NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17534999|ref|NP_496952|]
View 

Protein kinase domain-containing protein [Caenorhabditis elegans]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 132-291 9.20e-11

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 cd14017:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 263  Bit Score: 61.50  E-value: 9.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534999 132 MSLYfrgGPTLEQCFAMRN--KFTLGTAGRLAEDVLNVIRCAHKHGYLVRNMDLNSF---HYDAASRHLFMAD--ISSLV 204
Cdd:cd14017  75 MTLL---GPNLAELRRSQPrgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFaigRGPSDERTVYILDfgLARQY 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534999 205 KNISGDDGAP---IASYAGCLDYAP--CSDDGLVGARQDLETWFYQLVHLVLGELPWGSL-SREEAGVKKAEFQKSKEFA 278
Cdd:cd14017 152 TNKDGEVERPprnAAGFRGTVRYASvnAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLkDKEEVGKMKEKIDHEELLK 231

                       170
                ....*....|...
gi 17534999 279 ELPEVFHKIAEVV 291
Cdd:cd14017 232 GLPKEFFQILKHI 244
 
Name Accession Description Interval E-value
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
 132-291 9.20e-11

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 61.50  E-value: 9.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534999 132 MSLYfrgGPTLEQCFAMRN--KFTLGTAGRLAEDVLNVIRCAHKHGYLVRNMDLNSF---HYDAASRHLFMAD--ISSLV 204
Cdd:cd14017  75 MTLL---GPNLAELRRSQPrgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFaigRGPSDERTVYILDfgLARQY 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534999 205 KNISGDDGAP---IASYAGCLDYAP--CSDDGLVGARQDLETWFYQLVHLVLGELPWGSL-SREEAGVKKAEFQKSKEFA 278
Cdd:cd14017 152 TNKDGEVERPprnAAGFRGTVRYASvnAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLkDKEEVGKMKEKIDHEELLK 231

                       170
                ....*....|...
gi 17534999 279 ELPEVFHKIAEVV 291
Cdd:cd14017 232 GLPKEFFQILKHI 244
 
Name Accession Description Interval E-value
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
 132-291 9.20e-11

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 61.50  E-value: 9.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534999 132 MSLYfrgGPTLEQCFAMRN--KFTLGTAGRLAEDVLNVIRCAHKHGYLVRNMDLNSF---HYDAASRHLFMAD--ISSLV 204
Cdd:cd14017  75 MTLL---GPNLAELRRSQPrgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFaigRGPSDERTVYILDfgLARQY 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534999 205 KNISGDDGAP---IASYAGCLDYAP--CSDDGLVGARQDLETWFYQLVHLVLGELPWGSL-SREEAGVKKAEFQKSKEFA 278
Cdd:cd14017 152 TNKDGEVERPprnAAGFRGTVRYASvnAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLkDKEEVGKMKEKIDHEELLK 231

                       170
                ....*....|...
gi 17534999 279 ELPEVFHKIAEVV 291
Cdd:cd14017 232 GLPKEFFQILKHI 244
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
 149-284 8.39e-10

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


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 58.91  E-value: 8.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534999 149 RNKFTLGTAGRLAEDVLNVIRCAHKHGYLVRNMDLNSF---HYDAASRHLFMAD--ISSLVKNISGDDGAP--IASYAGC 221
Cdd:cd14129  91 RGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgRFPSTCRKCYMLDfgLARQFTNSCGDVRPPraVAGFRGT 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534999 222 LDYAPCS--DDGLVGARQDLETWFYQLVHLVLGELPWGSLS-REEAGVKKAEFQKSKEFAELPEVF 284
Cdd:cd14129 171 VRYASINahRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKdKEQVGSIKERYEHRLMLKHLPPEF 236
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
 149-285 9.73e-10

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


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 58.50  E-value: 9.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534999 149 RNKFTLGTAGRLAEDVLNVIRCAHKHGYLVRNMDLNSF---HYDAASRHLFMAD--ISSLVKNISGDDGAP--IASYAGC 221
Cdd:cd14130  91 RGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgRLPSTYRKCYMLDfgLARQYTNTTGEVRPPrnVAGFRGT 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17534999 222 LDYAPCS--DDGLVGARQDLETWFYQLVHLVLGELPWGSLS-REEAGVKKAEFQKSKEFAELPEVFH 285
Cdd:cd14130 171 VRYASVNahKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKdKEQVGMIKEKYEHRMLLKHMPSEFH 237
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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