| Primary Identifier | IPR001606 | Type | Domain |
| Short Name | ARID_dom |
| description | 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 cellproliferation, differentiation and development [, ]. The ARID domain appearsas a single-copy motif and can be found in association with other domains,such as JmjC, JmjN, Tudor and PHD-type zinc finger [].The basic structure of the ARID domain domain appears to be a series of sixα-helices separated by β-strands, loops, or turns, but the structuredregion may extend to an additional helix at either or both ends of the basicsix. Based on primary sequence homology, they can be partitioned into threestructural 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 arerestricted to metazoans. The ARID domain binds DNA as a monomer, recognizingthe duplex through insertion of a loop and an α-helix into the majorgroove, and by extensive non-specific anchoring contacts to the adjacentsugar-phosphate backbone [, , ].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 thecytomegalovirus major intermediate-early promoter.Drosophila melanogaster Dead ringer protein, a transcriptional regulatoryprotein required for early embryonic development.Yeast SWI1 protein, from the SWI/SNF complex involved in chromatinremodeling and broad aspects of transcription regulation.Drosophila melanogaster Osa. It is structurally related to SWI1 andassociates with the brahma complex, which is the Drosophila equivalent ofthe SWI/SNF complex. |
