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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQKISGQN-GTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNG 79
Cdd:cd14123   106 MVMDRLGTDLQKILIDNgGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYRNPNEVYLADYGLSYRYCPNG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  80 NHKQYQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEQNLKDPVAVQTAKTNLLDELPQSVLK 159
Cdd:cd14123   186 NHKEYKENPRKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWEQNLKNPVAVQEAKAKLLSNLPDSVLK 265

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217330771 160 WAPSGSSCCEIAQFLVCAHSLAYDEKPNYQALKKILN 196
Cdd:cd14123   266 WSTGGSSSMEIAQFLSRVKDLAYDEKPDYQALKKILS 302

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQKISGQN-GTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNG 79
Cdd:cd14123   106 MVMDRLGTDLQKILIDNgGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYRNPNEVYLADYGLSYRYCPNG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  80 NHKQYQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEQNLKDPVAVQTAKTNLLDELPQSVLK 159
Cdd:cd14123   186 NHKEYKENPRKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWEQNLKNPVAVQEAKAKLLSNLPDSVLK 265

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217330771 160 WAPSGSSCCEIAQFLVCAHSLAYDEKPNYQALKKILN 196
Cdd:cd14123   266 WSTGGSSSMEIAQFLSRVKDLAYDEKPDYQALKKILS 302

Serine/threonine protein kinase [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERL-GIDLQKISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNpdQVYLADYGLSYRYcpnG 79
Cdd:COG0515    84 LVMEYVeGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG--RVKLIDFGIARAL---G 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  80 NHKQYQENPRKghnGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEqnLKDPVAVQTAktnLLDELPQSVLK 159
Cdd:COG0515   159 GATLTQTGTVV---GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFD--GDSPAELLRA---HLREPPPPPSE 230

                  ...
gi 2217330771 160 WAP 162
Cdd:COG0515   231 LRP 233

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.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2217330771  36 LEYIHENEYVHGDIKAANLLLGykNPDQVYLADYGLS 72
Cdd:pfam07714 115 MEYLESKNFVHRDLAARNCLVS--ENLVVKISDFGLS 149

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330771   1 MVMERL-GIDL-QKISGQNGTFKKSTVLQLGIrmldvleyIHENEYVHGDIKAANLLLgykNPDQVYLADYGLSYR 74
Cdd:TIGR03724  74 IVMEYIeGKPLkDVIEENGDELAREIGRLVGK--------LHKAGIVHGDLTTSNIIV---RDDKVYLIDFGLGKY 138

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQKISGQN-GTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNG 79
Cdd:cd14123   106 MVMDRLGTDLQKILIDNgGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYRNPNEVYLADYGLSYRYCPNG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  80 NHKQYQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEQNLKDPVAVQTAKTNLLDELPQSVLK 159
Cdd:cd14123   186 NHKEYKENPRKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWEQNLKNPVAVQEAKAKLLSNLPDSVLK 265

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217330771 160 WAPSGSSCCEIAQFLVCAHSLAYDEKPNYQALKKILN 196
Cdd:cd14123   266 WSTGGSSSMEIAQFLSRVKDLAYDEKPDYQALKKILS 302

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQKISGQNGT-FKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNG 79
Cdd:cd14122   104 MIMDRFGSDLQKIYEANAKrFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLLSYKNPDQVYLVDYGLAYRYCPEG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  80 NHKQYQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEQNLKDPVAVQTAKTNLLDELPQSVLK 159
Cdd:cd14122   184 VHKEYKEDPKRCHDGTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLPWEDNLKDPNYVRDSKIRYRDNISELMEK 263

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217330771 160 WAPSGSSCCEIAQFLVCAHSLAYDEKPNYQALKKIL 195
Cdd:cd14122   264 CFPGKNKPGEIRKYMETVKLLGYTEKPLYPHLREIL 299

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQKI-SGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY-KNPDQVYLADYGLSYRYC-- 76
Cdd:cd14016    73 MVMDLLGPSLEDLfNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLgKNSNKVYLIDFGLAKKYRdp 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  77 PNGNHKQYQENprKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWeQNLKdpVAVQTAKTNLLDELPQS 156
Cdd:cd14016   153 RTGKHIPYREG--KSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPW-QGLK--AQSKKEKYEKIGEKKMN 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217330771 157 VlkwaPSGSSCC----EIAQFLVCAHSLAYDEKPNYQALKKIL 195
Cdd:cd14016   228 T----SPEELCKglpkEFAKYLEYVRSLKFEEEPDYDYLRQLF 266

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQ--KISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNPD--QVYLADYGLSYRYC 76
Cdd:cd14017    73 IVMTLLGPNLAelRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDerTVYILDFGLARQYT 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  77 -PNGNHKQyqeNPRK--GHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWeQNLKDPVAVQTAK-----TN 148
Cdd:cd14017   153 nKDGEVER---PPRNaaGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPW-RKLKDKEEVGKMKekidhEE 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2217330771 149 LLDELPQsvlkwapsgssccEIAQFLVCAHSLAYDEKPNYQALKKILN 196
Cdd:cd14017   229 LLKGLPK-------------EFFQILKHIRSLSYFDTPDYKKLHSLLE 263

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQKI-SGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY-KNPDQVYLADYGLS--YRYC 76
Cdd:cd14128    73 LVMDLLGPSLEDLfNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIgRHCNKLFLIDFGLAkkYRDS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  77 PNGNHKQYQENprKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWeQNLKdpVAVQTAKTNLLDE---- 152
Cdd:cd14128   153 RTRQHIPYRED--KNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPW-QGLK--AATKKQKYEKISEkkms 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217330771 153 LPQSVL-KWAPSgssccEIAQFLVCAHSLAYDEKPNYQALKKI 194
Cdd:cd14128   228 TPVEVLcKGFPA-----EFAMYLNYCRGLRFEEAPDYMYLRQL 265

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQKISGQ-NGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLG---YKNPDQVYLADYGLSYRY- 75
Cdd:cd14126    73 MVLELLGPSLEDLFDLcDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGrqsTKKQHVIHIIDFGLAKEYi 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  76 -CPNGNHKQYQEnpRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWeqnlkdpvavQTAKTNLLDELP 154
Cdd:cd14126   153 dPETNKHIPYRE--HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW----------QGLKADTLKERY 220

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217330771 155 QSV--LKWAPSGSSCC-----EIAQFLVCAHSLAYDEKPNYQALKKI 194
Cdd:cd14126   221 QKIgdTKRATPIEVLCenfpeEMATYLRYVRRLDFFETPDYDYLRKL 267

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERLGIDLQKI--SGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGyKNPD---QVYLADYGLSYRY 75
Cdd:cd14129    73 VVMQLQGRNLADLrrSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMG-RFPStcrKCYMLDFGLARQF 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  76 CpngNHKQYQENPR--KGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEQnLKDPVAVQTAKTNLLDEL 153
Cdd:cd14129   152 T---NSCGDVRPPRavAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK-IKDKEQVGSIKERYEHRL 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217330771 154 pqsVLKWAPSgssccEIAQFLVCAHSLAYDEKPNYQALKKILN 196
Cdd:cd14129   228 ---MLKHLPP-----EFSVFLDHISGLDYFTKPDYQLLVSVFD 262

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   1 MVMERL-GIDLQKISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKnpDQVYLADYGLSYrycPNG 79
Cdd:cd14014    77 IVMEYVeGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTED--GRVKLTDFGIAR---ALG 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217330771  80 NHKQYQENPRKghnGTIEFTSLDAHKGVALSRRSDVEILGyCMLRWLC-GKLPWE 133
Cdd:cd14014   152 DSGLTQTGSVL---GTPAYMAPEQARGGPVDPRSDIYSLG-VVLYELLtGRPPFD 202

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  10 LQKISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGykNPDQVYLADYGLSYRYcpNGNHKQYQENPR 89
Cdd:cd06606    86 LASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVD--SDGVVKLADFGCAKRL--AEIATGEGTKSL 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330771  90 KghnGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEqNLKDPVAV--QTAKTNLLDELPQ 155
Cdd:cd06606   162 R---GTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWS-ELGNPVAAlfKIGSSGEPPPIPE 225

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  32 MLDVLEYIHENEYVHGDIKAANLLLGYKNpdQVYLADYGLSyRYCPNGNHKQyqenprKGHNGTIEFTS---LDAHKGVA 108
Cdd:cd14008   117 LVLGLEYLHENGIVHRDIKPENLLLTADG--TVKISDFGVS-EMFEDGNDTL------QKTAGTPAFLApelCDGDSKTY 187

                          90       100
                  ....*....|....*....|....*...
gi 2217330771 109 LSRRSDVEILG---YCMlrwLCGKLPWE 133
Cdd:cd14008   188 SGKAADIWALGvtlYCL---VFGRLPFN 212

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330771   1 MVMERLGIDLQKISGQNGT-FKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNPdQVYLADYGLSYRY 75
Cdd:cd05118    78 LVFELMGMNLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELG-QLKLADFGLARSF 152

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217330771   1 MVMERLGIDLQK-ISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNpdQVYLADYGLS 72
Cdd:cd07829    75 LVFEYCDQDLKKyLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDG--VLKLADFGLA 145

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  22 KSTVLQLGIrmldVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRycpngnhkqyQENPRKGHNGTIEFTS- 100
Cdd:cd13987    94 KRCAAQLAS----ALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRR----------VGSTVKRVSGTIPYTAp 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217330771 101 --LDA--HKGVALSRRSDV---EILGYCMLRwlcGKLPWE 133
Cdd:cd13987   160 evCEAkkNEGFVVDPSIDVwafGVLLFCCLT---GNFPWE 196

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330771  22 KSTVLQLgirmLDVLEYIHENEYVHGDIKAANLLLgyKNPDQVYLADYGLSYRYCPNGN 80
Cdd:cd07840   107 KCYMKQL----LEGLQYLHSNGILHRDIKGSNILI--NNDGVLKLADFGLARPYTKENN 159

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330771   1 MVMERLGIDLQK-ISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLgykNPD-QVYLADYGLSYRY 75
Cdd:cd07841    79 LVFEFMETDLEKvIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLI---ASDgVLKLADFGLARSF 152

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771   2 VMERLGidlqKISGQNGTFKKSTVLQLGIRM---LDV---LEYIHENEYVHGDIKAANLLLGYKnpDQVYLADYGLSYR- 74
Cdd:cd13979    80 IMEYCG----NGTLQQLIYEGSEPLPLAHRIlisLDIaraLRFCHSHGIVHLDVKPANILISEQ--GVCKLCDFGCSVKl 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330771  75 YCPNGnhkqyQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWE 133
Cdd:cd13979   154 GEGNE-----VGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYA 207

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  32 MLDVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNGN-HKQYqenprkghnGTIEFTSLDAHKGVALS 110
Cdd:cd14006    98 LLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARKLNPGEElKEIF---------GTPEFVAPEIVNGEPVS 168

                          90
                  ....*....|....*.
gi 2217330771 111 RRSD---VEILGYCML 123
Cdd:cd14006   169 LATDmwsIGVLTYVLL 184

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330771  36 LEYIHENEYVHGDIKAANLLLGYKnpDQVYLADYGLSYRYCPNGnhkqyQENPRKGHNGTI-----EFTSLDAHKGvals 110
Cdd:cd14069   113 LKYLHSCGITHRDIKPENLLLDEN--DNLKISDFGLATVFRYKG-----KERLLNKMCGTLpyvapELLAKKKYRA---- 181

                          90       100
                  ....*....|....*....|....
gi 2217330771 111 RRSDVEILGYCMLRWLCGKLPWEQ 134
Cdd:cd14069   182 EPVDVWSCGIVLFAMLAGELPWDQ 205

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330771   1 MVMERLGIDLQK-ISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLlgYKNPDQVYLADYGLSYRY 75
Cdd:cd07843    83 MVMEYVEHDLKSlMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLL--LNNRGILKICDFGLAREY 156

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330771   7 GIDLQKISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNP-DQVYLADYGLSyRYCPNGNH 81
Cdd:cd14106    92 GGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPlGDIKLCDFGIS-RVIGEGEE 166