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 (PubMed:17099699, PubMed:28801535). 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 (PubMed:14759371, PubMed:17099699, PubMed:28801535). The ACF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the ACF-5 ISWI chromatin remodeling complex (PubMed:28801535). 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 (PubMed:17099699). Involved in DNA replication and together with SMARCA5/SNF2H is required for replication of pericentric heterochromatin in S-phase (PubMed:12434153). May have a role in nuclear receptor-mediated transcription repression (PubMed:17519354). 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 (PubMed:28801535). Within the ACF-1 ISWI chromatin remodeling complex interacts with SMARCA1; the interaction is direct (PubMed:28801535). 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 (PubMed:10880450, PubMed:12198550, PubMed:28801535). Within the ACF-5 ISWI chromatin remodeling complex interacts with SMARCA5/SNF2H; the interaction is direct (PubMed:10880450, PubMed:12198550, PubMed:28801535). 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 (PubMed:10880450, PubMed:12434153, PubMed:14759371). 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 (PubMed:10880450, PubMed:12434153, PubMed:14759371). Within the complex interacts with SMARCA5/SNF2H; the interaction is direct and promotes the interaction with the POLE3-CHRAC1 heterodimer (PubMed:10880450, PubMed:12434153, PubMed:14759371). Interacts with NCOR1 (via its RD1 domain); the interaction corepresses a number of NCOR1-regulated genes (PubMed:17519354). May target the CHRAC complex to heterochromatin. Highly expressed in testis and at low or undetectable levels in other tissues analyzed. Stimulated by double-stranded DNA and nucleosomal DNA. Belongs to the WAL family.