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Conserved domains on  [gi|17537195|ref|NP_496965|]
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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

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List of domain hits

Name Accession Description Interval E-value
PK_Tyr_Ser-Thr super family cl47985
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
189-338 7.05e-03

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.


The actual alignment was detected with superfamily member pfam07714:

Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 37.86  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537195   189 IELEQKLGGGIAGDAFNCTWKGLER-----VA-KIIPLHPSHRNKKAFQEVAALnrLGDVAHqtPNLVKFeMAAVVTGMP 262
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGEntkikVAvKTLKEGADEEEREDFLEEASI--MKKLDH--PNIVKL-LGVCTQGEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537195   263 qdvknqlrenwrtnHMLVVILSRGG------RpvasQPPDSLTAQQSIGIMKQFVMTM--LIgetSLKLYHNDAHCRNVL 334
Cdd:pfam07714  76 --------------LYIVTEYMPGGdlldflR----KHKRKLTLKDLLSMALQIAKGMeyLE---SKNFVHRDLAARNCL 134

                  ....
gi 17537195   335 LTDT 338
Cdd:pfam07714 135 VSEN 138
 
Name Accession Description Interval E-value
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
189-338 7.05e-03

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: 37.86  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537195   189 IELEQKLGGGIAGDAFNCTWKGLER-----VA-KIIPLHPSHRNKKAFQEVAALnrLGDVAHqtPNLVKFeMAAVVTGMP 262
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGEntkikVAvKTLKEGADEEEREDFLEEASI--MKKLDH--PNIVKL-LGVCTQGEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537195   263 qdvknqlrenwrtnHMLVVILSRGG------RpvasQPPDSLTAQQSIGIMKQFVMTM--LIgetSLKLYHNDAHCRNVL 334
Cdd:pfam07714  76 --------------LYIVTEYMPGGdlldflR----KHKRKLTLKDLLSMALQIAKGMeyLE---SKNFVHRDLAARNCL 134

                  ....
gi 17537195   335 LTDT 338
Cdd:pfam07714 135 VSEN 138
 
Name Accession Description Interval E-value
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
189-338 7.05e-03

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: 37.86  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537195   189 IELEQKLGGGIAGDAFNCTWKGLER-----VA-KIIPLHPSHRNKKAFQEVAALnrLGDVAHqtPNLVKFeMAAVVTGMP 262
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGEntkikVAvKTLKEGADEEEREDFLEEASI--MKKLDH--PNIVKL-LGVCTQGEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537195   263 qdvknqlrenwrtnHMLVVILSRGG------RpvasQPPDSLTAQQSIGIMKQFVMTM--LIgetSLKLYHNDAHCRNVL 334
Cdd:pfam07714  76 --------------LYIVTEYMPGGdlldflR----KHKRKLTLKDLLSMALQIAKGMeyLE---SKNFVHRDLAARNCL 134

                  ....
gi 17537195   335 LTDT 338
Cdd:pfam07714 135 VSEN 138
 
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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