Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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KIND kinase non-catalytic C-lobe domain

SMART accession number:	SM00750
Description:	It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features
Interpro abstract (IPR011019):	The KIND (kinase non-catalytic C-lobe domain) is a putative protein interaction domain, which has been identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). The presence of the KIND domain at the N terminus of signalling proteins and the absence of the active site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of the domain only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features [(PUBMED:12877999), (PUBMED:16099729)].
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 0 KIND domains in 0 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a KIND domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with KIND domain is also avaliable.

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• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Ciccarelli FD, Bork P, Kerkhoff E
  • The KIND module: a putative signalling domain evolved from the C lobe of the protein kinase fold.
  • Trends Biochem Sci. 2003; 28: 349-52
  • Display abstract

  • A novel putative interaction domain - KIND (kinase non-catalytic C-lobe domain) - has been identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of the novel domain only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features.

• Metabolism (metabolic pathways involving proteins which contain this domain)

• % proteins involved KEGG pathway ID Description 100.00 map04320 Dorso-ventral axis formation This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with KIND domain which could be assigned to a KEGG orthologous group, and not all proteins containing KIND domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Links (links to other resources describing this domain)

• INTERPRO	IPR011019

Send comments to Ivica Letunic