The retroviral oncogene v-myb, and its cellular counterpart c-myb, encode nuclear DNA-binding proteins. In myb, one of the most conserved regions consisting of three tandem repeats has been shown to be involved in DNA-binding. The SANT domain is present in nuclear receptor co-repressors and in the subunits of many chromatin-remodelling complexes. It has a strong structural similarity to the DNA-binding domain of Myb-related proteins. Both consist of tandem repeats of three alpha-helices that are arranged in a helix-turn-helix motif, each alpha helix containing a bulky aromatic residue. Despite the overall similarity there is differences that indicate that the SANT domain is functionally divergent from the canonical Myb DNA-binding domain.The myb/SANT domains can be classified into three groups: the myb-type HTH domain, which binds DNA, the SANT domain, which is a protein-protein interaction module, and the myb-like domain that can be involved in either of these functions. This entry represents a myb-like domain.