Brix domain (IPR007109)

Short name: Brix

Domain relationships



The Brix domain is found in a number of eukaryotic proteins including some from Saccharomyces cerevisiae and Homo sapiens, Arabidopsis thaliana Peter Pan-like protein and several hypothetical proteins.

There are six (one archaean and five eukaryotic) protein families which have a similar domain architecture with a central globular Brix domain. They have an optional N- and obligatory C-terminal segments, which both have charged low-complexity regions [PMID: 11406393].

Proteins from the Imp4/Brix superfamily appear to be involved in ribosomal RNA processing, which essential for the functioning of all cells. The N- and C-terminal halves of a member of the superfamily, Mil, show significant structural similarity to one another. This suggests an origin by means of an ancestral duplication. Both halves have the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. Structural evidence suggests that the Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their beta-sheet and a central alpha-helix [PMID: 15654320].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles