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.