PROSITE documentation PDOC51136
WAC domain profile


ACF (for ATP-utilizing chromatin assembly and remodeling factor) is a chromatin-remodeling complex that catalyzes the ATP-dependent assembly of periodic nucleosome arrays. This reaction utilizes the energy of ATP hydrolysis by ISWI, the smaller of the two subunits of ACF. Acf1, the large subunit of ACF, is essential for the full activity of the complex. The WAC (WSTF/Acf1/cbp146) domain is an ~110-residue module present at the N-termini of Acf1-related proteins in a variety of organisms. It is found in association with other domains such as the bromodomain (see <PDOC00550>), the PHD-type zinc finger (see <PDOC50016>), DDT (see <PDOC50827>) or WAKS. The DNA-binding region of Acf1 includes the WAC domain, which is necessary for the efficient binding of ACF complex to DNA. It seems probable that the WAC domain will be involved in DNA binding in other related factors [1,2].

Some proteins known to contain a WAC domain are listed below:

  • Drosophila melanogaster ATP-dependent chromatin assembly factor large subunit Acf1.
  • Human WSTF (Williams syndrome transcription factor).
  • Mouse cbp146.
  • Yeast imitation switch two complex protein 1 (ITC1 or YGL133w).
  • Yeast protein YPL216w.

The profile we developed covers the entire WAC domain.

Last update:

June 2005 / First entry.


Technical section

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

WAC, PS51136; WAC domain profile  (MATRIX)


1AuthorsIto T. Levenstein M.E. Fyodorov D.V. Kutach A.K. Kobayashi R. Kadonaga J.T.
TitleACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly.
SourceGenes Dev. 13:1529-1539(1999).
PubMed ID10385622

2AuthorsFyodorov D.V. Kadonaga J.T.
TitleBinding of Acf1 to DNA involves a WAC motif and is important for ACF-mediated chromatin assembly.
SourceMol. Cell. Biol. 22:6344-6353(2002).
PubMed ID12192034

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 prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)