Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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Brix

SMART accession number:	SM00879
Description:	The Brix domain is found in a number of eukaryotic proteins including SSF proteins from yeast and humans, Arabidopsis thaliana Peter Pan-like protein and several hypothetical proteins.
Interpro abstract (IPR007109):	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 [(PUBMED: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 [(PUBMED:15654320)].
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 1002 Brix domains in 1002 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a Brix domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Brix domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Cellular role (predicted cellular role)

• Cellular role: translation
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Fatica A, Cronshaw AD, Dlakic M, Tollervey D
  • Ssf1p prevents premature processing of an early pre-60S ribosomalparticle.
  • Mol Cell. 2002; 9: 341-51
  • Display abstract

  • Ssf1p and Ssf2p are two nearly identical and functionally redundantnucleolar proteins. In the absence of Ssf1p and Ssf2p, the 27SA(2)pre-rRNA was prematurely cleaved, inhibiting synthesis of the 27SB and 7Spre-rRNAs and the 5.8S and 25S rRNA components of the large ribosomalsubunit. On sucrose gradients, Ssf1p sedimented with pre-60S ribosomalparticles. The 27SA(2), 27SA(3), and 27SB pre-rRNAs were copurified withtagged Ssf1p, as were 23 large subunit ribosomal proteins and 21 otherproteins implicated in ribosome biogenesis. These included four Brixfamily proteins, Ssf1p, Rpf1p, Rpf2p, and Brx1p, indicating that theentire family functions in ribosome synthesis. This complex is distinctfrom recently reported pre-60S complexes in RNA and protein composition.We describe a multistep pathway of 60S preribosome maturation.

  • Wehner KA, Baserga SJ
  • The sigma(70)-like motif: a eukaryotic RNA binding domain unique to asuperfamily of proteins required for ribosome biogenesis.
  • Mol Cell. 2002; 9: 329-39
  • Display abstract

  • Little is understood about the role of nucleolar RNA binding proteins inribosome biogenesis, although there is a clear need for them based on thestrict folding requirements of the pre-rRNA. We have identified asuperfamily of RNA binding proteins whose members are required fordifferent stages of ribosome biogenesis. The Imp4 superfamily is composedof five individual families (Imp4, Rpf1, Rpf2, Brx1, and Ssf) that allpossess the sigma(70)-like motif, a eukaryotic RNA binding domain withprokaryotic origins. The Imp4 superfamily members associate with RNAs thatare consistent with their distinct roles in ribosome biogenesis andsuggest the mechanisms by which they function.

  • Eisenhaber F, Wechselberger C, Kreil G
  • The Brix domain protein family -- a key to the ribosomal biogenesispathway?
  • Trends Biochem Sci. 2001; 26: 345-7
  • Display abstract

  • Six (one archaean and five eukaryotic) protein families have similardomain architecture that includes a central globular Brix domain, andoptional N- and obligatory C-terminal segments, both with chargedlow-complexity regions. Biological data for some proteins in thissuperfamily suggest a role in ribosome biogenesis and rRNA binding.

  • Holmgren P, Lindquist O
  • Lethal intoxications with centrally stimulating amines in Sweden1966-1973.
  • Z Rechtsmed. 1975; 75: 265-73
  • Display abstract

  • Fatal intoxications with centrally stimulating amines (CSA) have becomeincreasingly common in Sweden. Toxicological data and pathologicalfindings of 32 cases of amphetamine and phenmetrazine intoxications whichoccurred from 1966-1973 in Sweden are described. Furthermore, 13 caseswhere these drugs were not the cause of death, but found in urine andorgans, are reported.

• Structure (3D structures containing this domain)

• 3D Structures of Brix domains in PDB

  PDB code	Main view	Title
  1w94		Crystal structure of mil (mth680), an archaeal imp4-like protein
  2cxh		Crystal structure of probable ribosomal biogenesis protein from aeropyrum pernix k1

• Links (links to other resources describing this domain)

• PFAM	Brix
  INTERPRO	IPR007109

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