Figure 4.

(A) Relative location of BAZ1B domains. Yellow circles are low complexity regions. Blue cylinders are coiled coil regions. The first N-terminally located domain is present in Acf1-related proteins in a variety of organisms. The WAC (WSTF/Acf1/cbp146) domain is within the DNA binding region of the Acf1 and is believed to be involved in DNA binding and is associated with the PHD finger and Brd domains in other proteins [18,19]. It spans residues 21–120 on BAZ1B. DDT stands for DNA-binding homobox-containing proteins and Different Transcription and chromatin remodeling factors. Such proteins share this domain, which spans almost 60 residues and is associated exclusively with nuclear domains including PHD finger, Brd, and DNA-binding homeodomain [20]. It spans residues 604–668 on BAZ1B. Residues 724–773 on BAZ1B locate WHIM1 conserved the α helical motif that along with the WHIM2, WHIM3, and DDT domain comprise an α helical module that is reported to interact with linker DNA and the SLIDE domain of ISWI proteins [21]. WHIM2 domain spans residues 899 to 936 on BAZ1B and contains the D-TOX E motif that is also known as the Williams–Beuren Syndrome DDT (WSD) motif. It is conserved from yeast to animals [22]. PHD zinc finger (spanning 1184 to 1234) and bromodomain (1356–1426) are the two C-terminally located domains. Refer to the main text for more information about these domains. (B) A 3D representation of BAZ1B based on its PDB file (PDB ID: Q9UIG0) predicted by the AlphaFold protein structure database [23]. Domains are highlighted with different colors as follows: BrD: yellow; PHD: magenta; WHIM1: cyan; WHIM2: green; WHIM3: orange; DDT: purple; WAC: red.