BRIGHT

BRIGHT, ARID (A/T-rich interaction domain) domain
BRIGHT
SMART accession number:SM00501
Description: DNA-binding domain containing a helix-turn-helix structure
Interpro abstract (IPR001606):

The AT-rich interaction domain (ARID) is an ~100-amino acid DNA-binding module found in a large number of eukaryotic transcription factors that regulate cell proliferation, differentiation and development [ (PUBMED:10545119) (PUBMED:11867548) ]. The ARID domain appears as a single-copy motif and can be found in association with other domains, such as JmjC, JmjN, Tudor and PHD-type zinc finger [ (PUBMED:11959810) ].

The basic structure of the ARID domain domain appears to be a series of six alpha-helices separated by beta-strands, loops, or turns, but the structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence homology, they can be partitioned into three structural classes:

  • Minimal ARID proteins that consist of a core domain formed by six alpha- helices;
  • ARID proteins that supplement the core domain with an N-terminal alpha- helix;
  • Extended-ARID proteins, which contain the core domain and additional alpha- helices at their N- and C-termini.

Minimal ARIDs are distributed in all eukaryotes, while extended ARIDs are restricted to metazoans. The ARID domain binds DNA as a monomer, recognizing the duplex through insertion of a loop and an alpha-helix into the major groove, and by extensive non-specific anchoring contacts to the adjacent sugar-phosphate backbone [ (PUBMED:10545119) (PUBMED:11867548) (PUBMED:14722072) ].

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

  • Eukaryotic transcription factors of the jumonji family.
  • Mammalian Bright, a B-cell-specific trans-activator of IgH transcription.
  • Mammalian PLU-1, a protein that is upregulated in breast cancer cells.
  • Mammalian RBP1 and RBP2, retinoblastoma binding factors.
  • Mammalian Mrf-1 and Mrf-2, transcriptional modulators of the cytomegalovirus major intermediate-early promoter.
  • Drosophila melanogaster Dead ringer protein, a transcriptional regulatory protein required for early embryonic development.
  • Yeast SWI1 protein, from the SWI/SNF complex involved in chromatin remodeling and broad aspects of transcription regulation.
  • Drosophila melanogaster Osa. It is structurally related to SWI1 and associates with the brahma complex, which is the Drosophila equivalent of the SWI/SNF complex.
GO function:DNA binding (GO:0003677)
Family alignment:
View or

There are 8834 BRIGHT domains in 8827 proteins in SMART's nrdb database.

Click on the following links for more information.