKIGDFGmargLC 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 268 NQSPDmaarlHS---TRVLGTFGYHAPEYAMT-GQLTQKSDVYSFGVVLLELLtGRKPV 322
Cdd:cd07855   161 TSPEE-----HKyfmTEYVATRWYRAPELMLSlPEYTQAIDMWSVGCIFAEML-GRRQL 213
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
119-322 2.04e-12

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


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 67.81  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYG---RAYYATLKDGKAVAVKKLDNAAepeSNVEFLTQVSRVSKL-----KHDNFVELFGYCV--EGNFR-ILAY 187
Cdd:cd07857     8 LGQGAYGivcSARNAETSEEETVAIKKITNVF---SKKILAKRALRELKLlrhfrGHKNITCLYDMDIvfPGNFNeLYLY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGRKGVQGAQpgptldwIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS 267
Cdd:cd07857    85 EELMEADLHQIIRSGQPLTDAH-------FQSFIYQI--LCGLKYIHSA---NVLHRDLKPGNLLVNADCELKICDFGLA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 268 ---NQSPDMAARlHSTRVLGTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLtGRKPV 322
Cdd:cd07857   153 rgfSENPGENAG-FMTEYVATRWYRAPEIMLSFQSYTKAiDVWSVGCILAELL-GRKPV 209
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
119-359 2.10e-12

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: 67.18  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFG-YCVEGNFRIlAYEFATMGSLh 196
Cdd:cd06622     9 LGKGNYGSVYKVLHRpTGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGaFFIEGAVYM-CMEYMDAGSL- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKGVQGAQPGPTLdwiqrVRIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQspdMAAR 276
Cdd:cd06622    87 DKLYAGGVATEGIPEDVL-----RRITYAVVKGLKFLKEEHN--IIHRDVKPTNVLVNGNGQVKLCDFGVSGN---LVAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 277 LHSTRVlGTFGYHAPEYAMTGQLTQ------KSDVYSFGVVLLELLTGRKP----VDHTMPRGQQSLVTWATPRL----- 341
Cdd:cd06622   157 LAKTNI-GCQSYMAPERIKSGGPNQnptytvQSDVWSLGLSILEMALGRYPyppeTYANIFAQLSAIVDGDPPTLpsgys 235
                         250       260
                  ....*....|....*....|..
gi 1032291014 342 --SEDKVKQCV--DPKLKGEYP 359
Cdd:cd06622   236 ddAQDFVAKCLnkIPNRRPTYA 257
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
154-321 2.13e-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: 66.74  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 154 EFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGVqgaqpgpTLDWIQRVRIAVDAARGLEYL 233
Cdd:cd14057    38 DFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHEGTGV-------VVDQSQAVKFALDIARGMAFL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 234 HeKVQPAVIHRDIRSSNVLLFEDFKAKI--ADFNLSNQSPdmaARLHSTrvlgtfGYHAPEYAMTGQ--LTQKS-DVYSF 308
Cdd:cd14057   111 H-TLEPLIPRHHLNSKHVMIDEDMTARInmADVKFSFQEP---GKMYNP------AWMAPEALQKKPedINRRSaDMWSF 180
                         170
                  ....*....|...
gi 1032291014 309 GVVLLELLTGRKP 321
Cdd:cd14057   181 AILLWELVTREVP 193
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
117-319 2.19e-12

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 66.96  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYATLKD-GKAVAVKK-LDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMgS 194
Cdd:cd07833     7 GVVGEGAYGVVLKCRNKAtGEIVAIKKfKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER-T 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGvqGAQPgptlDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd07833    86 LLELLEASPG--GLPP----DAVRS--YIWQLLQAIAYCHSH---NIIHRDIKPENILVSESGVLKLCDFGFARALTARP 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 275 ARlHSTRVLGTFGYHAPE----YAMTGqltQKSDVYSFGVVLLELLTGR 319
Cdd:cd07833   155 AS-PLTDYVATRWYRAPEllvgDTNYG---KPVDVWAIGCIMAELLDGE 199
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
119-323 2.24e-12

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 66.52  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKL--DNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd14161    11 LGKGTYGRVKKARDSSGRLVAIKSIrkDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRkgvqgaQPGPTLDWIQRVRIAVDAargLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspdmaar 276
Cdd:cd14161    91 DYISER------QRLSELEARHFFRQIVSA---VHYCH---ANGIVHRDLKLENILLDANGNIKIADFGLSNL------- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 277 LHSTRVLGTFG----YHAPEyAMTGQ--LTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14161   152 YNQDKFLQTYCgsplYASPE-IVNGRpyIGPEVDSWSLGVLLYILVHGTMPFD 203
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
118-323 2.26e-12

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: 66.49  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGKAVAVKKLDNA--AEPESNVEFLTQVSRVSKLKHDNFVElFGYCVEGNFRILAY-EFATMG 193
Cdd:cd14189     8 LLGKGGFARCYEMTdLATNKTYAVKVIPHSrvAKPHQREKIVNEIELHRDLHHKHVVK-FSHHFEDAENIYIFlELCSRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGVQGaqpgPTLDWIQRVRIAvdaarGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqspdm 273
Cdd:cd14189    87 SLAHIWKARHTLLE----PEVRYYLKQIIS-----GLKYLHLK---GILHRDLKLGNFFINENMELKVGDFGL------- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 274 AARLHSTR-----VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14189   148 AARLEPPEqrkktICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFE 202
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
119-317 2.28e-12

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: 67.13  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD------GKAVAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCV--EGNFRILAyEF 189
Cdd:cd05054    15 LGRGAFGKVIQASAFGidksatCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTkpGGPLMVIV-EF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRKgvQGAQPGPTLDWIQRVRIAVD-------------------AARGLEYLHEKvqpAVIHRDIRSSN 250
Cdd:cd05054    94 CKFGNLSNYLRSKR--EEFVPYRDKGARDVEEEEDDdelykepltledlicysfqVARGMEFLASR---KCIHRDLAARN 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 251 VLLFEDFKAKIADFNLSN---QSPDMaARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05054   169 ILLSENNVVKICDFGLARdiyKDPDY-VRKGDARL--PLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS 235
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
118-321 2.35e-12

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: 66.61  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLD-NAAEPESNVE---FLTQVSRVSKLKHDNFVELFGYCVEGNFRILA--YEFA 190
Cdd:cd06652     9 LLGQGAFGRVYLCYDADtGRELAVKQVQfDPESPETSKEvnaLECEIQLLKNLLHERIVQYYGCLRDPQERTLSifMEYM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRkgvqgaqpGPTLDWIQRvRIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQS 270
Cdd:cd06652    89 PGGSIKDQLKSY--------GALTENVTR-KYTRQILEGVHYLHSNM---IVHRDIKGANILRDSVGNVKLGDFGASKRL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 271 PDMAarLHST---RVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06652   157 QTIC--LSGTgmkSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPP 208
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
111-322 2.47e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 67.14  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKK--LDNAAE--PESNVEfltQVSRVSKLKHDNFVELFGYCVE------ 179
Cdd:cd07864     7 DKFDIIGIIGEGTYGQVYKAKDKDtGELVALKKvrLDNEKEgfPITAIR---EIKILRQLNHRSVVNLKEIVTDkqdald 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 180 -----GNFrILAYEFATmgslHDI--LHGRKGVQGAQpgptlDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVL 252
Cdd:cd07864    84 fkkdkGAF-YLVFEYMD----HDLmgLLESGLVHFSE-----DHIKS--FMKQLLEGLNYCHKK---NFLHRDIKCSNIL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 253 LFEDFKAKIADFNLSNQSPDMAARLHSTRVLgTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTgRKPV 322
Cdd:cd07864   149 LNNKGQIKLADFGLARLYNSEESRPYTNKVI-TLWYRPPELLLGEERYGPAiDVWSCGCILGELFT-KKPI 217
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
113-321 3.00e-12

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: 66.42  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKslIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLT-QVSRVSKLKHDNFVELfGYCVEGNFRI-LAYEF 189
Cdd:cd14097     5 FGRK--LGQGSFGVVIEAThKETQTKWAIKKINREKAGSSAVKLLErEVDILKHVNHAHIIHL-EEVFETPKRMyLVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHgRKGVQGAQPGPTLdwIQRVRIAVDaargleYLHEKvqpAVIHRDIRSSNVLL-------FEDFKAKIA 262
Cdd:cd14097    82 CEDGELKELLL-RKGFFSENETRHI--IQSLASAVA------YLHKN---DIVHRDLKLENILVkssiidnNDKLNIKVT 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 263 DFNLSNQSPDMAARlHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14097   150 DFGLSVQKYGLGED-MLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPP 207
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
119-322 3.20e-12

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: 66.52  E-value: 3.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVK--KLDNAAE--PESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFR-----ILAYE 188
Cdd:cd07863     8 IGVGAYGTVYKArDPHSGHFVALKsvRVQTNEDglPLSTVREVALLKRLEAFDHPNIVRLMDVCATSRTDretkvTLVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMgSLHDILHgrkgvQGAQPGPTLDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsn 268
Cdd:cd07863    88 HVDQ-DLRTYLD-----KVPPPGLPAETIKD--LMRQFLRGLDFLHAN---CIVHRDLKPENILVTSGGQVKLADFGL-- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 269 qspdmaARLHS-----TRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTgRKPV 322
Cdd:cd07863   155 ------ARIYScqmalTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFR-RKPL 206
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
119-323 3.58e-12

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 65.96  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGR---AYYATLKdgKAVAVKKLDNAAEPESNVE-FLT-QVSRVSKLKHDNFVELFGYCVEGNFRI-LAYEFATM 192
Cdd:cd14165     9 LGEGSYAKvksAYSERLK--CNVAIKIIDKKKAPDDFVEkFLPrELEILARLNHKSIIKTYEIFETSDGKVyIVMELGVQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHgrkgVQGAQPGptlDWIQRVRIAVDAArgLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ-SP 271
Cdd:cd14165    87 GDLLEFIK----LRGALPE---DVARKMFHQLSSA--IKYCHEL---DIVHRDLKCENLLLDKDFNIKLTDFGFSKRcLR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 272 DMAARLHSTRVL-GTFGYHAPEyAMTGQLTQ--KSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14165   155 DENGRIVLSKTFcGSAAYAAPE-VLQGIPYDprIYDIWSLGVILYIMVCGSMPYD 208
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
117-383 4.17e-12

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 66.19  E-value: 4.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYA-TLKDGKAVAVK--KLDNAAEPESNVEFLTQVSRVSK----LKHDNFVELFGYcvegnFRILAYEF 189
Cdd:cd13990     6 NLLGKGGFSEVYKAfDLVEQRYVACKihQLNKDWSEEKKQNYIKHALREYEihksLDHPRIVKLYDV-----FEIDTDSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDilhgrkgvqgaqpGPTLDWI--QRVRIAVDAAR--------GLEYLHEKVQPaVIHRDIRSSNVLLFEDFKA 259
Cdd:cd13990    81 CTVLEYCD-------------GNDLDFYlkQHKSIPEREARsiimqvvsALKYLNEIKPP-IIHYDLKPGNILLHSGNVS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 260 ---KIADFNLSNQSPDMAARLHSTRVL----GTFGYHAPEYAMTGQ----LTQKSDVYSFGVVLLELLTGRKPVDHTMpr 328
Cdd:cd13990   147 geiKITDFGLSKIMDDESYNSDGMELTsqgaGTYWYLPPECFVVGKtppkISSKVDVWSVGVIFYQMLYGRKPFGHNQ-- 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 329 GQQSLVTWATPRLSEdkvkqcvdpklKGEYP--PKAVAKLAAVAALCVQYESEFRPN 383
Cdd:cd13990   225 SQEAILEENTILKAT-----------EVEFPskPVVSSEAKDFIRRCLTYRKEDRPD 270
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
225-321 7.78e-12

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: 65.36  E-value: 7.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 225 DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRvlGTFGYHAPE-YAMTGQ-LTQK 302
Cdd:cd14200   132 DIVLGIEYLHYQ---KIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTA--GTPAFMAPEtLSDSGQsFSGK 206
                          90       100
                  ....*....|....*....|
gi 1032291014 303 S-DVYSFGVVLLELLTGRKP 321
Cdd:cd14200   207 AlDVWAMGVTLYCFVYGKCP 226
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
118-330 7.83e-12

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: 65.39  E-value: 7.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKK-LDNAAEPESNVefLTQVSRVSKLKHDNFVELFGYCV--EGNFRILAY---EFA 190
Cdd:cd13986     7 LLGEGGFSFVYLVeDLSTGRLYALKKiLCHSKEDVKEA--MREIENYRLFNHPNILRLLDSQIvkEAGGKKEVYlllPYY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRKgVQGaQPGPTldwIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQS 270
Cdd:cd13986    85 KRGSLQDEIERRL-VKG-TFFPE---DRILHIFLGICRGLKAMHEPELVPYAHRDIKPGNVLLSEDDEPILMDLGSMNPA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 271 P-------------DMAARlHSTRVlgtfgYHAPEY--AMTGQ-LTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQ 330
Cdd:cd13986   160 RieiegrrealalqDWAAE-HCTMP-----YRAPELfdVKSHCtIDEKTDIWSLGCTLYALMYGESPFERIFQKGD 229
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
106-323 8.03e-12

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


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 66.57  E-value: 8.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 106 LKEKtdnFGSKSLIGEGSYGRAYYATLKD---GKAVAVKKLDNAAEPESN----VEFLTQVS-RVSKL-KHDNFVELFGY 176
Cdd:COG5752    30 LKER---YRAIKPLGQGGFGRTFLAVDEDipsHPHCVIKQFYFPEQGPSSfqkaVELFRQEAvRLDELgKHPQIPELLAY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 177 CVEGNFRILAYEFATMGSLHDILHgRKGVqgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLL-FE 255
Cdd:COG5752   107 FEQDQRLYLVQEFIEGQTLAQELE-KKGV--------FSESQIWQLLKDLLPVLQFIHSR---NVIHRDIKPANIIRrRS 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 256 DFKAKIADFNLSNQSPDMAArLHSTRVLGTFGYHAPEYAMtGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:COG5752   175 DGKLVLIDFGVAKLLTITAL-LQTGTIIGTPEYMAPEQLR-GKVFPASDLYSLGVTCIYLLTGVSPFD 240
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
118-323 8.07e-12

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: 65.05  E-value: 8.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKLdNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFR----ILAYEFAT 191
Cdd:cd13985     7 QLGEGGFSYVYLAhDVNTGRRYALKRM-YFNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDSAILSSEGrkevLLLMEYCP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 mGSLHDILHGRkgvqgaqPGPTLDWIQRVRIAVDAARGLEYLHeKVQPAVIHRDIRSSNVLLFEDFKAKIADF-NLSNQS 270
Cdd:cd13985    86 -GSLVDILEKS-------PPSPLSEEEVLRIFYQICQAVGHLH-SQSPPIIHRDIKIENILFSNTGRFKLCDFgSATTEH 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 271 P------DMAARLHSTRVLGTFGYHAPE------YAMTGqltQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd13985   157 YpleraeEVNIIEEEIQKNTTPMYRAPEmidlysKKPIG---EKADIWALGCLLYKLCFFKLPFD 218
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
118-323 8.08e-12

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: 64.95  E-value: 8.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKAVAVKKL---DNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd14187    14 FLGKGGFAKCYEITDADTKEVFAGKIvpkSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGVQGaqpgPTLDWIQRVRIAvdaarGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd14187    94 LLELHKRRKALTE----PEARYYLRQIIL-----GCQYLHRN---RVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 275 ARlhSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14187   162 ER--KKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFE 208
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
119-344 8.28e-12

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: 65.02  E-value: 8.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD---GKAVAVKKLDNAAEPESNVEFLTQVSR----VSKLKHDNFVELFGYCVEGNFRI-LAYEFA 190
Cdd:cd13994     1 IGKGATSVVRIVTKKNprsGVLYAVKEYRRRDDESKRKDYVKRLTSeyiiSSKLHHPNIVKVLDLCQDLHGKWcLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHgrkgvqgAQPGPTLD----WIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd13994    81 PGGDLFTLIE-------KADSLSLEekdcFFKQI------LRGVAYLHSH---GIAHRDLKPENILLDEDGVLKLTDFGT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 267 SNQSPDMAARL--HSTRVLGTFGYHAPEyamtgQLTQKS------DVYSFGVVLLELLTGRKPvdhtmprgqqslvtWAT 338
Cdd:cd13994   145 AEVFGMPAEKEspMSAGLCGSEPYMAPE-----VFTSGSydgravDVWSCGIVLFALFTGRFP--------------WRS 205

                  ....*.
gi 1032291014 339 PRLSED 344
Cdd:cd13994   206 AKKSDS 211
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
221-322 1.01e-11

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 65.46  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 221 RIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAArlhsTRVLGTFGYHAPEYAMTGQLT 300
Cdd:cd06649   107 KVSIAVLRGLAYLREKHQ--IMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA----NSFVGTRSYMSPERLQGTHYS 180
                          90       100
                  ....*....|....*....|..
gi 1032291014 301 QKSDVYSFGVVLLELLTGRKPV 322
Cdd:cd06649   181 VQSDIWSMGLSLVELAIGRYPI 202
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
119-321 1.06e-11

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: 64.87  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLD----NAAEPESNVeflTQVSRVSKLKHDNFVELFG-YCVEGNFRILAY-EFAT 191
Cdd:cd08217     8 IGKGSFGTVRKVRRKsDGKILVWKEIDygkmSEKEKQQLV---SEVNILRELKHPNIVRYYDrIVDRANTTLYIVmEYCE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGVQGAQPGPTLdWiqrvRIAVDAARGLEYLH--EKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSN- 268
Cdd:cd08217    85 GGDLAQLIKKCKKENQYIPEEFI-W----KIFTQLLLALYECHnrSVGGGKILHRDLKPANIFLDSDNNVKLGDFGLARv 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 269 -QSPDMAArlhSTRVlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd08217   160 lSHDSSFA---KTYV-GTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPP 209
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
116-321 1.17e-11

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: 64.99  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYG----------RAYYATlkdgKAVAVKKLDNAA-------------------EPESNVEFLTQ-VSRVSKL 165
Cdd:cd14199     7 KDEIGKGSYGvvklayneddNTYYAM----KVLSKKKLMRQAgfprrppprgaraapegctQPRGPIERVYQeIAILKKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 166 KHDNFVELFGYCVEGN--FRILAYEFATMGSLHDIlhgrkgvqgaqpgPTLDWI--QRVRIAV-DAARGLEYLHEKvqpA 240
Cdd:cd14199    83 DHPNVVKLVEVLDDPSedHLYMVFELVKQGPVMEV-------------PTLKPLseDQARFYFqDLIKGIEYLHYQ---K 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 241 VIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTrvLGTFGYHAPEyamTGQLTQKS------DVYSFGVVLLE 314
Cdd:cd14199   147 IIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNT--VGTPAFMAPE---TLSETRKIfsgkalDVWAMGVTLYC 221

                  ....*..
gi 1032291014 315 LLTGRKP 321
Cdd:cd14199   222 FVFGQCP 228
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
119-319 1.21e-11

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: 65.46  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGR---AYYATLKdgKAVAVKKLDNAAEPESNVEFLTQVSRVSK-LKHDNFVELFGYCVEG----NFRILAYEFA 190
Cdd:cd07878    23 VGSGAYGSvcsAYDTRLR--QKVAVKKLSRPFQSLIHARRTYRELRLLKhMKHENVIGLLDVFTPAtsieNFNEVYLVTN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGS-LHDILHGRKgvqgaqpgPTLDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ 269
Cdd:cd07878   101 LMGAdLNNIVKCQK--------LSDEHVQF--LIYQLLRGLKYIHSA---GIIHRDLKPSNVAVNEDCELRILDFGLARQ 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 270 SPDmaarlHSTRVLGTFGYHAPEYAMTG-QLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07878   168 ADD-----EMTGYVATRWYRAPEIMLNWmHYNQTVDIWSVGCIMAELLKGK 213
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
117-323 1.22e-11

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


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 64.81  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGR------AYYATLKDGKAVAVK--KLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYE 188
Cdd:cd14076     7 RTLGEGEFGKvklgwpLPKANHRSGVQVAIKliRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHDILHGRKGVQGAQPgptldwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN 268
Cdd:cd14076    87 FVSGGELFDYILARRRLKDSVA---------CRLFAQLISGVAYLHKK---GVVHRDLKLENLLLDKNRNLVITDFGFAN 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 269 QSPDMAARLHSTRVlGTFGYHAPEYAMTGQL--TQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14076   155 TFDHFNGDLMSTSC-GSPCYAAPELVVSDSMyaGRKADIWSCGVILYAMLAGYLPFD 210
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
119-357 1.24e-11

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: 64.98  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFV------ELFGYCVEGNFRILAYEFAT 191
Cdd:cd14038     2 LGTGGFGNVLRWINQEtGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVaardvpEGLQKLAPNDLPLLAMEYCQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGVQGAQPGPTLDWIQrvriavDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA---KIADFNLSN 268
Cdd:cd14038    82 GGDLRKYLNQFENCCGLREGAILTLLS------DISSALRYLHEN---RIIHRDLKPENIVLQQGEQRlihKIIDLGYAK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 269 QSpDMAARlhSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVdhtMPRGQQslVTWATPRLSEDKVKQ 348
Cdd:cd14038   153 EL-DQGSL--CTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF---LPNWQP--VQWHGKVRQKSNEDI 224

                  ....*....
gi 1032291014 349 CVDPKLKGE 357
Cdd:cd14038   225 VVYEDLTGA 233
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
119-322 1.26e-11

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: 65.05  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDG-KAVAVKKLDNAAE----PESNVEFLTQVSRVSKLKHDNFVELFGYC-VEGNFR----ILAY 187
Cdd:cd07862     9 IGEGAYGKVFKArDLKNGgRFVALKRVRVQTGeegmPLSTIREVAVLRHLETFEHPNVVRLFDVCtVSRTDRetklTLVF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMgSLHDILHgrkgvQGAQPGPTLDWIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLs 267
Cdd:cd07862    89 EHVDQ-DLTTYLD-----KVPEPGVPTETIKDMMFQL--LRGLDFLHSH---RVVHRDLKPQNILVTSSGQIKLADFGL- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 268 nqspdmaARLHS-----TRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTgRKPV 322
Cdd:cd07862   157 -------ARIYSfqmalTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFR-RKPL 208
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
119-323 1.31e-11

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 64.21  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGR---AYYATlkDGKAVAVKKLDNAAEPESNVEflTQVSR----VSKLKHDNFVELfgycvegnfrilaYEFAT 191
Cdd:cd14079    10 LGVGSFGKvklAEHEL--TGHKVAVKILNRQKIKSLDME--EKIRReiqiLKLFRHPHIIRL-------------YEVIE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 mgSLHDILHGRKGVQGaqpGPTLDWI-QRVRIAVDAAR--------GLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd14079    73 --TPTDIFMVMEYVSG---GELFDYIvQKGRLSEDEARrffqqiisGVEYCHRHM---VVHRDLKPENLLLDSNMNVKIA 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 263 DFNLSNQSPDmaARLHSTRVlGTFGYHAPEyAMTGQLTQKS--DVYSFGVVLLELLTGRKPVD 323
Cdd:cd14079   145 DFGLSNIMRD--GEFLKTSC-GSPNYAAPE-VISGKLYAGPevDVWSCGVILYALLCGSLPFD 203
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
112-319 1.31e-11

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


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 64.83  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYA-TLKDGKAVAVKK--LDNAAE--PESNVEfltQVSRVSKLKHDNFVELFGYCVEGNFRILA 186
Cdd:cd07860     1 NFQKVEKIGEGTYGVVYKArNKLTGEVVALKKirLDTETEgvPSTAIR---EISLLKELNHPNIVKLLDVIHTENKLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFatmgsLHDILhgRKGVQGAQP-GPTLDWIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd07860    78 FEF-----LHQDL--KKFMDASALtGIPLPLIKSYLFQL--LQGLAFCHSH---RVLHRDLKPQNLLINTEGAIKLADFG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 266 LSnQSPDMAARLHSTRVLgTFGYHAPEYAMTGQL-TQKSDVYSFGVVLLELLTGR 319
Cdd:cd07860   146 LA-RAFGVPVRTYTHEVV-TLWYRAPEILLGCKYySTAVDIWSLGCIFAEMVTRR 198
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
119-264 1.36e-11

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: 61.69  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPE-SNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd13968     1 MGEGASAKVFWAeGECTTIGVAVKIGDDVNNEEgEDLESEMDILRRLKGLELNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 197 DILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd13968    81 AYTQEE----------ELDEKDVESIMYQLAECMRLLHSFH---LIHRDLNNDNILLSEDGNVKLIDF 135
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
113-317 1.49e-11

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: 64.25  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESN-VEFLTQVSRVSKLK-HDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSReDGKLYAVKRSRSRFRGEKDrKRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMgSLHDILHGRkgvqgaqpgptlDWIQRVR---IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd14050    83 CDT-SLQQYCEET------------HSLPESEvwnILLDLLKGLKHLHDH---GLIHLDIKPANIFLSKDGVCKLGDFGL 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 267 SNQSpDMAARLHSTRvlGTFGYHAPEyAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd14050   147 VVEL-DKEDIHDAQE--GDPRYMAPE-LLQGSFTKAADIFSLGITILELAC 193
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
134-324 1.79e-11

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 64.30  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 134 DGKAVAVKKLDNAAEPESN-------------VEFLTQVSRvsklkHDNFVELFGYCVEGNFRILAYEFATMGSLHDILh 200
Cdd:cd14093    27 TGQEFAVKIIDITGEKSSEneaeelreatrreIEILRQVSG-----HPNIIELHDVFESPTFIFLVFELCRKGELFDYL- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 201 gRKGVqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNlsnqspdMAARLHS- 279
Cdd:cd14093   101 -TEVV-------TLSEKKTRRIMRQLFEAVEFLHSL---NIVHRDLKPENILLDDNLNVKISDFG-------FATRLDEg 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 280 ---TRVLGTFGYHAPE------YAMTGQLTQKSDVYSFGVVLLELLTGRKPVDH 324
Cdd:cd14093   163 eklRELCGTPGYLAPEvlkcsmYDNAPGYGKEVDMWACGVIMYTLLAGCPPFWH 216
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
119-343 1.80e-11

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: 65.15  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEpesNVEFLTQVSRVSKL----KHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd07853     8 IGYGAFGVVWSVTdPRDGKRVALKKMPNVFQ---NLVSCKRVFRELKMlcffKHDNVLSALDILQPPHIDPFEEIYVVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHgrKGVQGAQPgPTLDWIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN-QSPD 272
Cdd:cd07853    85 LMQSDLH--KIIVSPQP-LSSDHVKVFLYQI--LRGLKYLHSA---GILHRDIKPGNLLVNSNCVLKICDFGLARvEEPD 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 273 maARLHSTRVLGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVT--WATPRLSE 343
Cdd:cd07853   157 --ESKHMTQEVVTQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITdlLGTPSLEA 228
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
119-321 1.84e-11

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: 64.16  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLdnaaePESNVEFLTQVSRV-------SKLKHDNFVELFgYCVEGNFRI-LAYEF 189
Cdd:cd05579     1 ISRGAYGRVYLAKKKsTGDLYAIKVI-----KKRDMIRKNQVDSVlaernilSQAQNPFVVKLY-YSFQGKKNLyLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILH--GRKGVQGAqpgptldwiqRVRIA--VDAargLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd05579    75 LPGGDLYSLLEnvGALDEDVA----------RIYIAeiVLA---LEYLH---SHGIIHRDLKPDNILIDANGHLKLTDFG 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 266 LS----NQSPDMAARL---------HSTRVLGTFGYHAPEyAMTGQLTQKS-DVYSFGVVLLELLTGRKP 321
Cdd:cd05579   139 LSkvglVRRQIKLSIQkksngapekEDRRIVGTPDYLAPE-ILLGQGHGKTvDWWSLGVILYEFLVGIPP 207
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
113-321 2.19e-11

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 64.24  E-value: 2.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNA-AEPESNVEflTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFA 190
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKqRSTGKLYALKCIKKSpLSRDSSLE--NEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHD-ILHgrKGVQGAQPGPTLdwIQRVRIAVdaarglEYLHEKvqpAVIHRDIRSSNVLLF---EDFKAKIADFNL 266
Cdd:cd14166    83 SGGELFDrILE--RGVYTEKDASRV--INQVLSAV------KYLHEN---GIVHRDLKPENLLYLtpdENSKIMITDFGL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 267 SNQSPDmaaRLHSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14166   150 SKMEQN---GIMST-ACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPP 200
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
119-353 2.32e-11

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 64.17  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAY-YATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRI-----LAYEFATM 192
Cdd:cd14039     1 LGTGGFGNVClYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAMEYCSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGAQPGPTLDWIQrvriavDAARGLEYLHEKvqpAVIHRDIRSSNVLLFE---DFKAKIADFNLSNq 269
Cdd:cd14039    81 GDLRKLLNKPENCCGLKESQVLSLLS------DIGSGIQYLHEN---KIIHRDLKPENIVLQEingKIVHKIIDLGYAK- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 270 spDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMprgqqSLVTWatprlsEDKVKQc 349
Cdd:cd14039   151 --DLDQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNL-----QPFTW------HEKIKK- 216

                  ....
gi 1032291014 350 VDPK 353
Cdd:cd14039   217 KDPK 220
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
119-319 2.41e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 64.40  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRV-------------SKLKHDNFVELFGYCVEGNFRI 184
Cdd:PTZ00024   17 LGEGTYGKVEKAYdTLTGKIVAIKKVKIIEISNDVTKDRQLVGMCgihfttlrelkimNEIKHENIMGLVDVYVEGDFIN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYEFATmGSLHDILHGRkgvqgaqpgpTLDWIQRVR-IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:PTZ00024   97 LVMDIMA-SDLKKVVDRK----------IRLTESQVKcILLQILNGLNVLHKW---YFMHRDLSPANIFINSKGICKIAD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 264 FNLS------------NQSPDMAARLHSTRVLGTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:PTZ00024  163 FGLArrygyppysdtlSKDETMQRREEMTSKVVTLWYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGK 231
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
87-321 3.13e-11

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 63.90  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  87 PDALKEPPSIDVPALSLDELKektdNFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLD--NAAEPESNVEFLTQVSRVS 163
Cdd:cd08229     4 PVPQFQPQKALRPDMGYNTLA----NFRIEKKIGRGQFSEVYRATcLLDGVPVALKKVQifDLMDAKARADCIKEIDLLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 164 KLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGVQGAQPGPTLdWiqrvRIAVDAARGLEYLHEKvqpAVIH 243
Cdd:cd08229    80 QLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPEKTV-W----KYFVQLCSALEHMHSR---RVMH 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 244 RDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd08229   152 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHS--LVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSP 227
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
117-319 3.21e-11

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: 64.03  E-value: 3.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESN-VEFLTQVSRVSKLKHDNFVELFGYCVEGN---FRILAYEFAT 191
Cdd:cd07859     6 EVIGKGSYGVVCSAIdTHTGEKVAIKKINDVFEHVSDaTRILREIKLLRLLRHPDIVEIKHIMLPPSrreFKDIYVVFEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGS-LHDILhgrkgvqGAQPGPTLDWIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQS 270
Cdd:cd07859    86 MESdLHQVI-------KANDDLTPEHHQFFLYQL--LRALKYIHTA---NVFHRDLKPKNILANADCKLKICDFGLARVA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 271 -PDMAARLHSTRVLGTFGYHAPEY--AMTGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07859   154 fNDTPTAIFWTDYVATRWYRAPELcgSFFSKYTPAIDIWSIGCIFAEVLTGK 205
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
118-325 4.10e-11

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: 62.72  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGKAVAVKKLDNA--AEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd14188     8 VLGKGGFAKCYEMTdLTTNKVYAAKIIPHSrvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGVQGaqpgPTLDWIQRVRIAvdaarGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd14188    88 MAHILKARKVLTE----PEVRYYLRQIVS-----GLKYLHEQ---EILHRDLKLGNFFINENMELKVGDFGLAARLEPLE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 275 ARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHT 325
Cdd:cd14188   156 HRRRT--ICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETT 204
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
107-331 4.41e-11

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: 63.18  E-value: 4.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 107 KEKTDNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLD---------NAAEPESNVEflTQVSRVSKLKHDNFVELFGY 176
Cdd:cd14084     2 KELRKKYIMSRTLGSGACGEVKLAYDKsTCKKVAIKIINkrkftigsrREINKPRNIE--TEIEILKKLSHPCIIKIEDF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 177 CVEGNFRILAYEFATMGSLHDILHGRKGVQgaQPGPTLDWIQRVRiavdaarGLEYLHEKvqpAVIHRDIRSSNVLLF-- 254
Cdd:cd14084    80 FDAEDDYYIVLELMEGGELFDRVVSNKRLK--EAICKLYFYQMLL-------AVKYLHSN---GIIHRDLKPENVLLSsq 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 255 -EDFKAKIADFNLSNQSPDMAarLHSTRVlGTFGYHAPE---YAMTGQLTQKSDVYSFGVVLLELLTGRKPVDH---TMP 327
Cdd:cd14084   148 eEECLIKITDFGLSKILGETS--LMKTLC-GTPTYLAPEvlrSFGTEGYTRAVDCWSLGVILFICLSGYPPFSEeytQMS 224

                  ....
gi 1032291014 328 RGQQ 331
Cdd:cd14084   225 LKEQ 228
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
108-319 5.08e-11

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: 62.91  E-value: 5.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 108 EKTDNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKK--LDNaaePESNVEFLTqvsrVSKLKHDNFVELFGYCV--EGN- 181
Cdd:cd14137     1 PVEISYTIEKVIGSGSFGVVYQAKLLEtGEVVAIKKvlQDK---RYKNRELQI----MRRLKHPNIVKLKYFFYssGEKk 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 182 ---FRILAYEFATMgSLHDILhgRKGVQGAQPGPTLDwiqrVRI-AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd14137    74 devYLNLVMEYMPE-TLYRVI--RHYSKNKQTIPIIY----VKLySYQLFRGLAYLHSL---GICHRDIKPQNLLVDPET 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 258 -KAKIADF----NLSNQSPDMAarLHSTRVlgtfgYHAPE-------YamtgqlTQKSDVYSFGVVLLELLTGR 319
Cdd:cd14137   144 gVLKLCDFgsakRLVPGEPNVS--YICSRY-----YRAPElifgatdY------TTAIDIWSAGCVLAELLLGQ 204
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
119-321 5.61e-11

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: 62.93  E-value: 5.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSR-VSKLKHDNFVELFGYCVEGNFRI-LAYEFATMGSL 195
Cdd:cd05577     1 LGRGGFGEVCACQVKAtGKMYACKKLDKKRIKKKKGETMALNEKiILEKVSSPFIVSLAYAFETKDKLcLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDIL--HGRKGVQGAqpgptldwiqRVRI-AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqSPD 272
Cdd:cd05577    81 KYHIynVGTRGFSEA----------RAIFyAAEIICGLEHLHNR---FIVYRDLKPENILLDDHGHVRISDLGL---AVE 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 273 MAARLHSTRVLGTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTGRKP 321
Cdd:cd05577   145 FKGGKKIKGRVGTHGYMAPEVLQKEVAYDFSvDWFALGCMLYEMIAGRSP 194
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
118-323 6.37e-11

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: 63.00  E-value: 6.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGKAVAVKKLD-NAAEPESNVEFLTQVSRVSKLKHDN-FVELFGYCVEGNFRIL-AYEFATMG 193
Cdd:cd05590     2 VLGKGSFGKVMLARLKeSGRLYAVKVLKkDVILQDDDVECTMTEKRILSLARNHpFLTQLYCCFQTPDRLFfVMEFVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLhdILHGRKGVQGAQPgptldwiqRVRI-AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspD 272
Cdd:cd05590    82 DL--MFHIQKSRRFDEA--------RARFyAAEITSALMFLHDK---GIIYRDLKLDNVLLDHEGHCKLADFGMCKE--G 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 273 MAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd05590   147 IFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFE 197
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
105-323 8.22e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 63.35  E-value: 8.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 105 ELKEKTDNFGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLD---------NAAEPEsnVEFLTQVSRVSKLK-HDNFVel 173
Cdd:PTZ00283   26 TAKEQAKKYWISRVLGSGATGTVLCAKrVSDGEPFAVKVVDmegmseadkNRAQAE--VCCLLNCDFFSIVKcHEDFA-- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 174 fgYCVEGN-----FRILAYEFATMGSLHDILHGRKGVQGA--QPGPTLDWIQrVRIAVdaarglEYLHEKvqpAVIHRDI 246
Cdd:PTZ00283  102 --KKDPRNpenvlMIALVLDYANAGDLRQEIKSRAKTNRTfrEHEAGLLFIQ-VLLAV------HHVHSK---HMIHRDI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 247 RSSNVLLFEDFKAKIADFNLSNqspdMAARLHSTRVLGTFG----YHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPV 322
Cdd:PTZ00283  170 KSANILLCSNGLVKLGDFGFSK----MYAATVSDDVGRTFCgtpyYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPF 245

                  .
gi 1032291014 323 D 323
Cdd:PTZ00283  246 D 246
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
118-321 8.33e-11

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction 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. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, 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). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 62.25  E-value: 8.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGK---AVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd05064    12 ILGTGRFGELCRGCLKlPSKrelPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGVQGAqpGPTLDWIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNlSNQSPDM 273
Cdd:cd05064    92 ALDSFLRKHEGQLVA--GQLMGMLPGL------ASGMKYLSEM---GYVHKGLAAHKVLVNSDLVCKISGFR-RLQEDKS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 274 AARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05064   160 EAIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSyGERP 208
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
119-321 1.09e-10

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 62.07  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT--LKDGKAVAVKKL------DNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFA 190
Cdd:cd14096     9 IGEGAFSNVYKAVplRNTGKPVAIKVVrkadlsSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSL-HDIlhgrkgvqgaqpgptldwIQRVRIAVDAAR--------GLEYLHEKvqpAVIHRDIRSSNvLLFE--DF-- 257
Cdd:cd14096    89 DGGEIfHQI------------------VRLTYFSEDLSRhvitqvasAVKYLHEI---GVVHRDIKPEN-LLFEpiPFip 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 258 ------------------------------KAKIADFNLSNQSPDMAARLHStrvlGTFGYHAPEYAMTGQLTQKSDVYS 307
Cdd:cd14096   147 sivklrkadddetkvdegefipgvggggigIVKLADFGLSKQVWDSNTKTPC----GTVGYTAPEVVKDERYSKKVDMWA 222
                         250
                  ....*....|....
gi 1032291014 308 FGVVLLELLTGRKP 321
Cdd:cd14096   223 LGCVLYTLLCGFPP 236
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
119-323 1.14e-10

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


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 61.64  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA-VAVKKLDNAAEPESNVEFL-TQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd14071     8 IGKGNFAVVKLARHRITKTeVAIKIIDKSQLDEENLKKIyREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DIL--HGRKGVQGAQPGptldwIQRVRIAVdaarglEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspdma 274
Cdd:cd14071    88 DYLaqHGRMSEKEARKK-----FWQILSAV------EYCHKR---HIVHRDLKAENLLLDANMNIKIADFGFSNF----- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 275 arLHSTRVLGTF----GYHAPEyAMTGQLTQ--KSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14071   149 --FKPGELLKTWcgspPYAAPE-VFEGKEYEgpQLDIWSLGVVLYVLVCGALPFD 200
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
119-358 1.55e-10

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


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 62.10  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLdNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRiLAYEFATMGSLHD 197
Cdd:cd07854    13 LGCGSNGLVFSAVDSDcDKRVAVKKI-VLTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGSD-LTEDVGSLTELNS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHgrkgVQGAQPGPTLDWIQRVRIAVDAA--------RGLEYLHEKvqpAVIHRDIRSSNVLL-FEDFKAKIADFNLSN 268
Cdd:cd07854    91 VYI----VQEYMETDLANVLEQGPLSEEHArlfmyqllRGLKYIHSA---NVLHRDLKPANVFInTEDLVLKIGDFGLAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 269 -QSPDMAARLHSTRVLGTFGYHAPEYAMT-GQLTQKSDVYSFGVVLLELLTGRK--PVDHTMPRGQQSLVTWATPRLSED 344
Cdd:cd07854   164 iVDPHYSHKGYLSEGLVTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPlfAGAHELEQMQLILESVPVVREEDR 243
                         250
                  ....*....|....
gi 1032291014 345 KVKQCVDPKLKGEY 358
Cdd:cd07854   244 NELLNVIPSFVRND 257
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
228-335 1.59e-10

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


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 61.82  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 228 RGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN-QSPDMAARLhSTRVlgtfgYHAPEYAMTGQ-LTQKSDV 305
Cdd:cd07856   119 RGLKYVHSA---GVIHRDLKPSNILVNENCDLKICDFGLARiQDPQMTGYV-STRY-----YRAPEIMLTWQkYDVEVDI 189
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1032291014 306 YSFGVVLLELLTGrKPV----DHTmprGQQSLVT 335
Cdd:cd07856   190 WSAGCIFAEMLEG-KPLfpgkDHV---NQFSIIT 219
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
108-318 1.84e-10

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 61.28  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 108 EKTDNFGsksLIGEGSYGRAYYATLKD-GKAVAVKK-LDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRIL 185
Cdd:cd07846     1 EKYENLG---LVGEGSYGMVMKCRHKEtGQIVAIKKfLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILHGRKGvqgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd07846    78 VFEFVDHTVLDDLEKYPNG---------LDESRVRKYLFQILRGIDFCHSH---NIIHRDIKPENILVSQSGVVKLCDFG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 266 LSN--QSPDMAArlhsTRVLGTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTG 318
Cdd:cd07846   146 FARtlAAPGEVY----TDYVATRWYRAPELLVGDTKYGKAvDVWAVGCLVTEMLTG 197
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
118-315 1.86e-10

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: 61.30  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHDNfveLFGYCVEGNFRI-------LAYEFA 190
Cdd:cd14143     2 SIGKGRFGEVWRGRWR-GEDVAVKIFSSREERSWFRE--AEIYQTVMLRHEN---ILGFIAADNKDNgtwtqlwLVSDYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRkgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKV-----QPAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd14143    76 EHGSLFDYLNRY----------TVTVEGMIKLALSIASGLAHLHMEIvgtqgKPAIAHRDLKSKNILVKKNGTCCIADLG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 266 LS--NQSPDMAARLHSTRVLGTFGYHAPEY-AMTGQLTQ-----KSDVYSFGVVLLEL 315
Cdd:cd14143   146 LAvrHDSATDTIDIAPNHRVGTKRYMAPEVlDDTINMKHfesfkRADIYALGLVFWEI 203
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
227-321 2.10e-10

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: 61.26  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 227 ARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVY 306
Cdd:cd05582   107 ALALDHLHSL---GIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYS--FCGTVEYMAPEVVNRRGHTQSADWW 181
                          90
                  ....*....|....*
gi 1032291014 307 SFGVVLLELLTGRKP 321
Cdd:cd05582   182 SFGVLMFEMLTGSLP 196
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
118-321 2.49e-10

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: 61.53  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATL------KDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFRILA-YEF 189
Cdd:cd05102    14 VLGHGAFGKVVEASAfgidksSSCETVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGACTKPNGPLMViVEF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRK-------------------------------------------GVQGAQPGPTLD--WIQRVRI-- 222
Cdd:cd05102    94 CKYGNLSNFLRAKRegfspyrersprtrsqvrsmveavradrrsrqgsdrvasftesTSSTNQPRQEVDdlWQSPLTMed 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 223 ----AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN---QSPDMaARLHSTRVlgTFGYHAPEYAM 295
Cdd:cd05102   174 licySFQVARGMEFLASR---KCIHRDLAARNILLSENNVVKICDFGLARdiyKDPDY-VRKGSARL--PLKWMAPESIF 247
                         250       260
                  ....*....|....*....|....*..
gi 1032291014 296 TGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05102   248 DKVYTTQSDVWSFGVLLWEIFSlGASP 274
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
112-321 2.49e-10

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: 60.81  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLD---NAAEPESNVEFL-TQVSRVSKLKHDNFVELFGYCVEGNFRILA 186
Cdd:cd06653     3 NWRLGKLLGRGAFGEVYLCYDADtGRELAVKQVPfdpDSQETSKEVNALeCEIQLLKNLRHDRIVQYYGCLRDPEEKKLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 --YEFATMGSLHDILHGRkgvqgaqpGPTLDWIQRvRIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd06653    83 ifVEYMPGGSVKDQLKAY--------GALTENVTR-RYTRQILQGVSYLHSNM---IVHRDIKGANILRDSAGNVKLGDF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 265 NLSNQSPDMAARLHSTR-VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06653   151 GASKRIQTICMSGTGIKsVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPP 208
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
119-321 2.82e-10

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: 60.92  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGrayYATL----KDGKAVAVKKLDNAAEP-ESNVE-FLTQVSRVSKLKHDNFV-------ELFgYCVEGNFRIL 185
Cdd:cd13989     1 LGSGGFG---YVTLwkhqDTGEYVAIKKCRQELSPsDKNRErWCLEVQIMKKLNHPNVVsardvppELE-KLSPNDLPLL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILHGRKGVQGAQPGPTLDwiqrvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFE---DFKAKIA 262
Cdd:cd13989    77 AMEYCSGGDLRKVLNQPENCCGLKESEVRT------LLSDISSAISYLHEN---RIIHRDLKPENIVLQQgggRVIYKLI 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 263 DF----NLSNQSPdmaarlhSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd13989   148 DLgyakELDQGSL-------CTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRP 203
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
117-321 3.07e-10

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 60.22  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKLDN-AAEPESNV-EFLTQVSRVSKL-KHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd14070     8 RKLGEGSFAKVREGLhAVTGEKVAIKVIDKkKAKKDSYVtKNLRREGRIQQMiRHPNITQLLDILETENSYYLVMELCPG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGAQpgpTLDWIQRVRIAVdaarglEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPD 272
Cdd:cd14070    88 GNLMHRIYDKKRLEERE---ARRYIRQLVSAV------EHLHRA---GVVHRDLKIENLLLDENDNIKLIDFGLSNCAGI 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 273 MAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14070   156 LGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLP 204
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
111-319 3.15e-10

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: 61.17  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLdnaaEPESNVEFLTQVSRVSKL----KHDNFVELFGYCVEGNFRil 185
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAVHKpTGQKVAIKKI----SPFEHQTYCLRTLREIKIllrfKHENIIGILDIQRPPTFE-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 ayefatmgSLHDILHgrkgVQGAQPGPTLDWIQRVRIAVDAA--------RGLEYLHEKvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd07849    79 --------SFKDVYI----VQELMETDLYKLIKTQHLSNDHIqyflyqilRGLKYIHSA---NVLHRDLKPSNLLLNTNC 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 258 KAKIADFNLsnqspdmaARLHS---------TRVLGTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTGR 319
Cdd:cd07849   144 DLKICDFGL--------ARIADpehdhtgflTEYVATRWYRAPEIMLNSKGYTKAiDIWSVGCILAEMLSNR 207
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
119-319 3.68e-10

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: 60.41  E-value: 3.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVelfgycvegnfrilayefatmgSLHD 197
Cdd:cd07871    13 LGEGTYATVFKGRSKlTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIV----------------------TLHD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKGV------------QGAQPGPTLDWIQRVRIAV-DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd07871    71 IIHTERCLtlvfeyldsdlkQYLDNCGNLMSMHNVKIFMfQLLRGLSYCHKR---KILHRDLKPQNLLINEKGELKLADF 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 265 NLSnQSPDMAARLHSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07871   148 GLA-RAKSVPTKTYSNEVV-TLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGR 201
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
107-321 6.13e-10

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 60.06  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 107 KEKTDN----FGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDNAA--EPESNVEflTQVSRVSKLKHDNFVELFGYCVE 179
Cdd:cd14168     2 KKQVEDikkiFEFKEVLGTGAFSEVVLAEERAtGKLFAVKCIPKKAlkGKESSIE--NEIAVLRKIKHENIVALEDIYES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 180 GNFRILAYEFATMGSLHDILHgRKGVQGAQPGPTLdwiqrVRIAVDAargLEYLHEKvqpAVIHRDIRSSNVLLF---ED 256
Cdd:cd14168    80 PNHLYLVMQLVSGGELFDRIV-EKGFYTEKDASTL-----IRQVLDA---VYYLHRM---GIVHRDLKPENLLYFsqdEE 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 257 FKAKIADFNLSNQspDMAARLHSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14168   148 SKIMISDFGLSKM--EGKGDVMST-ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP 209
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
119-324 6.19e-10

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: 59.74  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKK--LDNAAE--PESNVEfltQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMg 193
Cdd:cd07861     8 IGEGTYGVVYKGrNKKTGQIVAMKKirLESEEEgvPSTAIR---EISLLKELQHPNIVCLEDVLMQENRLYLVFEFLSM- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 slhDIlhgRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnQSPDM 273
Cdd:cd07861    84 ---DL---KKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSR---RVLHRDLKPQNLLIDNKGVIKLADFGLA-RAFGI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 274 AARLHSTRVLgTFGYHAPEYAMTGQL-TQKSDVYSFGVVLLELLTgRKPVDH 324
Cdd:cd07861   154 PVRVYTHEVV-TLWYRAPEVLLGSPRySTPVDIWSIGTIFAEMAT-KKPLFH 203
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
111-322 7.21e-10

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: 59.55  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPES-NVEFLTQVSRVSKLKHDNFVEL----FGYCVEGNFRI 184
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKtGEIVALKKLKMEKEKEGfPITSLREINILLKLQHPNIVTVkevvVGSNLDKIYMV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYefatmgslhdILHGRKGVQGAQPGPTLdwIQRVR-IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd07843    85 MEY----------VEHDLKSLMETMKQPFL--QSEVKcLMLQLLSGVAHLHDN---WILHRDLKTSNLLLNNRGILKICD 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 264 FNLSNQSPDMAARLhsTRVLGTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTgRKPV 322
Cdd:cd07843   150 FGLAREYGSPLKPY--TQLVVTLWYRAPELLLgAKEYSTAIDMWSVGCIFAELLT-KKPL 206
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
229-321 7.45e-10

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


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 59.71  E-value: 7.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnqSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd05592   108 GLQFLHSR---GIIYRDLKLDNVLLDREGHIKIADFGMC--KENIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSF 182
                          90
                  ....*....|...
gi 1032291014 309 GVVLLELLTGRKP 321
Cdd:cd05592   183 GVLLYEMLIGQSP 195
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
119-316 7.48e-10

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 59.49  E-value: 7.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVA---VKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd05086     5 IGNGWFGKVLLGEIYTGTSVArvvVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGDL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDIL-HGRKGVQGAQpgptlDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA 274
Cdd:cd05086    85 KTYLaNQQEKLRGDS-----QIMLLQRMACEIAAGLAHMHKH---NFLHSDLALRNCYLTSDLTVKVGDYGIGFSRYKED 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 275 ARLHSTRVLGTFGYHAPEYA-------MTGQLTQKSDVYSFGVVLLELL 316
Cdd:cd05086   157 YIETDDKKYAPLRWTAPELVtsfqdglLAAEQTKYSNIWSLGVTLWELF 205
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
119-318 8.66e-10

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 59.31  E-value: 8.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKK-LDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYcvegnFRI-----LAYEFAT 191
Cdd:cd07847     9 IGEGSYGVVFKCRNREtGQIVAIKKfVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEV-----FRRkrklhLVFEYCD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGVqgaqpgptlDWIQRVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLsnqsp 271
Cdd:cd07847    84 HTVLNELEKNPRGV---------PEHLIKKIIWQTLQAVNFCH---KHNCIHRDVKPENILITKQGQIKLCDFGF----- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 272 dmaARLHS------TRVLGTFGYHAPEYaMTG--QLTQKSDVYSFGVVLLELLTG 318
Cdd:cd07847   147 ---ARILTgpgddyTDYVATRWYRAPEL-LVGdtQYGPPVDVWAIGCVFAELLTG 197
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
118-321 9.06e-10

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


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 58.94  E-value: 9.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLD-NAAEPESNVEFLT---QVSRVSKLKHDNFVELFGYCVEGNFRILA--YEFA 190
Cdd:cd06651    14 LLGQGAFGRVYLCYDVDtGRELAAKQVQfDPESPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRAEKTLTifMEYM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILhgrKGVQGAQPGPTLDWIQRVriavdaARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQS 270
Cdd:cd06651    94 PGGSVKDQL---KAYGALTESVTRKYTRQI------LEGMSYLHSNM---IVHRDIKGANILRDSAGNVKLGDFGASKRL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 271 PDMAARLHSTR-VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd06651   162 QTICMSGTGIRsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 213
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
216-323 1.20e-09

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: 59.15  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 216 WIQRVR---------IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspDMAARLHSTRVLGTF 286
Cdd:cd05570    86 HIQRARrfteerarfYAAEICLALQFLHER---GIIYRDLKLDNVLLDAEGHIKIADFGMCKE--GIWGGNTTSTFCGTP 160
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1032291014 287 GYHAPEyAMTGQLTQKS-DVYSFGVVLLELLTGRKPVD 323
Cdd:cd05570   161 DYIAPE-ILREQDYGFSvDWWALGVLLYEMLAGQSPFE 197
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
118-382 1.44e-09

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 58.38  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKAVAVKKLD-NAAEPESNVEFLTQVSRVSKLKH-DNFVELFGYCVEGNFRILayeFATM--- 192
Cdd:cd14131     8 QLGKGGSSKVYKVLNPKKKIYALKRVDlEGADEQTLQSYKNEIELLKKLKGsDRIIQLYDYEVTDEDDYL---YMVMecg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 -GSLHDILHGRKGvqgaqpgPTLD-------WIQRVRiAVDAargleyLHEKvqpAVIHRDIRSSNVLLFEDfKAKIADF 264
Cdd:cd14131    85 eIDLATILKKKRP-------KPIDpnfiryyWKQMLE-AVHT------IHEE---GIVHSDLKPANFLLVKG-RLKLIDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 265 NLSNQSPDMAARLHSTRVLGTFGYHAPEyAMTG-----------QLTQKSDVYSFGVVLLELLTGRKPVDHtMPRGQQsl 333
Cdd:cd14131   147 GIAKAIQNDTTSIVRDSQVGTLNYMSPE-AIKDtsasgegkpksKIGRPSDVWSLGCILYQMVYGKTPFQH-ITNPIA-- 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 334 vtwatprlsedKVKQCVDPKLKGEYPPKAVAKLAAVAALCVQYESEFRP 382
Cdd:cd14131   223 -----------KLQAIIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRP 260
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
119-324 1.47e-09

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: 59.19  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSK-LKHDNFVELFGYCVEG----NFRILAYEFATM 192
Cdd:cd07880    23 VGSGAYGTVCSALdRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKhMKHENVIGLLDVFTPDlsldRFHDFYLVMPFM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GS-LHDILHGRKGVQgaqpgptldwiQRVRIAV-DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQS 270
Cdd:cd07880   103 GTdLGKLMKHEKLSE-----------DRIQFLVyQMLKGLKYIHAA---GIIHRDLKPGNLAVNEDCELKILDFGLARQT 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 271 PDMAARLHSTRvlgtfGYHAPEYAMTG-QLTQKSDVYSFGVVLLELLTGR---KPVDH 324
Cdd:cd07880   169 DSEMTGYVVTR-----WYRAPEVILNWmHYTQTVDIWSVGCIMAEMLTGKplfKGHDH 221
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
154-318 1.68e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 58.26  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 154 EFLTQVSRVSKLKHDNFVELFGYCVEGNFrILAYEFATMGSLHDILHGRKGvqgaqpGPTLDWiqRVRIAVDAARGLEYL 233
Cdd:cd05037    48 SFFETASLMSQISHKHLVKLYGVCVADEN-IMVQEYVRYGPLDKYLRRMGN------NVPLSW--KLQVAKQLASALHYL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 234 HEKvqpAVIHRDIRSSNVLLF-EDFKAKIADFNLSNQSPDMAARLHSTRVLGTfGYHAPEYAMTGQ--LTQKSDVYSFGV 310
Cdd:cd05037   119 EDK---KLIHGNVRGRNILLArEGLDGYPPFIKLSDPGVPITVLSREERVDRI-PWIAPECLRNLQanLTIAADKWSFGT 194

                  ....*...
gi 1032291014 311 VLLELLTG 318
Cdd:cd05037   195 TLWEICSG 202
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
119-322 1.76e-09

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: 58.21  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKK--LDNAAE--PESNvefLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAT-- 191
Cdd:cd07839     8 IGEGTYGTVFKAKNREtHEIVALKRvrLDDDDEgvPSSA---LREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCDqd 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILHGRKGVQGAQpgptldwiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnQSP 271
Cdd:cd07839    85 LKKYFDSCNGDIDPEIVK-----------SFMFQLLKGLAFCHSH---NVLHRDLKPQNLLINKNGELKLADFGLA-RAF 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 272 DMAARLHSTRVLgTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTGRKPV 322
Cdd:cd07839   150 GIPVRCYSAEVV-TLWYRPPDVLFGAKLYSTSiDMWSAGCIFAELANAGRPL 200
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
185-332 1.98e-09

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: 58.17  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYEFATMGSLHDILhgrKGVQGAQPGPTLDwiQRVRIAVDAAR--------GLEYLHekvQPAVIHRDIRSSNVLLFED 256
Cdd:cd05583    64 LHYAFQTDAKLHLIL---DYVNGGELFTHLY--QREHFTESEVRiyigeivlALEHLH---KLGIIYRDIKLENILLDSE 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 257 FKAKIADFNLSNQ-SPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKS--DVYSFGVVLLELLTGRKPVDHTMPRGQQS 332
Cdd:cd05583   136 GHVVLTDFGLSKEfLPGENDRAYS--FCGTIEYMAPEVVRGGSDGHDKavDWWSLGVLTYELLTGASPFTVDGERNSQS 212
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
116-321 2.03e-09

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: 58.48  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLiGEGSYGRAYYAT---LKDG---KAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHD-NFVELFGYCVE-GNFRILAY 187
Cdd:cd14207    13 KSL-GRGAFGKVVQASafgIKKSptcRVVAVKMLKEGATASEYKALMTELKILIHIGHHlNVVNLLGACTKsGGPLMVIV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGRK---------GVQG------AQPGPTLDWIQR--------------------------------- 219
Cdd:cd14207    92 EYCKYGNLSNYLKSKRdffvtnkdtSLQEelikekKEAEPTGGKKKRlesvtssesfassgfqedkslsdveeeeedsgd 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 220 -----------VRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN---QSPDMaARLHSTRVlgT 285
Cdd:cd14207   172 fykrpltmedlISYSFQVARGMEFLSSR---KCIHRDLAARNILLSENNVVKICDFGLARdiyKNPDY-VRKGDARL--P 245
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1032291014 286 FGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd14207   246 LKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSlGASP 282
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
241-321 2.23e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 58.87  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 241 VIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRK 320
Cdd:PTZ00267  190 MMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHR 269

                  .
gi 1032291014 321 P 321
Cdd:PTZ00267  270 P 270
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
116-323 2.29e-09

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: 57.54  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKDGKA-VAVKKLDNAAEPESNVEflTQVSRVSKLKHDNFVELFgYCVEGNFRI-LAYEFATMG 193
Cdd:cd14087     6 KALIGRGSFSRVVRVEHRVTRQpYAIKMIETKCRGREVCE--SELNVLRRVRHTNIIQLI-EVFETKERVyMVMELATGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHD--ILHGRKGVQGAQpgptldwiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFE---DFKAKIADFNLSN 268
Cdd:cd14087    83 ELFDriIAKGSFTERDAT-----------RVLQMVLDGVKYLHGL---GITHRDLKPENLLYYHpgpDSKIMITDFGLAS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 269 QSPDMAARLHSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14087   149 TRKKGPNCLMKT-TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFD 202
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
119-319 2.72e-09

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: 58.09  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVelfgycvegnfrilayefatmgSLHD 197
Cdd:cd07873    10 LGEGTYATVYKGRSKlTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIV----------------------TLHD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKGV------------QGAQPGPTLDWIQRVRIAV-DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd07873    68 IIHTEKSLtlvfeyldkdlkQYLDDCGNSINMHNVKLFLfQLLRGLAYCHRR---KVLHRDLKPQNLLINERGELKLADF 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 265 NLSnQSPDMAARLHSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07873   145 GLA-RAKSIPTKTYSNEVV-TLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGR 198
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
118-315 2.83e-09

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 57.71  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDgkAVAVKKLDNAAEPESNVE-FLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLH 196
Cdd:cd14153     7 LIGKGRFGQVYHGRWHG--EVAIRLIDIERDNEEQLKaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKGVqgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLlFEDFKAKIADFNLSNQSPDMAAR 276
Cdd:cd14153    85 SVVRDAKVV--------LDVNKTRQIAQEIVKGMGYLHAK---GILHKDLKSKNVF-YDNGKVVITDFGLFTISGVLQAG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 277 LHSTRVL---GTFGYHAPEyaMTGQLT-----------QKSDVYSFGVVLLEL 315
Cdd:cd14153   153 RREDKLRiqsGWLCHLAPE--IIRQLSpeteedklpfsKHSDVFAFGTIWYEL 203
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
119-315 3.42e-09

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: 57.75  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKdGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHDNFVELFGYCVEGNFR----ILAYEFATMGS 194
Cdd:cd14219    13 IGKGRYGEVWMGKWR-GEKVAVKVFFTTEEASWFRE--TEIYQTVLMRHENILGFIAADIKGTGSwtqlYLITDYHENGS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGrkgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKV-----QPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQ 269
Cdd:cd14219    90 LYDYLKS----------TTLDTKAMLKLAYSSVSGLCHLHTEIfstqgKPAIAHRDLKSKNILVKKNGTCCIADLGLAVK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 270 SPDMAARLH---STRVlGTFGYHAPEyAMTGQLTQK-------SDVYSFGVVLLEL 315
Cdd:cd14219   160 FISDTNEVDippNTRV-GTKRYMPPE-VLDESLNRNhfqsyimADMYSFGLILWEV 213
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
119-292 3.64e-09

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: 57.76  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKK--LDNAAEPESnVEFLTQVSRVSKLKHDNFVELFGYC-----VEGNFR---ILAY 187
Cdd:cd07865    20 IGQGTFGEVFKArHRKTGQIVALKKvlMENEKEGFP-ITALREIKILQLLKHENVVNLIEICrtkatPYNRYKgsiYLVF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATmgslHDI--LHGRKGVQGaqpgpTLDWIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFN 265
Cdd:cd07865    99 EFCE----HDLagLLSNKNVKF-----TLSEIKKVMKML--LNGLYYIHRN---KILHRDMKAANILITKDGVLKLADFG 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1032291014 266 LS---NQSPDMAARLHSTRVLgTFGYHAPE 292
Cdd:cd07865   165 LArafSLAKNSQPNRYTNRVV-TLWYRPPE 193
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
112-332 3.89e-09

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: 57.11  E-value: 3.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFA 190
Cdd:cd07836     1 NFKQLEKLGEGTYATVYKGRNRtTGEIVALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TmGSLHDILHGRkGVQGAQPGPTLDWIQRVRIavdaaRGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnQS 270
Cdd:cd07836    81 D-KDLKKYMDTH-GVRGALDPNTVKSFTYQLL-----KGIAFCHEN---RVLHRDLKPQNLLINKRGELKLADFGLA-RA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 271 PDMAARLHSTRVLgTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTGR--------------------KPVDHTMPRG 329
Cdd:cd07836   150 FGIPVNTFSNEVV-TLWYRAPDVLLGSRTYSTSiDIWSVGCIMAEMITGRplfpgtnnedqllkifrimgTPTESTWPGI 228

                  ...
gi 1032291014 330 QQS 332
Cdd:cd07836   229 SQL 231
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
112-335 4.04e-09

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 57.62  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYY---ATLKD-GKAVAVKKLDNAA--EPESNVEFlTQVSRvSKLKHdnfvelfgyCVEGNFRI- 184
Cdd:cd05614     1 NFELLKVLGTGAYGKVFLvrkVSGHDaNKLYAMKVLRKAAlvQKAKTVEH-TRTER-NVLEH---------VRQSPFLVt 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYEFATMGSLHDILhgrKGVQGAQPGPTLdwIQRVRIAVDAAR--------GLEYLHekvQPAVIHRDIRSSNVLLFED 256
Cdd:cd05614    70 LHYAFQTDAKLHLIL---DYVSGGELFTHL--YQRDHFSEDEVRfysgeiilALEHLH---KLGIVYRDIKLENILLDSE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 257 FKAKIADFNLSNQ-SPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTGRKPVDHTMPRGQQSLV 334
Cdd:cd05614   142 GHVVLTDFGLSKEfLTEEKERTYS--FCGTIEYMAPEIIRGKSGHGKAvDWWSLGILMFELLTGASPFTLEGEKNTQSEV 219

                  .
gi 1032291014 335 T 335
Cdd:cd05614   220 S 220
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
109-321 4.42e-09

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: 56.98  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 109 KTDNFGSKSLIGEGSYGRAYYATLK------DGKAVAVKKL-------DNAAEPESNVEFLTQV---SRVSKLK--HDNF 170
Cdd:cd14106     1 STENINEVYTVESTPLGRGKFAVVRkcihkeTGKEYAAKFLrkrrrgqDCRNEILHEIAVLELCkdcPRVVNLHevYETR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 171 VELfgycvegnfrILAYEFATMGSLHDILHGRKGVQGAQPgptldwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSN 250
Cdd:cd14106    81 SEL----------ILILELAAGGELQTLLDEEECLTEADV---------RRLMRQILEGVQYLHER---NIVHLDLKPQN 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 251 VLLFEDFK---AKIADFNLSNQspdMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14106   139 ILLTSEFPlgdIKLCDFGISRV---IGEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSP 209
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
109-323 4.49e-09

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: 57.70  E-value: 4.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 109 KTDNFGSKSLIGEGSYGRAYYATLKDGK---AVAVKKLDNAAEpESNVEFLTQVSRV-SKLKHDNFVELFGYCVEGNFRI 184
Cdd:cd05615     8 RLTDFNFLMVLGKGSFGKVMLAERKGSDelyAIKILKKDVVIQ-DDDVECTMVEKRVlALQDKPPFLTQLHSCFQTVDRL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 -LAYEFATMGSLhdILHGRKGVQGAQPgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd05615    87 yFVMEYVNGGDL--MYHIQQVGKFKEP-------QAVFYAAEISVGLFFLHKK---GIIYRDLKLDNVMLDSEGHIKIAD 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 264 FNLSNQspDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd05615   155 FGMCKE--HMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFD 212
PHA02988 PHA02988
hypothetical protein; Provisional
162-324 4.79e-09

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 57.06  E-value: 4.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 162 VSKLKHDNFVELFGY----CVEGNFRILAYEFATMGSLHDILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKV 237
Cdd:PHA02988   72 LRRIDSNNILKIYGFiidiVDDLPRLSLILEYCTRGYLREVLDKEK---------DLSFKTKLDMAIDCCKGLYNLYKYT 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 238 -QPaviHRDIRSSNVLLFEDFKAKIADFNLSN---------------QSPDMAARLHStrvlgtfgyhapeyamtgQLTQ 301
Cdd:PHA02988  143 nKP---YKNLTSVSFLVTENYKLKIICHGLEKilssppfknvnfmvyFSYKMLNDIFS------------------EYTI 201
                         170       180
                  ....*....|....*....|...
gi 1032291014 302 KSDVYSFGVVLLELLTGRKPVDH 324
Cdd:PHA02988  202 KDDIYSLGVVLWEIFTGKIPFEN 224
pknD PRK13184
serine/threonine-protein kinase PknD;
118-321 5.39e-09

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 58.24  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKL--DNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:PRK13184    9 LIGKGGMGEVYLAyDPVCSRRVALKKIreDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILhgrKGVQGAQPGPTLDWIQR-----VRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF----- 264
Cdd:PRK13184   89 LKSLL---KSVWQKESLSKELAEKTsvgafLSIFHKICATIEYVHSK---GVLHRDLKPDNILLGLFGEVVILDWgaaif 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 265 ------NLSNQSPDMAARLHST-----RVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:PRK13184  163 kkleeeDLLDIDVDERNICYSSmtipgKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFP 230
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
135-321 5.41e-09

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: 56.65  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 135 GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDN---FVELFgyCVEGNFRILAyEFATMGSLHDILhgrkgvqgAQPG 211
Cdd:cd14043    23 GDWVWLKKFPGGSHTELRPSTKNVFSKLRELRHENvnlFLGLF--VDCGILAIVS-EHCSRGSLEDLL--------RNDD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 212 PTLDWIQRVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADF---------NLSNQSPDMAARLhstrv 282
Cdd:cd14043    92 MKLDWMFKSSLLLDLIKGMRYLH---HRGIVHGRLKSRNCVVDGRFVLKITDYgyneileaqNLPLPEPAPEELL----- 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1032291014 283 lgtfgYHAPEY----AMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14043   164 -----WTAPELlrdpRLERRGTFPGDVFSFAIIMQEVIVRGAP 201
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
158-322 5.58e-09

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: 56.95  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 158 QVSRVSKLKHDNFVELFGYCVEGNFRI-LAYEFATmGSLHDILHGRKGVQGAQP---GPTLDWIQRVRIAVDAARGLEYL 233
Cdd:cd14011    52 GVKQLTRLRHPRILTVQHPLEESRESLaFATEPVF-ASLANVLGERDNMPSPPPelqDYKLYDVEIKYGLLQISEALSFL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 234 HEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMA----------ARLHSTrVLGTFGYHAPEYAMTGQLTQKS 303
Cdd:cd14011   131 HNDVK--LVHGNICPESVVINSNGEWKLAGFDFCISSEQATdqfpyfreydPNLPPL-AQPNLNYLAPEYILSKTCDPAS 207
                         170
                  ....*....|....*....
gi 1032291014 304 DVYSFGVVLLELLTGRKPV 322
Cdd:cd14011   208 DMFSLGVLIYAIYNKGKPL 226
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
113-324 5.76e-09

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 56.94  E-value: 5.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRaYYATLKDGKAVAVKKlDNAAEPesnvefLTQvSRVSKLKHDNFVELFGYCVEGNFRI-LAYEFAT 191
Cdd:cd05595     8 FGKVILVREKATGR-YYAMKILRKEVIIAK-DEVAHT------VTE-SRVLQNTRHPFLTALKYAFQTHDRLcFVMEYAN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLhdILHgrkgvqgaqpgptldwIQRVRI-AVDAAR--------GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd05595    79 GGEL--FFH----------------LSRERVfTEDRARfygaeivsALEYLHSR---DVVYRDIKLENLMLDKDGHIKIT 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 263 DFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPV---DH 324
Cdd:cd05595   138 DFGLCKEGITDGATMKT--FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynqDH 200
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
119-321 5.90e-09

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: 56.55  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYgRAYYATLKDGKAVAVKKLDNAAEPESNVE---FLTQVSRVSKLKHDNFVELFGY---CVEGNF-RILAYEFAT 191
Cdd:cd14033     9 IGRGSF-KTVYRGLDTETTVEVAWCELQTRKLSKGErqrFSEEVEMLKGLQHPNIVRFYDSwksTVRGHKcIILVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILhgrKGVQGAQPGPTLDWIQRVriavdaARGLEYLHEKVqPAVIHRDIRSSNVLLF-EDFKAKIADFNLSNQS 270
Cdd:cd14033    88 SGTLKTYL---KRFREMKLKLLQRWSRQI------LKGLHFLHSRC-PPILHRDLKCDNIFITgPTGSVKIGDLGLATLK 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 271 PDMAARlhstRVLGTFGYHAPEyAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14033   158 RASFAK----SVIGTPEFMAPE-MYEEKYDEAVDVYAFGMCILEMATSEYP 203
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
116-323 6.37e-09

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


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 56.49  E-value: 6.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLiGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVefLTQVSR---VSKL-KHDNFVELfgYCVEGNFR--ILAYE 188
Cdd:cd14081     7 KTL-GKGQTGLVKLAKHCVtGQKVAIKIVNKEKLSKESV--LMKVEReiaIMKLiEHPNVLKL--YDVYENKKylYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHDIL--HGRkgvqgAQPGPTLDWIQRVrIAvdaarGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNl 266
Cdd:cd14081    82 YVSGGELFDYLvkKGR-----LTEKEARKFFRQI-IS-----ALDYCH---SHSICHRDLKPENLLLDEKNNIKIADFG- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 267 snqspdMAARLHSTRVLGTF----GYHAPEYAMTGQLT-QKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd14081   147 ------MASLQPEGSLLETScgspHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFD 202
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
119-321 7.92e-09

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


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 56.14  E-value: 7.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPE---SNVefLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMgs 194
Cdd:cd07835     7 IGEGTYGVVYKArDKLTGEIVALKKIRLETEDEgvpSTA--IREISLLKELNHPNIVRLLDVVHSENKLYLVFEFLDL-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 lhDILHGRKGVQGAQPGPTLdwIQRVRIAVdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnQSPDMA 274
Cdd:cd07835    83 --DLKKYMDSSPLTGLDPPL--IKSYLYQL--LQGIAFCHSH---RVLHRDLKPQNLLIDTEGALKLADFGLA-RAFGVP 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 275 ARLHSTRVLgTFGYHAPEYAMTGqlTQKS---DVYSFGVVLLELLTgRKP 321
Cdd:cd07835   153 VRTYTHEVV-TLWYRAPEILLGS--KHYStpvDIWSVGCIFAEMVT-RRP 198
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
112-323 9.86e-09

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: 56.55  E-value: 9.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLKDGK---AVAVKKLDNAAEpESNVEFLTQVSRVSKLK-HDNFVELFGYCVEGNFRI-LA 186
Cdd:cd05616     1 DFNFLMVLGKGSFGKVMLAERKGTDelyAVKILKKDVVIQ-DDDVECTMVEKRVLALSgKPPFLTQLHSCFQTMDRLyFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLhdILHGRKGVQGAQPgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd05616    80 MEYVNGGDL--MYHIQQVGRFKEP-------HAVFYAAEIAIGLFFLQSK---GIIYRDLKLDNVMLDSEGHIKIADFGM 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 267 SNQspDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd05616   148 CKE--NIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFE 202
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
112-321 1.06e-08

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 55.70  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAT 191
Cdd:cd14190     5 SIHSKEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILhgrkgVQGAQPGPTLDWIQRVRIAVDaarGLEYLHekvQPAVIHRDIRSSNVLLFE--DFKAKIADFNLSNQ 269
Cdd:cd14190    85 GGELFERI-----VDEDYHLTEVDAMVFVRQICE---GIQFMH---QMRVLHLDLKPENILCVNrtGHQVKIIDFGLARR 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 270 -SPDMAARLHstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14190   154 yNPREKLKVN----FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSP 202
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
134-316 1.15e-08

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. 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-C 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: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 55.66  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 134 DGKAVAVKKL---DNAAEPESNVEfltqVSRVSKLKHDNFVELFGyCVEGNFRILAY-EFATMGSLHDILHGRKgvqgAQ 209
Cdd:cd14044    30 DKKVVILKDLknnEGNFTEKQKIE----LNKLLQIDYYNLTKFYG-TVKLDTMIFGViEYCERGSLRDVLNDKI----SY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 210 PGPT-LDWIQRVRIAVDAARGLEYLHekVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQspdmaarLHSTRVLGTfgy 288
Cdd:cd14044   101 PDGTfMDWEFKISVMYDIAKGMSYLH--SSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSI-------LPPSKDLWT--- 168
                         170       180
                  ....*....|....*....|....*...
gi 1032291014 289 hAPEYAMTGQLTQKSDVYSFGVVLLELL 316
Cdd:cd14044   169 -APEHLRQAGTSQKGDVYSYGIIAQEII 195
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
222-357 1.25e-08

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 55.83  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 222 IAVDAARGLEYLHEkVQPAVIHRDIRSSNVLLFEDF---KAKIADFNLSNQSPDMAARLH----STRVLGTFGYHAPEYA 294
Cdd:cd14040   116 IVMQIVNALRYLNE-IKPPIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDDSYGVDgmdlTSQGAGTYWYLPPECF 194
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 295 MTGQ----LTQKSDVYSFGVVLLELLTGRKPVDHTmpRGQQSLVTWATPrLSEDKVKQCVDPKLKGE 357
Cdd:cd14040   195 VVGKeppkISNKVDVWSVGVIFFQCLYGRKPFGHN--QSQQDILQENTI-LKATEVQFPVKPVVSNE 258
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
229-321 1.32e-08

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: 55.52  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNLSNqspDMAARLHSTRVlGTFGYHAPEYAMTGQLTQKS-DVYS 307
Cdd:cd05606   110 GLEHMHNRF---IVYRDLKPANILLDEHGHVRISDLGLAC---DFSKKKPHASV-GTHGYMAPEVLQKGVAYDSSaDWFS 182
                          90
                  ....*....|....
gi 1032291014 308 FGVVLLELLTGRKP 321
Cdd:cd05606   183 LGCMLYKLLKGHSP 196
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-321 1.42e-08

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


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 55.51  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRV-SKLKHDNFVELFGYCVEGNFRILAYE 188
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKsTGQEFAAKIINTKKLSARDHQKLEREARIcRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHDILHGRKGVQGAQPGPTldwIQRVRIAVDaargleYLHEKvqpAVIHRDIRSSNVLLFEDFK---AKIADFN 265
Cdd:cd14086    81 LVTGGELFEDIVAREFYSEADASHC---IQQILESVN------HCHQN---GIVHRDLKPENLLLASKSKgaaVKLADFG 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 266 LSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14086   149 LAIEVQGDQQAWFG--FAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPP 202
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
229-321 1.45e-08

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: 55.41  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmaARLHSTRVlGTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd05630   114 GLEDLH---RERIVYRDLKPENILLDDHGHIRISDLGLAVHVPE--GQTIKGRV-GTVGYMAPEVVKNERYTFSPDWWAL 187
                          90
                  ....*....|...
gi 1032291014 309 GVVLLELLTGRKP 321
Cdd:cd05630   188 GCLLYEMIAGQSP 200
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
109-318 1.47e-08

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


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 55.85  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 109 KTDNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd07869     3 KADSYEKLEKLGEGSYATVYKGKSKvNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMgSLHDILHGRKGvqGAQPGPTLDWIQRVriavdaARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNLS 267
Cdd:cd07869    83 EYVHT-DLCQYMDKHPG--GLHPENVKLFLFQL------LRGLSYIHQRY---ILHRDLKPQNLLISDTGELKLADFGLA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 268 nQSPDMAARLHSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTG 318
Cdd:cd07869   151 -RAKSVPSHTYSNEVV-TLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQG 200
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
118-321 1.51e-08

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 55.71  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNvefltQVSRV-------SKLKHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd05574     8 LLGKGDVGRVYLVRLKGtGKLFAMKVLDKEEMIKRN-----KVKRVltereilATLDHPFLPTLYASFQTSTHLCFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILhgRKgvqgaQPGPtldwiqrvRIAVDAAR--------GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKI 261
Cdd:cd05574    83 CPGGELFRLL--QK-----QPGK--------RLPEEVARfyaaevllALEYLHLL---GFVYRDLKPENILLHESGHIML 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 262 ADFNLSNQS---------------PDMAARLHSTRVL------------GTFGYHAPEyAMTGQlTQKSDV--YSFGVVL 312
Cdd:cd05574   145 TDFDLSKQSsvtpppvrkslrkgsRRSSVKSIEKETFvaepsarsnsfvGTEEYIAPE-VIKGD-GHGSAVdwWTLGILL 222

                  ....*....
gi 1032291014 313 LELLTGRKP 321
Cdd:cd05574   223 YEMLYGTTP 231
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
119-319 1.68e-08

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 55.64  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAepeSN----------VEFLTQVSrvsklKHDNFVELFG-YCVEGNFRI-L 185
Cdd:cd07852    15 LGKGAYGIVWKAIDKKtGEVVALKKIFDAF---RNatdaqrtfreIMFLQELN-----DHPNIIKLLNvIRAENDKDIyL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFatMGS-LHDILhgRKGVqgaqpgptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd07852    87 VFEY--METdLHAVI--RANI--------LEDIHKQYIMYQLLKALKYLHSG---GVIHRDLKPSNILLNSDCRVKLADF 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 265 NLS---NQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTGR 319
Cdd:cd07852   152 GLArslSQLEEDDENPVLTDYVATRWYRAPEILLGSTRYTKGvDMWSVGCILGEMLLGK 210
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
112-321 1.73e-08

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: 55.39  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYY----ATLKDGKAVAVKKLDNAaepesnveflTQVSRVSKLKHDNFV-ELFGYCVEGNFRI-L 185
Cdd:cd05613     1 NFELLKVLGTGAYGKVFLvrkvSGHDAGKLYAMKVLKKA----------TIVQKAKTAEHTRTErQVLEHIRQSPFLVtL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILhgrKGVQGAQPGPTLdwIQRVRIAVDAAR--------GLEYLHekvQPAVIHRDIRSSNVLLFEDF 257
Cdd:cd05613    71 HYAFQTDTKLHLIL---DYINGGELFTHL--SQRERFTENEVQiyigeivlALEHLH---KLGIIYRDIKLENILLDSSG 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 258 KAKIADFNLSNQ-SPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKS--DVYSFGVVLLELLTGRKP 321
Cdd:cd05613   143 HVVLTDFGLSKEfLLDENERAYS--FCGTIEYMAPEIVRGGDSGHDKavDWWSLGVLMYELLTGASP 207
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
228-328 1.75e-08

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 55.21  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 228 RGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNlSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYS 307
Cdd:cd14111   110 QGLEYLHGR---RVLHLDIKPDNIMVTNLNAIKIVDFG-SAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWS 185
                          90       100
                  ....*....|....*....|.
gi 1032291014 308 FGVVLLELLTGRKPVDHTMPR 328
Cdd:cd14111   186 IGVLTYIMLSGRSPFEDQDPQ 206
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
227-321 1.83e-08

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 55.76  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 227 ARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSN---QSPDMA----ARLhstrvlgTFGYHAPEYAMTGQL 299
Cdd:cd05103   189 AKGMEFLASR---KCIHRDLAARNILLSENNVVKICDFGLARdiyKDPDYVrkgdARL-------PLKWMAPETIFDRVY 258
                          90       100
                  ....*....|....*....|...
gi 1032291014 300 TQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05103   259 TIQSDVWSFGVLLWEIFSlGASP 281
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
118-315 2.34e-08

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 54.97  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVeFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd14152     7 LIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKL-FKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKGRTLYS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHgrkgvqgaQPGPTLDwIQRVR-IAVDAARGLEYLHEKvqpAVIHRDIRSSNVlLFEDFKAKIADFNLSNQSPDM-AA 275
Cdd:cd14152    86 FVR--------DPKTSLD-INKTRqIAQEIIKGMGYLHAK---GIVHKDLKSKNV-FYDNGKVVITDFGLFGISGVVqEG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 276 RLHSTRVL--GTFGYHAPEYA--MT-GQ------LTQKSDVYSFGVVLLEL 315
Cdd:cd14152   153 RRENELKLphDWLCYLAPEIVreMTpGKdedclpFSKAADVYAFGTIWYEL 203
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
119-319 2.38e-08

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: 54.97  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLdnAAEPESNVEF--LTQVSRVSKLKHDNFVelfgycvegnfrilayefatmgSL 195
Cdd:cd07870     8 LGEGSYATVYKGISRiNGQLVALKVI--SMKTEEGVPFtaIREASLLKGLKHANIV----------------------LL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQGAQPGPTLDWIQ------------RVRIAV-DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd07870    64 HDIIHTKETLTFVFEYMHTDLAQymiqhpgglhpyNVRLFMfQLLRGLAYIHGQ---HILHRDLKPQNLLISYLGELKLA 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 263 DFNLSnQSPDMAARLHSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07870   141 DFGLA-RAKSIPSQTYSSEVV-TLWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQ 196
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
228-321 2.65e-08

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: 54.54  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 228 RGLEYLHEKvqpAVIHRDIRSSNvLLFEDFKAK--IADFNLSNQSPDMAARlHSTRVlGTFGYHAPEYAM--TGQlTQKS 303
Cdd:cd14019   112 KALKHVHSF---GIIHRDVKPGN-FLYNRETGKgvLVDFGLAQREEDRPEQ-RAPRA-GTRGFRAPEVLFkcPHQ-TTAI 184
                          90
                  ....*....|....*...
gi 1032291014 304 DVYSFGVVLLELLTGRKP 321
Cdd:cd14019   185 DIWSAGVILLSILSGRFP 202
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
223-323 2.69e-08

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 55.09  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 223 AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL--SNQSPDMaarlhSTRVL-GTFGYHAPEYAMTGQL 299
Cdd:cd05587   103 AAEIAVGLFFLHSK---GIIYRDLKLDNVMLDAEGHIKIADFGMckEGIFGGK-----TTRTFcGTPDYIAPEIIAYQPY 174
                          90       100
                  ....*....|....*....|....
gi 1032291014 300 TQKSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd05587   175 GKSVDWWAYGVLLYEMLAGQPPFD 198
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
119-321 2.75e-08

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: 54.44  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLdnaAEPESNVEfltQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd13991    14 IGRGSFGEVHRMEDKQtGFQCAVKKV---RLEVFRAE---ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHgrkgVQGAQPGP-TLDWIQRvriavdAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK-AKIADFNLSNQ-SPDMA 274
Cdd:cd13991    88 LIK----EQGCLPEDrALHYLGQ------ALEGLEYLHSR---KILHGDVKADNVLLSSDGSdAFLCDFGHAEClDPDGL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 275 AR--LHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd13991   155 GKslFTGDYIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHP 203
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
116-315 2.78e-08

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 54.82  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYAT-LKDGKAVAVKKLdNAAEPESNVEFLTQVSRVSKLK-HDNFVELFGYC---------VEGNFRI 184
Cdd:cd14036     5 KRVIAEGGFAFVYEAQdVGTGKEYALKRL-LSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSAAsigkeesdqGQAEYLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAyEFATmGSLHDILHgrkgvQGAQPGP-TLDWIqrVRIAVDAARGLEYLHeKVQPAVIHRDIRSSNVLLFEDFKAKIAD 263
Cdd:cd14036    84 LT-ELCK-GQLVDFVK-----KVEAPGPfSPDTV--LKIFYQTCRAVQHMH-KQSPPIIHRDLKIENLLIGNQGQIKLCD 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 264 FNLSN---QSPDMAARLHS--------TRVLgTFGYHAPEYAMTGQ---LTQKSDVYSFGVVLLEL 315
Cdd:cd14036   154 FGSATteaHYPDYSWSAQKrslvedeiTRNT-TPMYRTPEMIDLYSnypIGEKQDIWALGCILYLL 218
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
118-319 3.05e-08

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


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 54.62  E-value: 3.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKDGKA-VAVKKLDNAAEPESNVEF-LTQVSRVSKLKHDNFVELfgycvEGNFR-----ILAYEFA 190
Cdd:cd07848     8 VVGEGAYGVVLKCRHKETKEiVAIKKFKDSEENEEVKETtLRELKMLRTLKQENIVEL-----KEAFRrrgklYLVFEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDIlhgRKGVQGAQPGPTLDWIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQS 270
Cdd:cd07848    83 EKNMLELL---EEMPNGVPPEKVRSYIYQL------IKAIHWCHKN---DIVHRDIKPENLLISHNDVLKLCDFGFARNL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 271 PDmAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07848   151 SE-GSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ 198
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
225-321 3.08e-08

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 55.21  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 225 DAAR----GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS---NQSPDMAarlhsTRVLGTFGYHAPEYAMTg 297
Cdd:PLN00034  172 DVARqilsGIAYLHRR---HIVHRDIKPSNLLINSAKNVKIADFGVSrilAQTMDPC-----NSSVGTIAYMSPERINT- 242
                          90       100       110
                  ....*....|....*....|....*....|
gi 1032291014 298 QLTQ------KSDVYSFGVVLLELLTGRKP 321
Cdd:PLN00034  243 DLNHgaydgyAGDIWSLGVSILEFYLGRFP 272
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
112-321 3.48e-08

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 54.15  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFAT 191
Cdd:cd14193     5 NVNKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 MGSLHDILhgrkgVQGAQPGPTLDWIQRVRiavDAARGLEYLHekvQPAVIHRDIRSSNVLLF--EDFKAKIADFNLSNQ 269
Cdd:cd14193    85 GGELFDRI-----IDENYNLTELDTILFIK---QICEGIQYMH---QMYILHLDLKPENILCVsrEANQVKIIDFGLARR 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 270 -SPDMAARLHstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14193   154 yKPREKLRVN----FGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSP 202
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
116-321 3.78e-08

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: 54.13  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 116 KSLIGEGSYGRAYYATLKDG-KAVAVKKLDNAA--EPESNVEflTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATM 192
Cdd:cd14169     8 KEKLGEGAFSEVVLAQERGSqRLVALKCIPKKAlrGKEAMVE--NEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHDILHGRKGVQGAqpgptlDWIQRVRIAVDAargLEYLHekvQPAVIHRDIRSSNVLL---FEDFKAKIADFNLSNq 269
Cdd:cd14169    86 GELFDRIIERGSYTEK------DASQLIGQVLQA---VKYLH---QLGIVHRDLKPENLLYatpFEDSKIMISDFGLSK- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 270 spdMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14169   153 ---IEAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPP 201
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
222-408 4.01e-08

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 54.30  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 222 IAVDAARGLEYLHEkVQPAVIHRDIRSSNVLLFEDF---KAKIADFNLSNQSPD-----MAARLHSTRVLGTFGYHAPEY 293
Cdd:cd14041   116 IIMQIVNALKYLNE-IKPPIIHYDLKPGNILLVNGTacgEIKITDFGLSKIMDDdsynsVDGMELTSQGAGTYWYLPPEC 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 294 AMTGQ----LTQKSDVYSFGVVLLELLTGRKPVDHTmpRGQQSLvtwatprLSEDKVKQCVDPKLKGEypPKAVAKLAAV 369
Cdd:cd14041   195 FVVGKeppkISNKVDVWSVGVIFYQCLYGRKPFGHN--QSQQDI-------LQENTILKATEVQFPPK--PVVTPEAKAF 263
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1032291014 370 AALCVQYESEFRPNMSIVV--KALQPLLRSSTAAAVPVQEA 408
Cdd:cd14041   264 IRRCLAYRKEDRIDVQQLAcdPYLLPHIRKSVSTSSPAGAA 304
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
119-317 4.08e-08

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 54.20  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLK-HDNFVELFGYCVEGNFRILAYEFATM-GSL 195
Cdd:cd07831     7 IGEGTFSEVLKAqSRKTGKYYAIKCMKKHFKSLEQVNNLREIQALRRLSpHPNILRLIEVLFDRKTGRLALVFELMdMNL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKgvqgaQPGPTldwiQRVR-IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDfKAKIADFNlSNQSpdMA 274
Cdd:cd07831    87 YELIKGRK-----RPLPE----KRVKnYMYQLLKSLDHMHRN---GIFHRDIKPENILIKDD-ILKLADFG-SCRG--IY 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1032291014 275 ARLHSTRVLGTFGYHAPEYAMT-GQLTQKSDVYSFGVVLLELLT 317
Cdd:cd07831   151 SKPPYTEYISTRWYRAPECLLTdGYYGPKMDIWAVGCVFFEILS 194
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
119-319 4.44e-08

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: 54.23  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVelfgycvegnfrilayefatmgSLHD 197
Cdd:cd07872    14 LGEGTYATVFKGRSKlTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIV----------------------TLHD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILHGRKGV------------QGAQPGPTLDWIQRVRIAV-DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd07872    72 IVHTDKSLtlvfeyldkdlkQYMDDCGNIMSMHNVKIFLyQILRGLAYCHRR---KVLHRDLKPQNLLINERGELKLADF 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 265 NLSnQSPDMAARLHSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07872   149 GLA-RAKSVPTKTYSNEVV-TLWYRPPDVLLgSSEYSTQIDMWGVGCIFFEMASGR 202
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
212-317 4.83e-08

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 54.63  E-value: 4.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 212 PTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAP 291
Cdd:cd05107   234 PALSYMDLVGFSYQVANGMEFLASK---NCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAP 310
                          90       100
                  ....*....|....*....|....*.
gi 1032291014 292 EYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd05107   311 ESIFNNLYTTLSDVWSFGILLWEIFT 336
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
138-391 4.94e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 53.80  E-value: 4.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 138 VAVKKLDNAAEPESNvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGvqgaqpgpTLDWI 217
Cdd:cd05078    34 VLLKVLDKAHRNYSE-SFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQEYVKFGSLDTYLKKNKN--------CINIL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 218 QRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLF--EDFKAKIADF-NLSNqsPDMAARLHSTRVL-GTFGYHAPE- 292
Cdd:cd05078   105 WKLEVAKQLAWAMHFLEEK---TLVHGNVCAKNILLIreEDRKTGNPPFiKLSD--PGISITVLPKDILlERIPWVPPEc 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 293 YAMTGQLTQKSDVYSFGVVLLELLTGrkpvdhtmprGQQSLVTWATPRLS---EDkvkqcvdpklKGEYPPKAVAKLAAV 369
Cdd:cd05078   180 IENPKNLSLATDKWSFGTTLWEICSG----------GDKPLSALDSQRKLqfyED----------RHQLPAPKWTELANL 239
                         250       260
                  ....*....|....*....|..
gi 1032291014 370 AALCVQYESEFRPNMSIVVKAL 391
Cdd:cd05078   240 INNCMDYEPDHRPSFRAIIRDL 261
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
121-321 6.43e-08

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 53.19  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 121 EGSYGRAYYATLK------DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFgYCVEGNFRI-LAYEFATM 192
Cdd:cd14074     8 EETLGRGHFAVVKlarhvfTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLvQHPNVVRLY-EVIDTQTKLyLILELGDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 193 GSLHD-ILHGRKGVqgAQPGPTLDWIQRVRiavdaarGLEYLHekvQPAVIHRDIRSSNVLLFEDFK-AKIADFNLSNQ- 269
Cdd:cd14074    87 GDMYDyIMKHENGL--NEDLARKYFRQIVS-------AISYCH---KLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKf 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 270 SPdmAARLHSTrvLGTFGYHAPEYAMTGQL-TQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14074   155 QP--GEKLETS--CGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPP 203
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
118-321 7.02e-08

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: 53.10  E-value: 7.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGKAVAVKKLDNA--AEPESNVEflTQVSRVSKLKHDNFVELFG-YCVEGNFrILAYEFATMG 193
Cdd:cd14095     7 VIGDGNFAVVKECRDKaTDKEYALKIIDKAkcKGKEHMIE--NEVAILRRVKHPNIVQLIEeYDTDTEL-YLVMELVKGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILhgRKGVQGAQPgptldwiQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFED----FKAKIADFNLSNQ 269
Cdd:cd14095    84 DLFDAI--TSSTKFTER-------DASRMVTDLAQALKYLHSL---SIVHRDIKPENLLVVEHedgsKSLKLADFGLATE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 270 SPDmaarLHSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14095   152 VKE----PLFT-VCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPP 198
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
119-319 8.50e-08

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: 8.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLdnAAEPESNVEF--LTQVSRVSKLKHDNFVelfgycvegnfrilayefatmgSL 195
Cdd:cd07844     8 LGEGSYATVYKGRSKlTGQLVALKEI--RLEHEEGAPFtaIREASLLKDLKHANIV----------------------TL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGV------------QGAQPGPTLDWIQRVRIAV-DAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd07844    64 HDIIHTKKTLtlvfeyldtdlkQYMDDCGGGLSMHNVRLFLfQLLRGLAYCHQR---RVLHRDLKPQNLLISERGELKLA 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 263 DFNLSnQSPDMAARLHSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07844   141 DFGLA-RAKSVPSKTYSNEVV-TLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGR 196
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
113-319 8.97e-08

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 53.37  E-value: 8.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESnveFLTQVSR----VSKLKHDNFVELFG-YCVEGNFRILA 186
Cdd:cd07879    17 YTSLKQVGSGAYGSVCSAIdKRTGEKVAIKKLSRPFQSEI---FAKRAYReltlLKHMQHENVIGLLDvFTSAVSGDEFQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLHDILHGRKGVQGAQpgptlDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd07879    94 DFYLVMPYMQTDLQKIMGHPLSE-----DKVQY--LVYQMLCGLKYIHSA---GIIHRDLKPGNLAVNEDCELKILDFGL 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 267 SNQspdmaARLHSTRVLGTFGYHAPEYAMTG-QLTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07879   164 ARH-----ADAEMTGYVVTRWYRAPEVILNWmHYNQTVDIWSVGCIMAEMLTGK 212
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
111-321 9.48e-08

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 53.70  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATL----KDGKA--VAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFR 183
Cdd:cd05106    38 DNLQFGKTLGAGAFGKVVEATAfglgKEDNVlrVAVKMLKASAHTDEREALMSELKILSHLgQHKNIVNLLGACTHGGPV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 184 ILAYEFATMGSLHDILhgRKGVQ---------GAQPGPTLDW----IQRVRIAVDA------------------------ 226
Cdd:cd05106   118 LVITEYCCYGDLLNFL--RKKAEtflnfvmalPEISETSSDYknitLEKKYIRSDSgfssqgsdtyvemrpvsssssqss 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 227 --------------------------ARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL-------SNQSPDM 273
Cdd:cd05106   196 dskdeedtedswpldlddllrfssqvAQGMDFLASK---NCIHRDVAARNVLLTDGRVAKICDFGLardimndSNYVVKG 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 274 AARLhstrvlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05106   273 NARL-------PVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGKSP 314
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
119-324 9.74e-08

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 53.15  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFR--ILAYEFATMGSLH 196
Cdd:cd07867    10 VGRGTYGHVYKAKRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRkvWLLFDYAEHDLWH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKGVQGAQPgptldwIQRVRIAVDA-----ARGLEYLHEKvqpAVIHRDIRSSNVLLF----EDFKAKIADFNLS 267
Cdd:cd07867    90 IIKFHRASKANKKP------MQLPRSMVKSllyqiLDGIHYLHAN---WVLHRDLKPANILVMgegpERGRVKIADMGFA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 268 N--QSPdMAARLHSTRVLGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLTGrKPVDH 324
Cdd:cd07867   161 RlfNSP-LKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTS-EPIFH 218
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
110-321 1.11e-07

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 53.10  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 110 TDNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDNAA-EPESNVEFLTQVSrvsklKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd14176    18 TDGYEVKEDIGVGSYSVCKRCIHKAtNMEFAVKIIDKSKrDPTEEIEILLRYG-----QHPNIITLKDVYDDGKYVYVVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGRKGVQGAQPGPTLDWIQRVriavdaargLEYLHEKvqpAVIHRDIRSSNVLLFEDF----KAKIAD 263
Cdd:cd14176    93 ELMKGGELLDKILRQKFFSEREASAVLFTITKT---------VEYLHAQ---GVVHRDLKPSNILYVDESgnpeSIRICD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 264 FNLSNQ---------SPDMAARLHSTRVLGTFGYHApeyamtgqltqKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14176   161 FGFAKQlraengllmTPCYTANFVAPEVLERQGYDA-----------ACDIWSLGVLLYTMLTGYTP 216
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
119-319 1.16e-07

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 52.92  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLK-HDNFVELFGYCVEGNFRILAYEFatM-GSL 195
Cdd:cd07830     7 LGDGTFGSVYLARNKEtGELVAIKKMKKKFYSWEECMNLREVKSLRKLNeHPNIVKLKEVFRENDELYFVFEY--MeGNL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGvqGAQPGPTL-DWIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS----NQS 270
Cdd:cd07830    85 YQLMKDRKG--KPFSESVIrSIIYQI------LQGLAHIHKH---GFFHRDLKPENLLVSGPEVVKIADFGLAreirSRP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 271 PdmaarlhSTRVLGTFGYHAPE-------YamtgqlTQKSDVYSFGVVLLELLTGR 319
Cdd:cd07830   154 P-------YTDYVSTRWYRAPEillrstsY------SSPVDIWALGCIMAELYTLR 196
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
113-352 1.18e-07

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


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 52.39  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 113 FGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNA-------------AEPESNVEFLtqvSRVSKLKHDNFVELFGYCV 178
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKsKGKEVVIKFIFKErilvdtwvrdrklGTVPLEIHIL---DTLNKRSHPNIVKLLDFFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 179 -EGNFRILAYEFATMGSLHDILHGRkgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd14004    79 dDEFYYLVMEKHGSGMDLFDFIERK---------PNMDEKEAKYIFRQVADAVKHLHDQ---GIVHRDIKDENVILDGNG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 258 KAKIADFNlsnqspdMAARLHSTR---VLGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLTGRKP---VDHTMPRGQ 330
Cdd:cd14004   147 TIKLIDFG-------SAAYIKSGPfdtFVGTIDYAAPEVLRGNPyGGKEQDIWALGVLLYTLVFKENPfynIEEILEADL 219
                         250       260
                  ....*....|....*....|..
gi 1032291014 331 QslVTWATPRLSEDKVKQCVDP 352
Cdd:cd14004   220 R--IPYAVSEDLIDLISRMLNR 239
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
110-321 1.31e-07

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 52.71  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 110 TDNFGSKSLIGEGSYGRAYYATLKDGKA-VAVKKLDNAA-EPESNVEFLTQVSrvsklKHDNFVELFGYCVEGNFRILAY 187
Cdd:cd14178     2 TDGYEIKEDIGIGSYSVCKRCVHKATSTeYAVKIIDKSKrDPSEEIEILLRYG-----QHPNIITLKDVYDDGKFVYLVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGRKGVQGAQPGPTLDWIQRVriavdaargLEYLHEKvqpAVIHRDIRSSNVLLFEDF----KAKIAD 263
Cdd:cd14178    77 ELMRGGELLDRILRQKCFSEREASAVLCTITKT---------VEYLHSQ---GVVHRDLKPSNILYMDESgnpeSIRICD 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 264 FNLSNQ---------SPDMAARLHSTRVLGTFGYHApeyamtgqltqKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14178   145 FGFAKQlraengllmTPCYTANFVAPEVLKRQGYDA-----------ACDIWSLGILLYTMLAGFTP 200
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
110-321 1.65e-07

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 52.32  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 110 TDNFGSKSLIGEGSYG---RAYYATlkDGKAVAVKKLDNAA-EPESNVEFLTQVSrvsklKHDNFVELFGYCVEGNFRIL 185
Cdd:cd14177     3 TDVYELKEDIGVGSYSvckRCIHRA--TNMEFAVKIIDKSKrDPSEEIEILMRYG-----QHPNIITLKDVYDDGRYVYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 186 AYEFATMGSLHDILHGRKGVQGAQPGPTLDWIQRVriavdaargLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA----KI 261
Cdd:cd14177    76 VTELMKGGELLDRILRQKFFSEREASAVLYTITKT---------VDYLHCQ---GVVHRDLKPSNILYMDDSANadsiRI 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 262 ADFNLSNQspdmaARLHSTRVLG---TFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14177   144 CDFGFAKQ-----LRGENGLLLTpcyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTP 201
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
115-321 1.82e-07

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 52.30  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 115 SKSLIGEGSYGRAY---YATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSK-LKHDNFVELFGYCVEGNFRILAYEFA 190
Cdd:cd08216     2 LLYEIGKCFKGGGVvhlAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRqLQHPNILPYVTSFVVDNDLYVVTPLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDIL--HGRKGVqgaqPGPTLDWIQRvriavDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNlSN 268
Cdd:cd08216    82 AYGSCRDLLktHFPEGL----PELAIAFILR-----DVLNALEYIHSK---GYIHRSVKASHILISGDGKVVLSGLR-YA 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 269 QSPDMAAR---------LHSTRVLGtfgYHAPEyaMTGQ----LTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd08216   149 YSMVKHGKrqrvvhdfpKSSEKNLP---WLSPE--VLQQnllgYNEKSDIYSVGITACELANGVVP 209
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
229-321 1.83e-07

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 52.19  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqSPDMAARLHSTR-VLGTFGYHAPEYAMTGQLTQKSDVYS 307
Cdd:cd05608   117 GLEHLHQR---RIIYRDLKPENVLLDDDGNVRISDLGL---AVELKDGQTKTKgYAGTPGFMAPELLLGEEYDYSVDYFT 190
                          90
                  ....*....|....
gi 1032291014 308 FGVVLLELLTGRKP 321
Cdd:cd05608   191 LGVTLYEMIAARGP 204
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
242-352 2.06e-07

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 52.32  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 242 IHRDIRSSNVLLFEDFKAKIADFNL-------SNQSPDMAarlHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLE 314
Cdd:cd05598   123 IHRDIKPDNILIDRDGHIKLTDFGLctgfrwtHDSKYYLA---HS--LVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYE 197
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 315 LLTGRKP-VDHTMPRGQQSLVTW-------ATPRLSEDK----VKQCVDP 352
Cdd:cd05598   198 MLVGQPPfLAQTPAETQLKVINWrttlkipHEANLSPEAkdliLRLCCDA 247
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
119-321 2.33e-07

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 52.11  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFR--ILAYEFATMGSL 195
Cdd:cd13988     1 LGQGATANVFRGRHKkTGDLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTTRhkVLVMELCPCGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHGRKGVQGAqpgPTLDWIQRVRiavDAARGLEYLHEKvqpAVIHRDIRSSNVLLF--EDFKA--KIADFNLSNQSP 271
Cdd:cd13988    81 YTVLEEPSNAYGL---PESEFLIVLR---DVVAGMNHLREN---GIVHRDIKPGNIMRVigEDGQSvyKLTDFGAARELE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 272 DMAarlHSTRVLGTFGYHAP---EYAMTGQLTQKS-----DVYSFGVVLLELLTGRKP 321
Cdd:cd13988   152 DDE---QFVSLYGTEEYLHPdmyERAVLRKDHQKKygatvDLWSIGVTFYHAATGSLP 206
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
229-321 2.64e-07

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 51.90  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmaARLHSTRVlGTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd05632   116 GLEDLH---RENTVYRDLKPENILLDDYGHIRISDLGLAVKIPE--GESIRGRV-GTVGYMAPEVLNNQRYTLSPDYWGL 189
                          90
                  ....*....|...
gi 1032291014 309 GVVLLELLTGRKP 321
Cdd:cd05632   190 GCLIYEMIEGQSP 202
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
119-324 2.66e-07

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 51.98  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDG---KAVAVKKLDNAAEPESNVEfltQVSRVSKLKHDNFVELFGYCVEGNFR--ILAYEFATMG 193
Cdd:cd07868    25 VGRGTYGHVYKAKRKDGkddKDYALKQIEGTGISMSACR---EIALLRELKHPNVISLQKVFLSHADRkvWLLFDYAEHD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGVQGAQPgptldwIQRVRIAVDA-----ARGLEYLHEKvqpAVIHRDIRSSNVLLF----EDFKAKIADF 264
Cdd:cd07868   102 LWHIIKFHRASKANKKP------VQLPRGMVKSllyqiLDGIHYLHAN---WVLHRDLKPANILVMgegpERGRVKIADM 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 265 NLSN--QSPdMAARLHSTRVLGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLTGrKPVDH 324
Cdd:cd07868   173 GFARlfNSP-LKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTS-EPIFH 233
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
155-355 2.71e-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: 51.65  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 155 FLTQVSRVSKLKHDNFVELFGY---------CVegnfrILAYEFATMGSLHDILhgrKGVQGAQPGPTLDWIQRVriavd 225
Cdd:cd14031    56 FKEEAEMLKGLQHPNIVRFYDSwesvlkgkkCI-----VLVTELMTSGTLKTYL---KRFKVMKPKVLRSWCRQI----- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 226 aARGLEYLHEKVqPAVIHRDIRSSNVLLF-EDFKAKIADFNLSNQSPDMAARlhstRVLGTFGYHAPEyAMTGQLTQKSD 304
Cdd:cd14031   123 -LKGLQFLHTRT-PPIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTSFAK----SVIGTPEFMAPE-MYEEHYDESVD 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032291014 305 VYSFGVVLLELLTGRKPVDHTMPRGQqsLVTWATPRLSEDKVKQCVDPKLK 355
Cdd:cd14031   196 VYAFGMCMLEMATSEYPYSECQNAAQ--IYRKVTSGIKPASFNKVTDPEVK 244
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
119-328 2.82e-07

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 51.52  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEflTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd14665     8 IGSGNFGVARLMRDKqTKELVAVKYIERGEKIDENVQ--REIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGGELFE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgAQPGptldwiqrvRIAVDAAR--------GLEYLHEKvqpAVIHRDIRSSNVLL--FEDFKAKIADFNLS 267
Cdd:cd14665    86 RI--------CNAG---------RFSEDEARfffqqlisGVSYCHSM---QICHRDLKLENTLLdgSPAPRLKICDFGYS 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 268 NQSpdmaaRLHST--RVLGTFGYHAPEYAMTGQLTQK-SDVYSFGVVLLELLTGRKPV-DHTMPR 328
Cdd:cd14665   146 KSS-----VLHSQpkSTVGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFeDPEEPR 205
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
230-324 3.00e-07

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 51.97  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 230 LEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAArlhSTRVL-GTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd05571   108 LGYLHSQ---GIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGA---TTKTFcGTPEYLAPEVLEDNDYGRAVDWWGL 181
                          90
                  ....*....|....*....
gi 1032291014 309 GVVLLELLTGRKPV---DH 324
Cdd:cd05571   182 GVVMYEMMCGRLPFynrDH 200
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
223-321 3.29e-07

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: 51.99  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 223 AVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNL----SNQSPdmaarlHSTrvLGTFGYHAPEYAMTGQ 298
Cdd:cd05633   114 ATEIILGLEHMHNRF---VVYRDLKPANILLDEHGHVRISDLGLacdfSKKKP------HAS--VGTHGYMAPEVLQKGT 182
                          90       100
                  ....*....|....*....|....
gi 1032291014 299 LTQKS-DVYSFGVVLLELLTGRKP 321
Cdd:cd05633   183 AYDSSaDWFSLGCMLFKLLRGHSP 206
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
119-321 3.55e-07

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: 51.07  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEflTQVSR----VSKLKHDNFVELFGYCVEGNFRILAYEFATMG 193
Cdd:cd05572     1 LGVGGFGRVELVQLKsKGRTFALKCVKKRHIVQTRQQ--EHIFSekeiLEECNSPFIVKLYRTFKDKKYLYMLMEYCLGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRkgvqgaqpGPTLDWIQRVRIA--VDAargLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqsp 271
Cdd:cd05572    79 ELWTILRDR--------GLFDEYTARFYTAcvVLA---FEYLHSR---GIIYRDLKPENLLLDSNGYVKLVDFGF----- 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 272 dmAARLHSTR----VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05572   140 --AKKLGSGRktwtFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPP 191
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
119-328 3.77e-07

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 51.80  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVS-KLKHDNF-VELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd05610    12 ISRGAFGKVYLGRKKnNSKLYAVKVVKKADMINKNMVHQVQAERDAlALSKSPFiVHLYYSLQSANNVYLVMEYLIGGDV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILHgrkgVQGaqpgpTLDWIQRVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSN------- 268
Cdd:cd05610    92 KSLLH----IYG-----YFDEEMAVKYISEVALALDYLH---RHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnrel 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 269 ------QSPDMA--------------------------------------ARLHSTRVLGTFGYHAPEYAMTGQLTQKSD 304
Cdd:cd05610   160 nmmdilTTPSMAkpkndysrtpgqvlslisslgfntptpyrtpksvrrgaARVEGERILGTPDYLAPELLLGKPHGPAVD 239
                         250       260
                  ....*....|....*....|....
gi 1032291014 305 VYSFGVVLLELLTGRKPVDHTMPR 328
Cdd:cd05610   240 WWALGVCLFEFLTGIPPFNDETPQ 263
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
118-321 4.87e-07

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 51.12  E-value: 4.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGKAVAVKKLDNAA---EPESNVEFLTQVSRVSKLKHDNFVELFgycvegnfrilaYEFATMG 193
Cdd:cd05603     2 VIGKGSFGKVLLAKRKcDGKFYAVKVLQKKTilkKKEQNHIMAERNVLLKNLKHPFLVGLH------------YSFQTSE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHGRKGvqgaqpGPTLDWIQRVR---------IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF 264
Cdd:cd05603    70 KLYFVLDYVNG------GELFFHLQRERcfleprarfYAAEVASAIGYLHSL---NIIYRDLKPENILLDCQGHVVLTDF 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 265 NLSNQSpdMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05603   141 GLCKEG--MEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPP 195
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
107-321 5.24e-07

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: 51.24  E-value: 5.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 107 KEKTDN-FGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAE-PESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFR 183
Cdd:cd05593    10 KRKTMNdFDYLKLLGKGTFGKVILVREKaSGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 184 I-LAYEFATMGSLHDILhGRKGVQGAQpgptldwiqRVRI-AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKI 261
Cdd:cd05593    90 LcFVMEYVNGGELFFHL-SRERVFSED---------RTRFyGAEIVSALDYLHSG---KIVYRDLKLENLMLDKDGHIKI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 262 ADFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05593   157 TDFGLCKEGITDAATMKT--FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 214
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
140-324 5.78e-07

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 50.68  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 140 VKKLDNAAEPEsnVEFLTQVSrvsklKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKgvqgaqpgpTLDWIQR 219
Cdd:cd14182    49 VQELREATLKE--IDILRKVS-----GHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKV---------TLSEKET 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 220 VRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmAARLHstRVLGTFGYHAPEY---AMT 296
Cdd:cd14182   113 RKIMRALLEVICALHKL---NIVHRDLKPENILLDDDMNIKLTDFGFSCQLDP-GEKLR--EVCGTPGYLAPEIiecSMD 186
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1032291014 297 GQ---LTQKSDVYSFGVVLLELLTGRKPVDH 324
Cdd:cd14182   187 DNhpgYGKEVDMWSTGVIMYTLLAGSPPFWH 217
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
118-347 5.79e-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: 50.67  E-value: 5.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSR-VSKLKHDNFVELFGYCVEGNFRI-LAYEFATMGS 194
Cdd:cd05607     9 VLGKGGFGEVCAVQVKNtGQMYACKKLDKKRLKKKSGEKMALLEKeILEKVNSPFIVSLAYAFETKTHLcLVMSLMNGGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 L-HDILH-GRKGVQgaqpgptldwIQRV-RIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSP 271
Cdd:cd05607    89 LkYHIYNvGERGIE----------MERViFYSAQITCGILHLHSL---KIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 272 DMAArlhSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPV-DHTMPRGQQSLVTwatpRLSEDKVK 347
Cdd:cd05607   156 EGKP---ITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFrDHKEKVSKEELKR----RTLEDEVK 225
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
230-321 6.83e-07

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 50.87  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 230 LEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFG 309
Cdd:cd05584   113 LGHLHSL---GIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHT--FCGTIEYMAPEILTRSGHGKAVDWWSLG 187
                          90
                  ....*....|..
gi 1032291014 310 VVLLELLTGRKP 321
Cdd:cd05584   188 ALMYDMLTGAPP 199
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
155-355 7.70e-07

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: 50.08  E-value: 7.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 155 FLTQVSRVSKLKHDNFVELFGY---------CVegnfrILAYEFATMGSLHDILhgrKGVQGAQPGPTLDWIQRVriavd 225
Cdd:cd14032    47 FKEEAEMLKGLQHPNIVRFYDFwescakgkrCI-----VLVTELMTSGTLKTYL---KRFKVMKPKVLRSWCRQI----- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 226 aARGLEYLHEKVqPAVIHRDIRSSNVLLF-EDFKAKIADFNLSNQSPDMAARlhstRVLGTFGYHAPEyAMTGQLTQKSD 304
Cdd:cd14032   114 -LKGLLFLHTRT-PPIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRASFAK----SVIGTPEFMAPE-MYEEHYDESVD 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 305 VYSFGVVLLELLTGRKPVDHTMPRGQ-QSLVTWATPRLSEDKVKqcvDPKLK 355
Cdd:cd14032   187 VYAFGMCMLEMATSEYPYSECQNAAQiYRKVTCGIKPASFEKVT---DPEIK 235
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
118-321 8.05e-07

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: 50.27  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLKD-GKAVAVKKLDNAAepesnVEFLTQVSRV-------SKLKHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd05580     8 TLGTGSFGRVRLVKHKDsGKYYALKILKKAK-----IIKLKQVEHVlnekrilSEVRHPFIVNLLGSFQDDRNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILhgRKgvqgaqpgptldwiqRVRIAVDAAR--------GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKI 261
Cdd:cd05580    83 VPGGELFSLL--RR---------------SGRFPNDVAKfyaaevvlALEYLHSL---DIVYRDLKPENLLLDSDGHIKI 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 262 ADFNLSNQSPDmaaRLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05580   143 TDFGFAKRVKD---RTYT--LCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPP 197
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
212-321 8.07e-07

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: 50.38  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 212 PTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDmaARLHSTRVlGTFGYHAP 291
Cdd:cd05631    97 PGFDEQRAIFYAAELCCGLEDLQRE---RIVYRDLKPENILLDDRGHIRISDLGLAVQIPE--GETVRGRV-GTVGYMAP 170
                          90       100       110
                  ....*....|....*....|....*....|
gi 1032291014 292 EYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05631   171 EVINNEKYTFSPDWWGLGCLIYEMIQGQSP 200
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
111-321 8.44e-07

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 50.41  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAA-EPESNVEFLTQVSrvsklKHDNFVELFGYCVEGNFRILAYE 188
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKaTNMEYAVKVIDKSKrDPSEEIEILLRYG-----QHPNIITLKDVYDDGKHVYLVTE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHDILHGRKGVQGAQPGPTLDWIqrvriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF----KAKIADF 264
Cdd:cd14175    76 LMRGGELLDKILRQKFFSEREASSVLHTI---------CKTVEYLHSQ---GVVHRDLKPSNILYVDESgnpeSLRICDF 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 265 NLSNQ---------SPDMAARLHSTRVLGTFGYhapeyamtgqlTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14175   144 GFAKQlraengllmTPCYTANFVAPEVLKRQGY-----------DEGCDIWSLGILLYTMLAGYTP 198
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
221-318 9.19e-07

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 50.27  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 221 RIAVDAARGLEYLHEKVQpaVIHRDIRSSNVLL-FEDFKAKIADFNLSNQSpdmaaRLHSTRVLGTFGYHAPEYAMTGQL 299
Cdd:cd14136   123 KIARQVLQGLDYLHTKCG--IIHTDIKPENVLLcISKIEVKIADLGNACWT-----DKHFTEDIQTRQYRSPEVILGAGY 195
                          90
                  ....*....|....*....
gi 1032291014 300 TQKSDVYSFGVVLLELLTG 318
Cdd:cd14136   196 GTPADIWSTACMAFELATG 214
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
112-321 1.14e-06

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: 50.05  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 112 NFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCvegnfriLAYEFA 190
Cdd:cd14223     1 DFSVHRIIGRGGFGEVYGCRKADtGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVC-------MSYAFH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRKG----VQGAQPGPTLDWIQRVrIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNL 266
Cdd:cd14223    74 TPDKLSFILDLMNGgdlhYHLSQHGVFSEAEMRF-YAAEIILGLEHMHSRF---VVYRDLKPANILLDEFGHVRISDLGL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 267 ----SNQSPdmaarlHSTrvLGTFGYHAPEYAMTGQLTQKS-DVYSFGVVLLELLTGRKP 321
Cdd:cd14223   150 acdfSKKKP------HAS--VGTHGYMAPEVLQKGVAYDSSaDWFSLGCMLFKLLRGHSP 201
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
119-321 1.27e-06

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


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 49.26  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGR---AYYATLKDgkAVAVKKLDNAAEPESNVEFLTQ-VSRVSKLKHDNFVELFgYCVEGNFRI-LAYEFATMG 193
Cdd:cd14075    10 LGSGNFSQvklGIHQLTKE--KVAIKILDKTKLDQKTQRLLSReISSMEKLHHPNIIRLY-EVVETLSKLhLVMEYASGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 194 SLHDILHgrkgvqgaQPGPTLDWIQRVRIA--VDAargLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSp 271
Cdd:cd14075    87 ELYTKIS--------TEGKLSESEAKPLFAqiVSA---VKHMHEN---NIIHRDLKAENVFYASNNCVKVGDFGFSTHA- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 272 dmaarlHSTRVLGTF----GYHAPE------YAmtGQLTqksDVYSFGVVLLELLTGRKP 321
Cdd:cd14075   152 ------KRGETLNTFcgspPYAAPElfkdehYI--GIYV---DIWALGVLLYFMVTGVMP 200
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
229-321 1.52e-06

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 49.61  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLhSTrVLGTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd05589   113 GLQFLHEH---KIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRT-ST-FCGTPEFLAPEVLTDTSYTRAVDWWGL 187
                          90
                  ....*....|...
gi 1032291014 309 GVVLLELLTGRKP 321
Cdd:cd05589   188 GVLIYEMLVGESP 200
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
231-321 1.69e-06

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 49.43  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 231 EYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLhstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGV 310
Cdd:PTZ00263  132 EYLHSK---DIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTL-----CGTPEYLAPEVIQSKGHGKAVDWWTMGV 203
                          90
                  ....*....|.
gi 1032291014 311 VLLELLTGRKP 321
Cdd:PTZ00263  204 LLYEFIAGYPP 214
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
136-321 1.69e-06

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 49.44  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 136 KAVAVKKLDNAAEPESnveFLTQVSRVSKLKHDNFV---ELFgycvEGNFRI-LAYEFATMGSLHDILHgRKGVQGAqpg 211
Cdd:cd14085    29 KPYAVKKLKKTVDKKI---VRTEIGVLLRLSHPNIIklkEIF----ETPTEIsLVLELVTGGELFDRIV-EKGYYSE--- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 212 ptldwiqrvRIAVDAAR----GLEYLHEKvqpAVIHRDIRSSNVLLF---EDFKAKIADFNLSNQSPDmaaRLHSTRVLG 284
Cdd:cd14085    98 ---------RDAADAVKqileAVAYLHEN---GIVHRDLKPENLLYAtpaPDAPLKIADFGLSKIVDQ---QVTMKTVCG 162
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1032291014 285 TFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14085   163 TPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEP 199
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
230-334 1.70e-06

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 49.46  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 230 LEYLHEKvqpAVIHRDIRSSNVLLF-EDFKA--KIADFNLSNQSPDMAARLHStRVlGTFGYHAPEYAMTGQLTQKSDVY 306
Cdd:cd14094   122 LRYCHDN---NIIHRDVKPHCVLLAsKENSApvKLGGFGVAIQLGESGLVAGG-RV-GTPHFMAPEVVKREPYGKPVDVW 196
                          90       100
                  ....*....|....*....|....*...
gi 1032291014 307 SFGVVLLELLTGRKPVDHTMPRGQQSLV 334
Cdd:cd14094   197 GCGVILFILLSGCLPFYGTKERLFEGII 224
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
185-321 2.04e-06

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 48.89  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 185 LAYEFATMGSLHDILHGRKGvqG---------AQPGPTldwIQRVRI-AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLF 254
Cdd:cd05605    65 LAYAYETKDALCLVLTIMNG--GdlkfhiynmGNPGFE---EERAVFyAAEITCGLEHLHSE---RIVYRDLKPENILLD 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 255 EDFKAKIADFNLSNQSPDmaARLHSTRVlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05605   137 DHGHVRISDLGLAVEIPE--GETIRGRV-GTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAP 200
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
218-321 2.13e-06

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 48.77  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 218 QRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF---KAKIADFNLSNQSPDmAARLHstRVLGTFGYHAPEYA 294
Cdd:cd14198   111 DIIRLIRQILEGVYYLHQN---NIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKIGH-ACELR--EIMGTPEYLAPEIL 184
                          90       100
                  ....*....|....*....|....*..
gi 1032291014 295 MTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14198   185 NYDPITTATDMWNIGVIAYMLLTHESP 211
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
119-321 2.26e-06

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 48.73  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDI 198
Cdd:cd14114    10 LGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELFER 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 199 LhgrkgvqgAQPGPTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVlLFEDFKA---KIADFNLSNQ-SPDMA 274
Cdd:cd14114    90 I--------AAEHYKMSEAEVINYMRQVCEGLCHMHEN---NIVHLDIKPENI-MCTTKRSnevKLIDFGLATHlDPKES 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032291014 275 ARLHStrvlGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14114   158 VKVTT----GTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSP 200
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
121-321 2.78e-06

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


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 48.46  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 121 EGSYGRAYYAtlkdgKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILH 200
Cdd:cd14195    26 EKGTGKEYAA-----KFIKKRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLILELVSGGELFDFLA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 201 GRKGVQGAQPGPTLDWIqrvriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFE----DFKAKIADFNLSNQspdMAAR 276
Cdd:cd14195   101 EKESLTEEEATQFLKQI---------LDGVHYLHSK---RIAHFDLKPENIMLLDknvpNPRIKLIDFGIAHK---IEAG 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1032291014 277 LHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14195   166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP 210
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
107-324 2.79e-06

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


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 48.43  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 107 KEKTDNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDNAAE---PES----------NVEFLTQVSrvsklKHDNFVE 172
Cdd:cd14181     6 KEFYQKYDPKEVIGRGVSSVVRRCVHRHtGQEFAVKIIEVTAErlsPEQleevrsstlkEIHILRQVS-----GHPSIIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 173 LFGYCVEGNFRILAYEFATMGSLHDILHGRKgvqgaqpgpTLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVL 252
Cdd:cd14181    81 LIDSYESSTFIFLVFDLMRRGELFDYLTEKV---------TLSEKETRSIMRSLLEAVSYLHAN---NIVHRDLKPENIL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 253 LFEDFKAKIADFNLSNQ-SPDMAARlhstRVLGTFGYHAPEYAMTGQ------LTQKSDVYSFGVVLLELLTGRKPVDH 324
Cdd:cd14181   149 LDDQLHIKLSDFGFSCHlEPGEKLR----ELCGTPGYLAPEILKCSMdethpgYGKEVDLWACGVILFTLLAGSPPFWH 223
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
223-323 2.88e-06

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: 48.86  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 223 AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpdMAARLHSTRVLGTFGYHAPEYAMTGQLTQK 302
Cdd:cd05617   122 AAEICIALNFLHER---GIIYRDLKLDNVLLDADGHIKLTDYGMCKEG--LGPGDTTSTFCGTPNYIAPEILRGEEYGFS 196
                          90       100
                  ....*....|....*....|.
gi 1032291014 303 SDVYSFGVVLLELLTGRKPVD 323
Cdd:cd05617   197 VDWWALGVLMFEMMAGRSPFD 217
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
227-317 3.50e-06

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 48.87  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 227 ARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVY 306
Cdd:cd05105   247 ARGMEFLASK---NCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVW 323
                          90
                  ....*....|.
gi 1032291014 307 SFGVVLLELLT 317
Cdd:cd05105   324 SYGILLWEIFS 334
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
195-321 3.70e-06

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: 48.33  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKGVQGAQPGPTLDWIQRVRI-----AVDAARGL----EYLHEKvqpAVIHRDIRSSNVLLFEDFKA---KIA 262
Cdd:cd14180    70 LHDQYHTYLVMELLRGGELLDRIKKKARfseseASQLMRSLvsavSFMHEA---GVVHRDLKPENILYADESDGavlKVI 146
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 263 DFNLSNQSPDMAARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14180   147 DFGFARLRPQGSRPLQTPCF--TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVP 203
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
228-316 4.43e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 48.33  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 228 RGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSnQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYS 307
Cdd:PHA03209  168 EGLRYLH---AQRIIHRDVKTENIFINDVDQVCIGDLGAA-QFPVVAPAFLG--LAGTVETNAPEVLARDKYNSKADIWS 241

                  ....*....
gi 1032291014 308 FGVVLLELL 316
Cdd:PHA03209  242 AGIVLFEML 250
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
155-326 4.43e-06

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 48.01  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 155 FLTQVSRVSKLK-HDNFVELFG-----YCVEGNFRILAYEFATMgSLHDILhgrkgVQGAQPGPTLDWIQRVriAVDAAR 228
Cdd:cd14020    50 FAKERAALEQLQgHRNIVTLYGvftnhYSANVPSRCLLLELLDV-SVSELL-----LRSSNQGCSMWMIQHC--ARDVLE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA-KIADFNLSNQSPDmaarlHSTRVLGTFGYHAPEYAMTGQLTQKS---- 303
Cdd:cd14020   122 ALAFLHHE---GYVHADLKPRNILWSAEDECfKLIDFGLSFKEGN-----QDVKYIQTDGYRAPEAELQNCLAQAGlqse 193
                         170       180       190
                  ....*....|....*....|....*....|
gi 1032291014 304 -------DVYSFGVVLLELLTGRKpVDHTM 326
Cdd:cd14020   194 tectsavDLWSLGIVLLEMFSGMK-LKHTV 222
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
87-321 4.83e-06

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: 48.10  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  87 PDALKEPPSIDVpalSLDELKEKT--DNFGSKSLIGEGSYGRA----------YYATLKDGKAVAVKKlDNAAEPesnve 154
Cdd:cd05594     2 PSDNSGAEEMEV---SLTKPKHKVtmNDFEYLKLLGKGTFGKVilvkekatgrYYAMKILKKEVIVAK-DEVAHT----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 155 fLTQvSRVSKLKHDNFVELFGYCVEGNFRI-LAYEFATMGSLhdILHGRKGVQGAQpgptldwiQRVRI-AVDAARGLEY 232
Cdd:cd05594    73 -LTE-NRVLQNSRHPFLTALKYSFQTHDRLcFVMEYANGGEL--FFHLSRERVFSE--------DRARFyGAEIVSALDY 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 233 LHEKVQpaVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVL 312
Cdd:cd05594   141 LHSEKN--VVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKT--FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVM 216

                  ....*....
gi 1032291014 313 LELLTGRKP 321
Cdd:cd05594   217 YEMMCGRLP 225
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
118-321 5.94e-06

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 47.65  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGycvegnfriLAYEFATMGSLH 196
Cdd:cd05604     3 VIGKGSFGKVLLAKRKrDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVG---------LHYSFQTTDKLY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKGvqgaqpGPTLDWIQRVR---------IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLS 267
Cdd:cd05604    74 FVLDFVNG------GELFFHLQRERsfpeprarfYAAEIASALGYLHSI---NIVYRDLKPENILLDSQGHIVLTDFGLC 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 268 NQSpdMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05604   145 KEG--ISNSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPP 196
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
117-351 6.12e-06

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 47.23  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKLdnaaePESNVEFLTQVS-------------RVSKLKHDNFVELFGYCVEGNF 182
Cdd:cd14005     6 DLLGKGGFGTVYSGVrIRDGLPVAVKFV-----PKSRVTEWAMINgpvpvpleialllKASKPGVPGVIRLLDWYERPDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 183 RILAYEfatmgslhdilhgrkgvqgaQPGPT---LDWI-QRVRIAVDAARGL-----EYLHEKVQPAVIHRDIRSSNVLL 253
Cdd:cd14005    81 FLLIME--------------------RPEPCqdlFDFItERGALSENLARIIfrqvvEAVRHCHQRGVLHRDIKDENLLI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 254 -FEDFKAKIADFNlsnqspdMAARLHS---TRVLGTFGYHAPEYAMTGQ-LTQKSDVYSFGVVLLELLTGRKPVDHTmpr 328
Cdd:cd14005   141 nLRTGEVKLIDFG-------CGALLKDsvyTDFDGTRVYSPPEWIRHGRyHGRPATVWSLGILLYDMLCGDIPFEND--- 210
                         250       260
                  ....*....|....*....|....*.
gi 1032291014 329 gqQSLVTWAT---PRLSedkvKQCVD 351
Cdd:cd14005   211 --EQILRGNVlfrPRLS----KECCD 230
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
157-333 6.61e-06

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: 47.25  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 157 TQVSRVSKLKHDNFVELFG-YCVEGNFrILAYEFATMGSLHDILhgRKGVQGAQPGPTLdwiqrvrIAVDAARGLEYLHE 235
Cdd:cd14185    47 SEILIIKSLSHPNIVKLFEvYETEKEI-YLILEYVRGGDLFDAI--IESVKFTEHDAAL-------MIIDLCEALVYIHS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 236 KvqpAVIHRDIRSSNVLLFEDFKA----KIADFNLSnqspdmaarLHSTR----VLGTFGYHAPEYAMTGQLTQKSDVYS 307
Cdd:cd14185   117 K---HIVHRDLKPENLLVQHNPDKsttlKLADFGLA---------KYVTGpiftVCGTPTYVAPEILSEKGYGLEVDMWA 184
                         170       180
                  ....*....|....*....|....*.
gi 1032291014 308 FGVVLLELLTGRKPVdHTMPRGQQSL 333
Cdd:cd14185   185 AGVILYILLCGFPPF-RSPERDQEEL 209
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
118-316 7.96e-06

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: 47.28  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKLDNAAEPESNVeFLTQVSRVSKLK-HDNFVELFGYCV----EGNFRILAY-EFA 190
Cdd:cd14037    10 YLAEGGFAHVYLVkTSNGGNRAALKRVYVNDEHDLNV-CKREIEIMKRLSgHKNIVGYIDSSAnrsgNGVYEVLLLmEYC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 191 TMGSLHDILHGRkgvqgAQPGPTLDWIqrVRIAVDAARGLEYLHEkVQPAVIHRDIRSSNVLLFEDFKAKIADF------ 264
Cdd:cd14037    89 KGGGVIDLMNQR-----LQTGLTESEI--LKIFCDVCEAVAAMHY-LKPPLIHRDLKVENVLISDSGNYKLCDFgsattk 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 265 NLSNQSPD-MAARLHSTRVLGTFGYHAPEYA--MTGQ-LTQKSDVYSFGVVLLELL 316
Cdd:cd14037   161 ILPPQTKQgVTYVEEDIKKYTTLQYRAPEMIdlYRGKpITEKSDIWALGCLLYKLC 216
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
158-321 8.90e-06

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 46.94  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 158 QVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGVQGAQPGPTLDWIqrvriavdaARGLEYLHEKv 237
Cdd:cd14194    58 EVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQI---------LNGVYYLHSL- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 238 qpAVIHRDIRSSNVLLFEDF----KAKIADFNLSNQSpDMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLL 313
Cdd:cd14194   128 --QIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHKI-DFGNEFKN--IFGTPEFVAPEIVNYEPLGLEADMWSIGVITY 202

                  ....*...
gi 1032291014 314 ELLTGRKP 321
Cdd:cd14194   203 ILLSGASP 210
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
122-321 9.03e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.53  E-value: 9.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 122 GSYGRAYYATLKDG---KAVAVKKLDNAAEPESNVEFLTQVSrvsklkHDNFVELfgycvegnfrILAYEFATMGSL--- 195
Cdd:PHA03207  103 GSEGEVFVCTKHGDeqrKKVIVKAVTGGKTPGREIDILKTIS------HRAIINL----------IHAYRWKSTVCMvmp 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 ---HDILhgrKGVQGAQPGPTLDWIQRVRIAVDAargLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPD 272
Cdd:PHA03207  167 kykCDLF---TYVDRSGPLPLEQAITIQRRLLEA---LAYLHGR---GIIHRDVKTENIFLDEPENAVLGDFGAACKLDA 237
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1032291014 273 MAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:PHA03207  238 HPDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVT 286
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
105-321 9.31e-06

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: 46.86  E-value: 9.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 105 ELKEKtdnfgskslIGEGSYGRAYYATLK-DGKAVAVKKLDNAA-EPESNVEFLTQVSRvsklkHDNFVELFGYCVEGNF 182
Cdd:cd14091     3 EIKEE---------IGKGSYSVCKRCIHKaTGKEYAVKIIDKSKrDPSEEIEILLRYGQ-----HPNIITLRDVYDDGNS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 183 RILAYEFATMGSLHDILHGRKGVQGAQPGPTLDWIqrvriavdaARGLEYLHEKvqpAVIHRDIRSSNVlLFEDFKA--- 259
Cdd:cd14091    69 VYLVTELLRGGELLDRILRQKFFSEREASAVMKTL---------TKTVEYLHSQ---GVVHRDLKPSNI-LYADESGdpe 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 260 --KIADFNLSNQ---------SPDMAARLHSTRVLGTFGYHApeyamtgqltqKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14091   136 slRICDFGFAKQlraengllmTPCYTANFVAPEVLKKQGYDA-----------ACDIWSLGVLLYTMLAGYTP 197
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
111-321 9.48e-06

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: 47.05  E-value: 9.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKDGKA-VAVKKLDnaaepESNVEFLTQVSRV-------SKLKHDNFVELFGYCVEGNF 182
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHyYALKVMA-----IPEVIRLKQEQHVhnekrvlKEVSHPFIIRLFWTEHDQRF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 183 RILAYEFATMGSLHDILHGRKGVQGAQPgptldwiqrVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIA 262
Cdd:cd05612    76 LYMLMEYVPGGELFSYLRNSGRFSNSTG---------LFYASEIVCALEYLHSK---EIVYRDLKPENILLDKEGHIKLT 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 263 DFNLSNQSPDMAARLhstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05612   144 DFGFAKKLRDRTWTL-----CGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPP 197
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
230-321 9.53e-06

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: 47.18  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 230 LEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSnqSPDMAARLHSTRVLGTFGYHAPEYAMTGQ-LTQKSDVYSF 308
Cdd:cd05586   109 LEHLHKN---DIVYRDLKPENILLDANGHIALCDFGLS--KADLTDNKTTNTFCGTTEYLAPEVLLDEKgYTKMVDFWSL 183
                          90
                  ....*....|...
gi 1032291014 309 GVVLLELLTGRKP 321
Cdd:cd05586   184 GVLVFEMCCGWSP 196
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
230-321 9.77e-06

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 47.28  E-value: 9.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 230 LEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLS----------------NQSPDMAARL-----------HSTRV 282
Cdd:cd05573   114 LDSLH---KLGFIHRDIKPDNILLDADGHIKLADFGLCtkmnksgdresylndsVNTLFQDNVLarrrphkqrrvRAYSA 190
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1032291014 283 LGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05573   191 VGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPP 229
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
217-321 1.20e-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: 46.72  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 217 IQRVR---------IAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpdMAARLHSTRVLGTFG 287
Cdd:cd05591    87 IQRARkfdeprarfYAAEVTLALMFLH---RHGVIYRDLKLDNILLDAEGHCKLADFGMCKEG--ILNGKTTTTFCGTPD 161
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1032291014 288 YHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05591   162 YIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP 195
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
162-344 1.25e-05

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 46.42  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 162 VSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHgRKGVqgAQPGPTLDWIQRVriavdaARGLEYLHEKvqpAV 241
Cdd:cd14107    52 LARLSHRRLTCLLDQFETRKTLILILELCSSEELLDRLF-LKGV--VTEAEVKLYIQQV------LEGIGYLHGM---NI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 242 IHRDIRSSNVLLF----EDFKakIADFNLSnQSPDMAARLHSTrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:cd14107   120 LHLDIKPDNILMVsptrEDIK--ICDFGFA-QEITPSEHQFSK--YGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLT 194
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1032291014 318 GRKPVDHTMPRG-----QQSLVTWATP---RLSED 344
Cdd:cd14107   195 CHSPFAGENDRAtllnvAEGVVSWDTPeitHLSED 229
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
119-321 1.28e-05

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 46.30  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKDGKA-VAVKKLDNAAEPESNV--EFLTQVSrvskLKHDNFVELFGYCVEGNFRILAYEFATMGSL 195
Cdd:cd14662     8 IGSGNFGVARLMRNKETKElVAVKYIERGLKIDENVqrEIINHRS----LRHPNIIRFKEVVLTPTHLAIVMEYAAGGEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 196 HDILhgrkgvqgaqpgptldwIQRVRIAVDAAR--------GLEYLHEKvqpAVIHRDIRSSNVLL--FEDFKAKIADFN 265
Cdd:cd14662    84 FERI-----------------CNAGRFSEDEARyffqqlisGVSYCHSM---QICHRDLKLENTLLdgSPAPRLKICDFG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 266 LSNQSpdmaaRLHS--TRVLGTFGYHAPEYAMTGQLTQK-SDVYSFGVVLLELLTGRKP 321
Cdd:cd14662   144 YSKSS-----VLHSqpKSTVGTPAYIAPEVLSRKEYDGKvADVWSCGVTLYVMLVGAYP 197
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
109-321 1.52e-05

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 46.55  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 109 KTDNFGSKSLIGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGycvegnfriLAY 187
Cdd:cd05602     5 KPSDFHFLKVIGKGSFGKVLLARHKsDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVG---------LHF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGRKGvqgaqpGPTLDWIQRVRI---------AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK 258
Cdd:cd05602    76 SFQTTDKLYFVLDYING------GELFYHLQRERCfleprarfyAAEIASALGYLHSL---NIVYRDLKPENILLDSQGH 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 259 AKIADFNLSNQspDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05602   147 IVLTDFGLCKE--NIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPP 207
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
228-319 1.53e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 46.91  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 228 RGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRVlGTFGYHAPEYAMTGQLTQKSDVYS 307
Cdd:PHA03212  193 RAIQYLHEN---RIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINANKYYGWA-GTIATNAPELLARDPYGPAVDIWS 268
                          90
                  ....*....|..
gi 1032291014 308 FGVVLLELLTGR 319
Cdd:PHA03212  269 AGIVLFEMATCH 280
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
230-321 1.90e-05

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


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 46.02  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 230 LEYLHEKvqpAVIHRDIRSSNVLLfeDFKAKIA--DFNLSNQspDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYS 307
Cdd:cd05585   107 LECLHKF---NVIYRDLKPENILL--DYTGHIAlcDFGLCKL--NMKDDDKTNTFCGTPEYLAPELLLGHGYTKAVDWWT 179
                          90
                  ....*....|....
gi 1032291014 308 FGVVLLELLTGRKP 321
Cdd:cd05585   180 LGVLLYEMLTGLPP 193
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
119-321 2.39e-05

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 45.77  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAA----------EPESNVefltqvsRVSKLKHDNFVELFgycvegnfrilaY 187
Cdd:cd05575     3 IGKGSFGKVLLARHKaEGKLYAVKVLQKKAilkrnevkhiMAERNV-------LLKNVKHPFLVGLH------------Y 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 188 EFATMGSLHDILHGRKGvqgaqpGPTLDWIQRVRI---------AVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFK 258
Cdd:cd05575    64 SFQTKDKLYFVLDYVNG------GELFFHLQRERHfpeprarfyAAEIASALGYLHSL---NIIYRDLKPENILLDSQGH 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 259 AKIADFNLSNQspDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05575   135 VVLTDFGLCKE--GIEPSDTTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPP 195
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
222-323 2.44e-05

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: 46.18  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 222 IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpdMAARLHSTRVLGTFGYHAPEYAMTGQLTQ 301
Cdd:cd05618   126 YSAEISLALNYLHER---GIIYRDLKLDNVLLDSEGHIKLTDYGMCKEG--LRPGDTTSTFCGTPNYIAPEILRGEDYGF 200
                          90       100
                  ....*....|....*....|..
gi 1032291014 302 KSDVYSFGVVLLELLTGRKPVD 323
Cdd:cd05618   201 SVDWWALGVLMFEMMAGRSPFD 222
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
118-321 2.66e-05

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: 45.41  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYgrayyATLKD------GKAVAVKKLDNA--AEPESNVEflTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd14184     8 VIGDGNF-----AVVKEcverstGKEFALKIIDKAkcCGKEHLIE--NEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGrkgvqgaqpgpTLDWIQRVRIAV--DAARGLEYLHekvQPAVIHRDIRSSNVLLFE----DFKAKIAD 263
Cdd:cd14184    81 VKGGDLFDAITS-----------STKYTERDASAMvyNLASALKYLH---GLCIVHRDIKPENLLVCEypdgTKSLKLGD 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 264 FNLSN--QSPdmaarLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14184   147 FGLATvvEGP-----LYT--VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPP 199
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
121-321 2.70e-05

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 45.33  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 121 EGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEFLTQVsrvsklKHDNFVELFGYCVEGNFRILAYEFATMGSLHDIL 199
Cdd:cd14196    26 EKSTGLEYAAKfIKKRQSRASRRGVSREEIEREVSILRQV------LHPNIITLHDVYENRTDVVLILELVSGGELFDFL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 200 HGRKGVQGAQpgpTLDWIQRVriavdaARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF----KAKIADFNLSNQSPDmaa 275
Cdd:cd14196   100 AQKESLSEEE---ATSFIKQI------LDGVNYLHTK---KIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIED--- 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1032291014 276 RLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14196   165 GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP 210
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
229-321 2.93e-05

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 45.31  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHekvQPAVIHRDIRSSNVLLFEDF---KAKIADFNLSNqspdMAARLHSTR-VLGTFGYHAPEYAMTGQLTQKSD 304
Cdd:cd14197   123 GVSFLH---NNNVVHLDLKPQNILLTSESplgDIKIVDFGLSR----ILKNSEELReIMGTPEYVAPEILSYEPISTATD 195
                          90
                  ....*....|....*..
gi 1032291014 305 VYSFGVVLLELLTGRKP 321
Cdd:cd14197   196 MWSIGVLAYVMLTGISP 212
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
229-318 3.10e-05

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 45.79  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpdmAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd07876   135 GIKHLHSA---GIIHRDLKPSNIVVKSDCTLKILDFGLARTA---CTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSV 208
                          90
                  ....*....|
gi 1032291014 309 GVVLLELLTG 318
Cdd:cd07876   209 GCIMGELVKG 218
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
213-321 3.32e-05

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 45.67  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 213 TLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNL-------SNQSPDMAARLhstrvlgT 285
Cdd:cd05104   210 ALDTEDLLSFSYQVAKGMEFLASK---NCIHRDLAARNILLTHGRITKICDFGLardirndSNYVVKGNARL-------P 279
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1032291014 286 FGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT-GRKP 321
Cdd:cd05104   280 VKWMAPESIFECVYTFESDVWSYGILLWEIFSlGSSP 316
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
119-315 3.77e-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: 45.21  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLKD-GKAVAVKK----LDNAAEPESNvefLTQVSRVSKLKHDNF-VELFgyCVE-----GNFRI-LA 186
Cdd:cd07837     9 IGEGTYGKVYKARDKNtGKLVALKKtrleMEEEGVPSTA---LREVSLLQMLSQSIYiVRLL--DVEhveenGKPLLyLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLHDILHGRKGVQGAQPGPTLDwiqrvRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA-KIADFN 265
Cdd:cd07837    84 FEYLDTDLKKFIDSYGRGPHNPLPAKTIQ-----SFMYQLCKGVAHCHSH---GVMHRDLKPQNLLVDKQKGLlKIADLG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032291014 266 LSNQ-SPDMAARLHStrvLGTFGYHAPEYAMTG-QLTQKSDVYSFGVVLLEL 315
Cdd:cd07837   156 LGRAfTIPIKSYTHE---IVTLWYRAPEVLLGStHYSTPVDMWSVGCIFAEM 204
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
228-321 4.13e-05

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: 45.04  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 228 RGLEYLHEKVqPAVIHRDIRSSNVLLF-EDFKAKIADFNLSNQSPDMAARlhstRVLGTFGYHAPEyAMTGQLTQKSDVY 306
Cdd:cd14030   139 KGLQFLHTRT-PPIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRASFAK----SVIGTPEFMAPE-MYEEKYDESVDVY 212
                          90
                  ....*....|....*
gi 1032291014 307 SFGVVLLELLTGRKP 321
Cdd:cd14030   213 AFGMCMLEMATSEYP 227
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
118-321 4.60e-05

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 44.57  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYAT-LKDGKAVAVK--KLDNAAEPEsnvEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGS 194
Cdd:cd14192    11 VLGGGRFGQVHKCTeLSTGLTLAAKiiKVKGAKERE---EVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 195 LHDILHGRKgvqgaqpgPTLDWIQRVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDF--KAKIADFNLSNQ-SP 271
Cdd:cd14192    88 LFDRITDES--------YQLTELDAILFTRQICEGVHYLH---QHYILHLDLKPENILCVNSTgnQIKIIDFGLARRyKP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 272 DMAARLHstrvLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14192   157 REKLKVN----FGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSP 202
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
119-322 4.62e-05

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 44.57  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPESNVefLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHD 197
Cdd:cd14006     1 LGRGRFGVVKRCIEKaTGREFAAKFIPKRDKKKEAV--LREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 198 ILhgrkgvqgAQPGPTLDwiQRVRIAV-DAARGLEYLHEKvqpAVIHRDIRSSNVLLFE--DFKAKIADFNLSNQspdMA 274
Cdd:cd14006    79 RL--------AERGSLSE--EEVRTYMrQLLEGLQYLHNH---HILHLDLKPENILLADrpSPQIKIIDFGLARK---LN 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1032291014 275 ARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPV 322
Cdd:cd14006   143 PGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPF 190
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
103-321 5.05e-05

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 45.00  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 103 LDELKEKTDNFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAEpesnvefLTQVSRVSKLKHDNFVELFGYCVEgnF 182
Cdd:cd05624    64 VKEMQLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWE-------MLKRAETACFREERNVLVNGDCQW--I 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 183 RILAYEFATMGSLHDILHGRKGvqgaqpGPTLDWIQRV--RIAVDAARGleYLHEKV-------QPAVIHRDIRSSNVLL 253
Cdd:cd05624   135 TTLHYAFQDENYLYLVMDYYVG------GDLLTLLSKFedKLPEDMARF--YIGEMVlaihsihQLHYVHRDIKPDNVLL 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032291014 254 FEDFKAKIADFNlSNQSPDMAARLHSTRVLGTFGYHAPEY--AM---TGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05624   207 DMNGHIRLADFG-SCLKMNDDGTVQSSVAVGTPDYISPEIlqAMedgMGKYGPECDWWSLGVCMYEMLYGETP 278
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
229-323 5.45e-05

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: 44.72  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpdmaarLHSTRVLGTF----GYHAPEYAMTGQLTQKSD 304
Cdd:cd05588   108 ALNFLHEK---GIIYRDLKLDNVLLDSEGHIKLTDYGMCKEG------LRPGDTTSTFcgtpNYIAPEILRGEDYGFSVD 178
                          90
                  ....*....|....*....
gi 1032291014 305 VYSFGVVLLELLTGRKPVD 323
Cdd:cd05588   179 WWALGVLMFEMLAGRSPFD 197
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
111-327 5.64e-05

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 44.70  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDnaaepESNVEFLTQVSRVSKLKHDNFVELFGYCVEgnfriLAYEF 189
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKEtGNYYAMKILD-----KQKVVKLKQVEHTLNEKRILQAINFPFLVK-----LEYSF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRKGvqgaqpGPTLDWIQRVR---------IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAK 260
Cdd:cd14209    71 KDNSNLYMVMEYVPG------GEMFSHLRRIGrfsepharfYAAQIVLAFEYLHSL---DLIYRDLKPENLLIDQQGYIK 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 261 IADFNLSNQspdmaARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP 327
Cdd:cd14209   142 VTDFGFAKR-----VKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQP 203
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
242-353 5.96e-05

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


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 45.04  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 242 IHRDIRSSNVLLFEDFKAKIADFNL--------------------------SNQSPD---------------MAARLH-- 278
Cdd:cd05625   123 IHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgdhlrqdsmdfSNEWGDpencrcgdrlkplerRAARQHqr 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 279 --STRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMP-RGQQSLVTWAT-----------PRLSED 344
Cdd:cd05625   203 clAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPlETQMKVINWQTslhippqaklsPEASDL 282

                  ....*....
gi 1032291014 345 KVKQCVDPK 353
Cdd:cd05625   283 IIKLCRGPE 291
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
119-316 6.04e-05

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: 44.85  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATL-KDGKAVAVKKLDNAAePEsNVEF-------LTQVSR------------------VSKLKHDN--- 169
Cdd:cd13977     8 VGRGSYGVVYEAVVrRTGARVAVKKIRCNA-PE-NVELalrefwaLSSIQRqhpnviqleecvlqrdglAQRMSHGSsks 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 170 --FVELFGYCVEGNfRILAY----------EFATMGSLHDILHGRKgvqgaqPGPTLD--WIQRVRIAvdaargLEYLHE 235
Cdd:cd13977    86 dlYLLLVETSLKGE-RCFDPrsacylwfvmEFCDGGDMNEYLLSRR------PDRQTNtsFMLQLSSA------LAFLHR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 236 KvqpAVIHRDIRSSNVLLFEDFKA---KIADFNLSN------QSPDMAARLHSTRV---LGTFGYHAPEyAMTGQLTQKS 303
Cdd:cd13977   153 N---QIVHRDLKPDNILISHKRGEpilKVADFGLSKvcsgsgLNPEEPANVNKHFLssaCGSDFYMAPE-VWEGHYTAKA 228
                         250
                  ....*....|...
gi 1032291014 304 DVYSFGVVLLELL 316
Cdd:cd13977   229 DIFALGIIIWAMV 241
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
105-321 1.05e-04

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 44.23  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 105 ELKEKTDNFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAE--PESNVEFLTQVSRVSKLKHDNFV-ELFGYCVEGN 181
Cdd:cd05622    67 DLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEmiKRSDSAFFWEERDIMAFANSPWVvQLFYAFQDDR 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 182 FRILAYEFATMGSLHDILHGRKGVQgaqpgptlDWIQ----RVRIAVDAARGLEYlhekvqpavIHRDIRSSNVLLFEDF 257
Cdd:cd05622   147 YLYMVMEYMPGGDLVNLMSNYDVPE--------KWARfytaEVVLALDAIHSMGF---------IHRDVKPDNMLLDKSG 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 258 KAKIADFNlSNQSPDMAARLHSTRVLGTFGYHAPEYAMT----GQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05622   210 HLKLADFG-TCMKMNKEGMVRCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLVGDTP 276
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
105-321 1.32e-04

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 43.83  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 105 ELKEKTDNFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAE--PESNVEFLTQVSRVSKLKHDNFV-ELFGYCVEGN 181
Cdd:cd05621    46 ELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEmiKRSDSAFFWEERDIMAFANSPWVvQLFCAFQDDK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 182 FRILAYEFATMGSLHDILHGRKGVQgaqpgptlDWIQ----RVRIAVDAARGLeylhekvqpAVIHRDIRSSNVLLFEDF 257
Cdd:cd05621   126 YLYMVMEYMPGGDLVNLMSNYDVPE--------KWAKfytaEVVLALDAIHSM---------GLIHRDVKPDNMLLDKYG 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 258 KAKIADFNlSNQSPDMAARLHSTRVLGTFGYHAPEYAMT----GQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05621   189 HLKLADFG-TCMKMDETGMVHCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLFEMLVGDTP 255
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
117-321 1.42e-04

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 43.49  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVKKLDNAAEPESNVEfltqvsrVSKLK----HDNFVELfgycvegnfrilaYEFat 191
Cdd:cd14179    13 KPLGEGSFSICRKCLhKKTNQEYAVKIVSKRMEANTQRE-------IAALKlcegHPNIVKL-------------HEV-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 192 mgsLHDILHGRKGVQGAQPGPTLDWIQRVRI--AVDAARGLEYLHEKVQP----AVIHRDIRSSNvLLFED----FKAKI 261
Cdd:cd14179    71 ---YHDQLHTFLVMELLKGGELLERIKKKQHfsETEASHIMRKLVSAVSHmhdvGVVHRDLKPEN-LLFTDesdnSEIKI 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 262 ADFNLSNQSPDMAARLHSTRVlgTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14179   147 IDFGFARLKPPDNQPLKTPCF--TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVP 204
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
229-319 2.20e-04

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 42.79  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLsnqspdmaARLHSTRVLG-----TFGYHAPEYAMTGQLTQKS 303
Cdd:cd07850   114 GIKHLHSA---GIIHRDLKPSNIVVKSDCTLKILDFGL--------ARTAGTSFMMtpyvvTRYYRAPEVILGMGYKENV 182
                          90
                  ....*....|....*.
gi 1032291014 304 DVYSFGVVLLELLTGR 319
Cdd:cd07850   183 DIWSVGCIMGEMIRGT 198
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
62-317 2.29e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 43.14  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  62 NEHLRSPKHHNDFGHHTRKPQAAVKPDAL-----KEPPSIDVPALSLDELKEKTDNFGSK-SLIG---EGSYGRAYYATL 132
Cdd:PHA03210   90 GELLVPRSNADLFASAGDGPSGAEDSDAShldfdEAPPDAAGPVPLAQAKLKHDDEFLAHfRVIDdlpAGAFGKIFICAL 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 133 KD--GKAVAVKKLDNAAEPESNVE-----FLTQVSRVS-----------KLKHDNFV---ELFGYcvEGNFRILA--YEF 189
Cdd:PHA03210  170 RAstEEAEARRGVNSTNQGKPKCErliakRVKAGSRAAiqleneilalgRLNHENILkieEILRS--EANTYMITqkYDF 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDilhgrkGVQGAQPGPTLdWIQRvRIAVDAARGLEYLHEKVqpaVIHRDIRSSNVLLFEDFKAKIADFNlsnq 269
Cdd:PHA03210  248 DLYSFMYD------EAFDWKDRPLL-KQTR-AIMKQLLCAVEYIHDKK---LIHRDIKLENIFLNCDGKIVLGDFG---- 312
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032291014 270 spdMAARLHSTRV------LGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLT 317
Cdd:PHA03210  313 ---TAMPFEKEREafdygwVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLS 363
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
118-318 2.40e-04

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 42.81  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 118 LIGEGSYGRAYYA-TLKDGKAVAVKKLDN-------AAEpesNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd14224    72 VIGKGSFGQVVKAyDHKTHQHVALKMVRNekrfhrqAAE---EIRILEHLKKQDKDNTMNVIHMLESFTFRNHICMTFEL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMgSLHDILHgRKGVQGAQpgptldwIQRVR-IAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA--KIADFNL 266
Cdd:cd14224   149 LSM-NLYELIK-KNKFQGFS-------LQLVRkFAHSILQCLDALHRN---KIIHCDLKPENILLKQQGRSgiKVIDFGS 216
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014 267 S---NQspdmaaRLHsTRVLGTFgYHAPEYAMTGQLTQKSDVYSFGVVLLELLTG 318
Cdd:cd14224   217 ScyeHQ------RIY-TYIQSRF-YRAPEVILGARYGMPIDMWSFGCILAELLTG 263
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
117-318 2.70e-04

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 42.55  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYGRAYYAT-LKDGKAVAVK------KLDNAAEPESNVefltqvsrVSKLKHDNFVELFgYCV--------EGN 181
Cdd:cd14134    18 RLLGEGTFGKVLECWdRKRKRYVAVKiirnveKYREAAKIEIDV--------LETLAEKDPNGKS-HCVqlrdwfdyRGH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 182 FRILayeFATMG-SLHDIL--HGRKGVqgaqpgpTLDWIQRvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLlFEDFK 258
Cdd:cd14134    89 MCIV---FELLGpSLYDFLkkNNYGPF-------PLEHVQH--IAKQLLEAVAFLHDL---KLTHTDLKPENIL-LVDSD 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 259 AKIADFNLSNQ------SPDMaaRL------------HSTrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTG 318
Cdd:cd14134   153 YVKVYNPKKKRqirvpkSTDI--KLidfgsatfddeyHSS-IVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTG 227
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
229-324 2.99e-04

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 42.77  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpdmAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd07874   131 GIKHLHSA---GIIHRDLKPSNIVVKSDCTLKILDFGLARTA---GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSV 204
                          90       100
                  ....*....|....*....|..
gi 1032291014 309 GVVLLE------LLTGRKPVDH 324
Cdd:cd07874   205 GCIMGEmvrhkiLFPGRDYIDQ 226
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
111-328 3.08e-04

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 42.72  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNF--VELFgYCVEGNFRI-LA 186
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDtGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLwvVKMF-YSFQDKLNLyLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 187 YEFATMGSLHDILHGRKGVQGAQpgpTLDWIQRVRIAVDAARGLEYlhekvqpavIHRDIRSSNVLLFEDFKAKIADF-- 264
Cdd:cd05628    80 MEFLPGGDMMTLLMKKDTLTEEE---TQFYIAETVLAIDSIHQLGF---------IHRDIKPDNLLLDSKGHVKLSDFgl 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 265 --------------NLSNQSPD--MAARLHSTR---------------VLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLL 313
Cdd:cd05628   148 ctglkkahrtefyrNLNHSLPSdfTFQNMNSKRkaetwkrnrrqlafsTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMY 227
                         250
                  ....*....|....*
gi 1032291014 314 ELLTGRKPVDHTMPR 328
Cdd:cd05628   228 EMLIGYPPFCSETPQ 242
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
229-319 3.22e-04

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 42.72  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSpdmAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd07875   138 GIKHLHSA---GIIHRDLKPSNIVVKSDCTLKILDFGLARTA---GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSV 211
                          90
                  ....*....|.
gi 1032291014 309 GVVLLELLTGR 319
Cdd:cd07875   212 GCIMGEMIKGG 222
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
229-321 3.44e-04

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 42.11  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLLFEDfKAKIADFNLSNQspdMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSF 308
Cdd:cd14109   111 ALKHMHDL---GIAHLDLRPEDILLQDD-KLKLADFGQSRR---LLRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSV 183
                          90
                  ....*....|...
gi 1032291014 309 GVVLLELLTGRKP 321
Cdd:cd14109   184 GVLTYVLLGGISP 196
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
110-321 4.20e-04

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


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 41.91  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 110 TDNFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEF 189
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 190 ATMGSLHDILHGRKgvqgaqpgptLDWIQR--VRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDF--KAKIADFN 265
Cdd:cd14191    81 VSGGELFERIIDED----------FELTERecIKYMRQISEGVEYIHKQ---GIVHLDLKPENIMCVNKTgtKIKLIDFG 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1032291014 266 LSNQSPDMAarlhSTRVL-GTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14191   148 LARRLENAG----SLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSP 200
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
232-321 4.46e-04

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 41.91  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 232 YLHEKVQpAV--------IHRDIRSSNVLLFEDFKAKIADF-NLSNQSPDMAARlhSTRVLGTFGYHAPEY--AMTGQLT 300
Cdd:cd05601   107 YLAELVL-AIhslhsmgyVHRDIKPENILIDRTGHIKLADFgSAAKLSSDKTVT--SKMPVGTPDYIAPEVltSMNGGSK 183
                          90       100
                  ....*....|....*....|....*
gi 1032291014 301 Q----KSDVYSFGVVLLELLTGRKP 321
Cdd:cd05601   184 GtygvECDWWSLGIVAYEMLYGKTP 208
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
216-321 4.69e-04

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 41.98  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 216 WIQRVRIAVDAARGLEYlhekvqpavIHRDIRSSNVLLFEDFKAKIADFNLSNQSpDMAARLHSTRVLGTFGYHAPEYAM 295
Cdd:cd05596   130 YTAEVVLALDAIHSMGF---------VHRDVKPDNMLLDASGHLKLADFGTCMKM-DKDGLVRSDTAVGTPDYISPEVLK 199
                          90       100       110
                  ....*....|....*....|....*....|
gi 1032291014 296 T----GQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05596   200 SqggdGVYGRECDWWSVGVFLYEMLVGDTP 229
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
222-321 4.74e-04

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 41.95  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 222 IAVDAARGLEYlhekvqpavIHRDIRSSNVLLFEDFKAKIADFNlSNQSPDMAARLHSTRVLGTFGYHAPEY--AM---T 296
Cdd:cd05597   113 LAIDSIHQLGY---------VHRDIKPDNVLLDRNGHIRLADFG-SCLKLREDGTVQSSVAVGTPDYISPEIlqAMedgK 182
                          90       100
                  ....*....|....*....|....*
gi 1032291014 297 GQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05597   183 GRYGPECDWWSLGVCMYEMLYGETP 207
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
111-321 5.22e-04

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 41.50  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 111 DNFGS-KSLIGEgsYGRAYYATLK------DGKAVAVKKLDNAAEPESNVEFltQVSRVSKLKHDNFVELFGYCVEGNFR 183
Cdd:cd14113     3 DNFDSfYSEVAE--LGRGRFSVVKkcdqrgTKRAVATKFVNKKLMKRDQVTH--ELGVLQSLQHPQLVGLLDTFETPTSY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 184 ILAYEFATMGSLHDILhgrkgvqgAQPGPTLDwiQRVRIAV-DAARGLEYLHekvQPAVIHRDIRSSNVLLFEDFKA--- 259
Cdd:cd14113    79 ILVLEMADQGRLLDYV--------VRWGNLTE--EKIRFYLrEILEALQYLH---NCRIAHLDLKPENILVDQSLSKpti 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032291014 260 KIADFNlsnqspdMAARLHST----RVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14113   146 KLADFG-------DAVQLNTTyyihQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSP 204
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
221-339 5.94e-04

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 41.38  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 221 RIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRVlgtfgYHAPEYAMTGQLT 300
Cdd:cd05576   117 RWAAEMVVALDALHRE---GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIENM-----YCAPEVGGISEET 188
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1032291014 301 QKSDVYSFGVVLLELLTGrKPVDHTMPRGQQSLVTWATP 339
Cdd:cd05576   189 EACDWWSLGALLFELLTG-KALVECHPAGINTHTTLNIP 226
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
164-315 6.69e-04

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 40.98  E-value: 6.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 164 KLKHDNFVELFGYCV---EGNFR-ILAYEFATMGSLHDILhgRKGVQGAQPGPTLDWIQRVRIAVDAargLEYLHeKVQP 239
Cdd:cd13984    51 QLDHPNIVKFHRYWTdvqEEKARvIFITEYMSSGSLKQFL--KKTKKNHKTMNEKSWKRWCTQILSA---LSYLH-SCDP 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 240 AVIHRDIRSSNVLLFEDFKAKIADFnlsnqSPDMAArlHSTRVL----GTFGYHAPEYAMTGQLTQKSDVYSFGVVLLEL 315
Cdd:cd13984   125 PIIHGNLTCDTIFIQHNGLIKIGSV-----APDAIH--NHVKTCreehRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEM 197
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
135-328 6.92e-04

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 41.06  E-value: 6.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 135 GKAVAVKKLdnAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGVQGAQpgpTL 214
Cdd:cd14110    28 GQMLAAKII--PYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAERNSYSEAE---VT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 215 DWIQRVRIAVDaargleYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF-NLSNQSPDMAArlhstrVLGTFGYH---- 289
Cdd:cd14110   103 DYLWQILSAVD------YLHSR---RILHLDLRSENMIITEKNLLKIVDLgNAQPFNQGKVL------MTDKKGDYvetm 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1032291014 290 APEYaMTGQ-LTQKSDVYSFGVVLLELLTGRKPVDHTMPR 328
Cdd:cd14110   168 APEL-LEGQgAGPQTDIWAIGVTAFIMLSADYPVSSDLNW 206
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
216-321 8.59e-04

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 41.15  E-value: 8.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 216 WIQRVRIAVDAARGLEYlhekvqpavIHRDIRSSNVLLFEDFKAKIADFNlSNQSPDMAARLHSTRVLGTFGYHAPEY-- 293
Cdd:cd05623   178 YLAEMVLAIDSVHQLHY---------VHRDIKPDNILMDMNGHIRLADFG-SCLKLMEDGTVQSSVAVGTPDYISPEIlq 247
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1032291014 294 AM---TGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd05623   248 AMedgKGKYGPECDWWSLGVCMYEMLYGETP 278
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
119-321 8.73e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 41.65  E-value: 8.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  119 IGEGSYGRAYYATLKDG------KAVAVKKLDnaaEPESNvEFLTQVSRVSKLKHDNFVELFG-YCVEGNFRI-LAYEFA 190
Cdd:PTZ00266    21 IGNGRFGEVFLVKHKRTqeffcwKAISYRGLK---EREKS-QLVIEVNVMRELKHKNIVRYIDrFLNKANQKLyILMEFC 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014  191 TMGSL-HDILHGRKGVQGAQPGPTLDwiqrvrIAVDAARGLEYLHE-KVQP---AVIHRDIRSSNVLLFEDFK------- 258
Cdd:PTZ00266    97 DAGDLsRNIQKCYKMFGKIEEHAIVD------ITRQLLHALAYCHNlKDGPngeRVLHRDLKPQNIFLSTGIRhigkita 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032291014  259 ----------AKIADFNLSnQSPDMAARLHStrVLGTFGYHAPEYAM--TGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:PTZ00266   171 qannlngrpiAKIGDFGLS-KNIGIESMAHS--CVGTPYYWSPELLLheTKSYDDKSDMWALGCIIYELCSGKTP 242
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
135-333 9.66e-04

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 41.08  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 135 GKAVAVKKLDNAAEPESNVEFLTQVSRVSKL-KHDNFVELFGYCVEGNFRILAYEFATMGSLHDIL--HGRKGvqgaqpg 211
Cdd:cd08227    25 GEYVTVRRINLEACTNEMVTFLQGELHVSKLfNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFMDG------- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 212 ptLDWIQRVRIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKAKIADF--NLSNQSPDMAARL------HSTRVL 283
Cdd:cd08227    98 --MSELAIAYILQGVLKALDYIHHM---GYVHRSVKASHILISVDGKVYLSGLrsNLSMINHGQRLRVvhdfpkYSVKVL 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032291014 284 GTFGYHAPEYAMTGqLTQKSDVYSFGVVLLELLTGRKPVdHTMPRGQQSL 333
Cdd:cd08227   173 PWLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPF-KDMPATQMLL 220
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
231-321 9.80e-04

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 40.75  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 231 EYLHEKvqpAVIHRDIRSSNvLLF----EDFKAKIADFNLSNQSPDMaARLHsTRVLgTFGYHAPEYAMTGQLTQ----K 302
Cdd:cd14092   113 SFMHSK---GVVHRDLKPEN-LLFtdedDDAEIKIVDFGFARLKPEN-QPLK-TPCF-TLPYAAPEVLKQALSTQgydeS 185
                          90
                  ....*....|....*....
gi 1032291014 303 SDVYSFGVVLLELLTGRKP 321
Cdd:cd14092   186 CDLWSLGVILYTMLSGQVP 204
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
110-321 9.96e-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: 40.75  E-value: 9.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 110 TDNFGSKSLIGEGSYGRAYYATLKD-GKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYE 188
Cdd:cd14183     5 SERYKVGRTIGDGNFAVVKECVERStGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 189 FATMGSLHD-ILHGRKGVQGAQPGptldwiqrvrIAVDAARGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA----KIAD 263
Cdd:cd14183    85 LVKGGDLFDaITSTNKYTERDASG----------MLYNLASAIKYLHSL---NIVHRDIKPENLLVYEHQDGskslKLGD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032291014 264 FNLSNQspdMAARLHStrVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKP 321
Cdd:cd14183   152 FGLATV---VDGPLYT--VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPP 204
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
158-321 1.27e-03

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 40.16  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 158 QVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGVQGAQPGPTLDWIqrvriavdaARGLEYLHEKv 237
Cdd:cd14105    58 EVSILRQVLHPNIITLHDVFENKTDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQI---------LDGVNYLHTK- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 238 qpAVIHRDIRSSNVLLFE----DFKAKIADFNLSNQSPDMAarlHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLL 313
Cdd:cd14105   128 --NIAHFDLKPENIMLLDknvpIPRIKLIDFGLAHKIEDGN---EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITY 202

                  ....*...
gi 1032291014 314 ELLTGRKP 321
Cdd:cd14105   203 ILLSGASP 210
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
119-319 1.44e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 40.19  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 119 IGEGSYGRAYYATLK-DGKAVAVKKLDNAAEPES-NVEFLTQVSRVSKLKHDNFVELfgycvegnfrilayefatmgslH 196
Cdd:PLN00009   10 IGEGTYGVVYKARDRvTNETIALKKIRLEQEDEGvPSTAIREISLLKEMQHGNIVRL----------------------Q 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 197 DILHGRKGVQGAQPGPTLDWIQRVRIAVDAA--------------RGLEYLHEKvqpAVIHRDIRSSNVLLFEDFKA-KI 261
Cdd:PLN00009   68 DVVHSEKRLYLVFEYLDLDLKKHMDSSPDFAknprliktylyqilRGIAYCHSH---RVLHRDLKPQNLLIDRRTNAlKL 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 262 ADFNLSnQSPDMAARLHSTRVLgTFGYHAPEYAM-TGQLTQKSDVYSFGVVLLELLTGR 319
Cdd:PLN00009  145 ADFGLA-RAFGIPVRTFTHEVV-TLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQK 201
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
117-318 1.67e-03

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 40.38  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 117 SLIGEGSYG---RAYyaTLKDGKAVAVKKLDNaaepesNVEFLTQVS---RVSKL--KHD-----NFVELFGYCVEGNFR 183
Cdd:cd14226    19 SLIGKGSFGqvvKAY--DHVEQEWVAIKIIKN------KKAFLNQAQievRLLELmnKHDtenkyYIVRLKRHFMFRNHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 184 ILAYEFATMgSLHDILHgRKGVQGAQPGPTLDWIQRVriavdaargLEYLHEKVQP--AVIHRDIRSSNVLLFEDFKA-- 259
Cdd:cd14226    91 CLVFELLSY-NLYDLLR-NTNFRGVSLNLTRKFAQQL---------CTALLFLSTPelSIIHCDLKPENILLCNPKRSai 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032291014 260 KIADFNLSNQSPDMAARLHSTRVlgtfgYHAPEYAMTGQLTQKSDVYSFGVVLLELLTG 318
Cdd:cd14226   160 KIIDFGSSCQLGQRIYQYIQSRF-----YRSPEVLLGLPYDLAIDMWSLGCILVEMHTG 213
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
178-340 3.39e-03

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 38.71  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 178 VEGNFRILAYEFATMGSLHDILHGRKGVQGAQPgptldwiqrVRIAVDAARGLEYLHekvQPAVIHRDIRSSNVLLFEDF 257
Cdd:cd14024    54 VIGQDRAYAFFSRHYGDMHSHVRRRRRLSEDEA---------RGLFTQMARAVAHCH---QHGVILRDLKLRRFVFTDEL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 258 KAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLT--QKSDVYSFGVVLLELLTGRKPVDHTMP-------- 327
Cdd:cd14024   122 RTKLVLVNLEDSCPLNGDDDSLTDKHGCPAYVGPEILSSRRSYsgKAADVWSLGVCLYTMLLGRYPFQDTEPaalfakir 201
                         170
                  ....*....|...
gi 1032291014 328 RGQQSLVTWATPR 340
Cdd:cd14024   202 RGAFSLPAWLSPG 214
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
229-321 4.66e-03

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 38.68  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHEKvqpAVIHRDIRSSNVLlFEDFKAKI--ADFNLSNqspdmaaRLHSTRVL-GTFGYHAPEyAMTGQLTQKS-D 304
Cdd:PHA03390  121 ALNDLHKH---NIIHNDIKLENVL-YDRAKDRIylCDYGLCK-------IIGTPSCYdGTLDYFSPE-KIKGHNYDVSfD 188
                          90
                  ....*....|....*..
gi 1032291014 305 VYSFGVVLLELLTGRKP 321
Cdd:PHA03390  189 WWAVGVLTYELLTGKHP 205
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
229-321 5.85e-03

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 38.34  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032291014 229 GLEYLHekvQPAVIHRDIRSSNVLLFE--DFKAKIADF-NLSNQSPDMAARLHstrvLGTFGYHAPEYAMTGQLTQKSDV 305
Cdd:cd14108   109 GIEYLH---QNDVLHLDLKPENLLMADqkTDQVRICDFgNAQELTPNEPQYCK----YGTPEFVAPEIVNQSPVSKVTDI 181
                          90
                  ....*....|....*.
gi 1032291014 306 YSFGVVLLELLTGRKP 321
Cdd:cd14108   182 WPVGVIAYLCLTGISP 197
 
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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