The domain within your query sequence starts at position 32 and ends at position 217; the E-value for the SBF domain shown below is 3.3e-47.

VVMLLLIMLSLGCTMEFSKIKAHFWKPKGVIIAIVAQYGIMPLSAFLLGKVFHLTSIEAL
AILICGCSPGGNLSNLFTLAMKGDMNLSIVMTTCSSFTALGMMPLLLYIYSKGIYDGDLK
DKVPYKGIMLSLVMVLIPCAIGIFLKSKRPHYVPYVLKAGMIITFSLSVAVTVLSVINVG
NSIMFV

SBF

SBF
PFAM accession number:PF01758
Interpro abstract (IPR002657):

This family of proteins are found both in prokaryotes and eukaryotes. They are related to the human bile acid:sodium symporters (TC 2.A.28), which are transmembrane proteins functioning in the liver in the uptake of bile acids from portal blood plasma, a process mediated by the co-transport of Na+ [(PUBMED:1961729)].

This entry also includes members of the ACR3 family of arsenite (As(III)) permeases, which confer resistance to arsenic by extrusion from cells [(PUBMED:19494117)]. They exist in prokaryotes and eukaryotes (lower plants and fungi) [(PUBMED:20530755), (PUBMED:24291645)]. The ACR3 permeases have ten-transmembrane span topology [(PUBMED:18088595)]. Corynebacterium glutamicum has three Acr3 proteins, CgAcr3-1, CgAcr3-2, and CgAcr3-3. CgAcr3-1 is thought to be an antiporter that catalyses arsenite-proton exchange [(PUBMED:22102279)].

The Shewanella oneidensis Acr3 is not able to transport As(III) and confers resistance only to arsenate (As(V)) [(PUBMED:19039703)], whereas the Acr3 orthologue from Synechocystis mediates tolerance to As(III), As(V) and antimonite (Sb(III)) [(PUBMED:12949088)].

In budding yeast, overexpression of the Acr3 gene confers an arsenite- but not an arsenate-resistance phenotype [(PUBMED:9234670)]. Saccharomyces cerevisiae Acr3 is a plasma membrane metalloid/H+ antiporter that transports arsenite and antimonite [(PUBMED:21447319)].

GO component:membrane (GO:0016020)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SBF