Regulatory subunit of the ATP-dependent ACF-1 and ACF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and slide edge- and center-positioned histone octamers away from their original location on the DNA template to facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (By similarity). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template in an ATP-dependent manner (By similarity). The ACF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the ACF-5 ISWI chromatin remodeling complex (By similarity). Has a role in sensing the length of DNA which flank nucleosomes, which modulates the nucleosome spacing activity of the ACF-5 ISWI chromatin remodeling complex (By similarity). Involved in DNA replication and together with SMARCA5/SNF2H is required for replication of pericentric heterochromatin in S-phase (By similarity). May have a role in nuclear receptor-mediated transcription repression (By similarity). Component of the ACF-1 ISWI chromatin remodeling complex at least composed of SMARCA1 and BAZ1A, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (By similarity). Within the ACF-1 ISWI chromatin remodeling complex interacts with SMARCA1; the interaction is direct (By similarity). Component of the ACF-5 ISWI chromatin remodeling complex (also called the ACF complex) at least composed of BAZ1A and SMARCA5/SNF2H, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (By similarity). Within the ACF-5 ISWI chromatin remodeling complex interacts with SMARCA5/SNF2H; the interaction is direct (By similarity). Component of the CHRAC ISWI chromatin remodeling complex at least composed of SMARCA5/SNF2H, BAZ1A/ACF1, CHRAC1 and POLE3; the complex preferentially binds DNA through the CHRAC1-POLE3 heterodimer and possesses ATP-dependent nucleosome-remodeling activity (By similarity). Within the complex interacts (via N-terminus) with POLE3-CHRAC1 heterodimer; the interaction is direct and is required for the complex to preferentially bind to DNA (By similarity). Within the complex interacts with SMARCA5/SNF2H; the interaction is direct and promotes the interaction with the POLE3-CHRAC1 heterodimer (By similarity). Interacts with NCOR1 (via its RD1 domain); the interaction corepresses a number of NCOR1-regulated genes (By similarity). Concentrated in pericentric to heterochromatin. Belongs to the WAL family. Extended N-terminus.