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PROSITE documentation PDOC51413 [for PROSITE entry PS51413]

DBINO domain profile





Description

Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodelling complexes that are implicated in epigenetic control of gene expression. Members of the SNF2 family of proteins have been identified in organisms ranging from Escherichia coli to Homo sapiens. All of them contain the conserved SNF2 domain, which is defined by the existence of seven motifs (I, Ia, and II-VI) with sequences similarity to those motifs found in DNA and RNA helicases (see <PDOC51192>). SNF2-like family members can be further subdivided into several subfamilies according to the presence of protein motifs outside of the ATPase region. The DBINO (DNA binding domain of INO80) domain is characteristic of the INO80 subfamily and is predicted to have DNA-binding function. The DBINO domain is a 126 amino acid long peptide located near the N-terminus, approximately 100 residues upstream of the SNF2 helicase domain. The presence of this domain in all the INO80 subfamily proteins from yeast to humans suggests its conserved function in evolution [1,2].

The most significant feature of DBINO domain is the occurence of the positive amino acids arginine and lysine in tandem (RK/KR), in multiple positions, which are likely to bind DNA [1].

The profile we developed covers the entire DBINO domain.

Last update:

December 2008 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

DBINO, PS51413; DBINO domain profile  (MATRIX)


References

1AuthorsBakshi R. Prakash T. Dash D. Brahmachari V.
TitleIn silico characterization of the INO80 subfamily of SWI2/SNF2 chromatin remodeling proteins.
SourceBiochem. Biophys. Res. Commun. 320:197-204(2004).
PubMed ID15207721
DOI10.1016/j.bbrc.2004.05.147

2AuthorsBakshi R. Mehta A.K. Sharma R. Maiti S. Pasha S. Brahmachari V.
TitleCharacterization of a human SWI2/SNF2 like protein hINO80: demonstration of catalytic and DNA binding activity.
SourceBiochem. Biophys. Res. Commun. 339:313-320(2006).
PubMed ID16298340
DOI10.1016/j.bbrc.2005.10.206



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