Fig. 1. KIS-L is related to chromatin-remodeling factors. The two major KIS isoforms (KIS-S and KIS-L) are compared with other Drosophila ATPases involved in chromatin remodeling, including BRM, Mi-2, CHD1 and ISWI. The ATPase domain of KIS-L is most closely related to that of BRM (44% identical) and CHD family members (50% identical). The C-terminal segment common to KIS-S and KIS-L (shaded light gray) contains a BRK domain, but lacks the bromodomain (BD) found in BRM and other SWI2/SNF2 family members. The N-terminal extension unique to KIS-L contains an ATPase domain and two chromodomains (CD), but lacks the PHD fingers (PHD) and putative DNA-binding domains found in other CHD proteins. KIS-L also lacks a SANT domain, a nucleosome-recognition module found in ISWI and other proteins. A and B indicate regions of KIS proteins against which antibodies were raised (residues 100-300 and 3902-4200, respectively).