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):

In Saccharomyces cerevisiae, Brr6 and Brl1 are interacting proteins that localise to the nuclear envelope and regulate lipid homeostasis [ (PUBMED:26432634) ]. Mutation studies have implicated the proteins in nuclear pore complex biogenesis and mRNA nuclear export [ (PUBMED:11483521) ], although it may be that these observed effects are due to defects in maintaining the biophysical properties of the nuclear envelope [ (PUBMED:26432634) ].

This entry represents a highly conserved domain found in the C terminus of Brl1 and in Brr6. It is likely that this domain plays an important role in their interaction. Mutation studies have shown the domain to be essential for Brl1 function [ (PUBMED:15882446) ].

Interestingly, many fungi, including Saccharomyces cerevisiae, contain both Brr6 and Brl1 genes. However, S. pombe,Pneumocystis carinii, and other fungi distantly related to S. cerevisiae have a unique gene that is more closely related to Brl1 than to Brr6 [ (PUBMED:26432634) ]. The S. pombe homologue has been shown to be involved in SPB biogenesis [ (PUBMED:22042620) ].

GO process:lipid homeostasis (GO:0055088)
GO component:nuclear membrane (GO:0031965)
Family alignment:
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There are 510 Brr6_like_C_C domains in 510 proteins in SMART's nrdb database.

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