The myb/SANT-like domain in Adf-1 (MADF) is a ~80-amino-acid module that directs sequence specific DNA binding to a site consisting of multiple trinucleotide repeats. The MADF domain is found in one or more copies in eukaryotic and viral proteins and is often associated with the BESS domain (see <PDOC51031>) [1,2,3].

It is likely that the MADF domain is more closely related to the myb/SANT domain than it is to other HTH domains [1,2,3].

Some proteins known to contain a MADF domain are listed below:

• Drosophila Adf-1, a transcription factor first identified on the basis of its interaction with the alcohol dehydrogenase promoter but that binds the promoters of a diverse group of genes [1].
• Drosophila Dorsal-interacting protein 3 (Dip3). It functions both as an activator to bind DNA in a sequence specific manner and a coactivator to stimulate synergistic activation by Dorsal and Twist [2].
• Drosophila Stonewall (Stwl), a putative transcription factor required for maintenance of female germline stem cells as well as oocyte differentiation.

The profile we developed covers the entire MADF domain.