SMART: Brr6_like_C_C domain annotation

Brr6_like_C_C Di-sulfide bridge nucleocytoplasmic transport domain

SMART accession number:	SM01042
Description:	Brr6_like_C_C is the highly conserved C-terminal region of a group of proteins found in fungi. It carries four highly conserved cysteine residues. It is suggested that members of the family interact with each other via di-sulfide bridges to form a complex which is involved in nucleocytoplasmic transport (PUBMED:15882446) .
Interpro abstract (IPR018767):	This entry represents a highly conserved domain found in the C terminus of fungal protein Brl1, which is a nuclear envelope protein required for nuclear transport [(PUBMED:15882446)]. The domain is also found in the related fungal protein Brr6, which is an essential nuclear envelope integral membrane protein that is required for mRNA nuclear export [(PUBMED:11483521)]. Brr6 and Brl1 interact to form a complex, and it is likely that this domain plays an important role in their binding. Mutation studies have shown the domain to be essential for Brl1 function [(PUBMED:15882446)].
GO process:	mRNA export from nucleus (GO:0006406), protein export from nucleus (GO:0006611), nuclear envelope organization (GO:0006998)
GO component:	nuclear membrane (GO:0031965)
Family alignment:	View or

There are 76 Brr6_like_C_C domains in 76 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Brr6_like_C_C domain is also avaliable.

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Go to specific node: Saccharomyces cerevisiae
Cellular role (predicted cellular role)
Cellular role: transport
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Saitoh YH, Ogawa K, Nishimoto T
- Brl1p -- a novel nuclear envelope protein required for nuclear transport.
- Traffic. 2005; 6: 502-17
- Display abstract
- In this article, we identify a cold-sensitive mutant of Xpo1p designatedas xop1-2 (but will be referred to from here on as xpo1-ok) that issynthetically lethal with srm1-1, a Saccharomyces cerevisiae RCC1 homolog.xpo1-ok was a novel mutated allele with a single point mutation, T283P.Suppressors of xpo1-ok were isolated, and one of them was found to encodea novel nuclear envelope integral membrane protein designated as Brl1p(Brr6 like protein no. 1). Brl1p is homologous with Brr6p at theC-terminal domain, which is well conserved in the Brr6/Brl1 family. Tocharacterize the function of Brl1p, a series of temperature-sensitivemutants of Brl1p were isolated. All of brl1 mutations were localized tothe conserved C-terminal domain that is essential for a function of Brl1p.Some brl1 alleles showed defects in nuclear export of either mRNA orprotein, and nuclear pore clustering, similar to brr6-1. The cellularlocalization of Brl1p is also similar to that of Brr6p. The geneticanalysis suggested that Brl1p functionally interacts with Brr6p. Aninteraction of Brl1p with Brr6p was shown by the two-hybrid method. Wehypothesize that Brl1p functions for nuclear export as a complex withBrr6p.
Links (links to other resources describing this domain)
PFAM Brr6_like_C_C
INTERPRO IPR018767

PFAM	Brr6_like_C_C
INTERPRO	IPR018767