|SMART accession number:||SM01025|
|Description:||The BEN domain is 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. Computational analysis suggests that the BEN domain mediates protein-DNA and protein-protein interactions during chromatin organisation and transcription.|
|Interpro abstract (IPR018379):|
The BEN domain is found in diverse proteins including:
The BEN domain is predicted to function as an adaptor for the higher-order structuring of chromatin, and recruitment of chromatin modifying factors in transcriptional regulation. It has been suggested to mediate protein-DNA and protein-protein interactions during chromatin organisation and transcription. The presence of BEN domains in a poxviral early virosomal protein and in polydnaviral proteins also suggests a possible role in the organisation of viral DNA during replication or transcription. They are generally linked to other globular domains with functions related to transcriptional regulation and chromatin structure, such as BTB, C4DM, and C2H2 fingers [(PUBMED:18203771)].
This domain is predicted to form an all-alpha fold with four conserved helices. Its conservation pattern reveals several conserved residues, most of which have hydrophobic side-chains and are likely to stabilise the fold through helix-helix packing [(PUBMED:18203771)].
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- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
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