PROSITE documentation PDOC51038

BAH domain profile

The Bromo-adjacent homology (BAH) domain is a domain first identified in the vertebrate polybromo protein, a protein present in the large nuclear complex Swi/Snf [1,2]. It corresponds to a region of about 110 amino-acids, which can contain insertions of variable length. This domain has been identified in a number of proteins present in large complex involved in chromatin replication, epigenetic mechanisms (DNA methylation), transcriptional repression or activation [1]. The BAH domain appears to act as a protein-protein interaction module specialized in gene silencing, as suggested by its interaction within yeast Orc1p with the silent information regulator Sir1p [1]. It can be found in a duplicated form in PB1 as well as in animal DNA MTases, or unique in CMT1 for example.

The BAH domain is frequently found in association with other domains implicated in epigenetic mechanisms such as bromodomain (see <PDOC00550>), SET (see <PDOC50280>), PHD finger (see <PDOC50016>), and/or in DNA binding such as HMG boxes (see <PDOC00305>), AT hooks, GATA (see <PDOC00300>), and myb-like domains (see <PDOC00037>).

The crystal structure of the BAH domain has been solved (see <PDB:1M4Z>)[3], It revealed that it consists of an elongated shape that can be divided in a large subdomain comprised of mainly anti-parallel β-strands (β-1 to β-10) and a small helical subdomain.

The profile we developed covers the BAH structure from β-4 to β-10.