The domain within your query sequence starts at position 505 and ends at position 569; the E-value for the BET domain shown below is 9.2e-34.



PFAM accession number:PF17035
Interpro abstract (IPR027353):

The bromodomain and extraterminal (BET) proteins are a class of transcriptional regulators whose members can be found in animals, plants and fungi. BET proteins are involved in diverse cellular phenomena such as meiosis, cell-cycle control, and homeosis and have been suggested to modulate chromatin structure and affect transcription via a sequence-independent mechanism. BET proteins are defined as having one (plants) or two (animals/yeast) bromodomains and an Extra Terminal (ET) domain. The ET domain consists of three separate regions, only one of which, the N-terminal ET (NET) domain is conserved in all BET proteins. The function of the NET domain is assumed to be protein binding [ (PUBMED:7816623) (PUBMED:11487468) (PUBMED:12969431) (PUBMED:18815416) ].

The structure of the NET domain comprises three alpha-helices and a characteristic loop region of an irregular but well-defined structure. The NET structure has an acidic patch that forms a continuous ridge with a hydrophobic cleft. which may interact with other proteins and/or DNA [ (PUBMED:18815416) ].

Some proteins known to contain a NET domain include:

  • Human RING3 (now designated Brd2)
  • Murine MCAP (now designated Brd4)
  • Drosophila Fsh
  • Yeast Bdf1 and Bdf2
  • Arabidopsis imbibition-inducible (IMB1), whichplays a role in abscisic acid (ABA) and phytochrome A (phyA) mediated responses of seed germination.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry BET