PROSITE documentation PDOC51457

BEN domain profile

The BEN domain is an α-helical module found in diverse animal proteins such as BANP/SMAR1, NAC1 and the Drosophila mod(mdg4) isoform C, in the chordopoxvirus virosomal protein E5R and in several proteins of polydnaviruses. The BEN domain is present in one or more copies in these proteins and has been named after experimentally characterized proteins BANP, E5R and NAC1 in which it is present. The BEN domain is predicted to functions as an adaptor for the higher-order structuring of chromatin, and recruitment of chromatin modifying factors in transcriptional regulation. It has been suggested that the BEN domain mediates protein-DNA and protein-protein interactions during chromatin organization and transcription. The presence of BEN domains in a poxviral early virosomal protein and in polydnaviral proteins also suggests a possible role for them in organization of viral DNA during replication or transcription. BEN domains are linked in polypetides to other globular domains with functions related to transcriptional regulation and chromatin structure, such as BTB (see <PDOC50097>), C4DM, C2H2 fingers, MCAF N-terminal domain (MCAFN) and a domain that is also found N-terminal to the SAM domain in sex comb on midleg-like 1 (SCML1), a protein of the vertebrate polycomb complex [1].

The BEN domain is predicted to have an all-α fold with four conserved helices. Its conservation pattern revealed several conserved residues, most of which have hydrophobic side-chains and are likely to stabilize the fold through helix-helix packing [1].

The profile we developed covers the entire BEN domain.