{PDOC51413}
{PS51413; DBINO}
{BEGIN}
************************
* DBINO domain profile *
************************

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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2008 / First entry.

[ 1] Bakshi R., Prakash T., Dash D., Brahmachari V.
     "In silico characterization of the INO80 subfamily of SWI2/SNF2
     chromatin remodeling proteins."
     Biochem. Biophys. Res. Commun. 320:197-204(2004).
     PubMed=15207721; DOI=10.1016/j.bbrc.2004.05.147
[ 2] Bakshi R., Mehta A.K., Sharma R., Maiti S., Pasha S., Brahmachari V.
     "Characterization of a human SWI2/SNF2 like protein hINO80:
     demonstration of catalytic and DNA binding activity."
     Biochem. Biophys. Res. Commun. 339:313-320(2006).
     PubMed=16298340; DOI=10.1016/j.bbrc.2005.10.206

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}