The domain within your query sequence starts at position 319 and ends at position 558; the E-value for the ArsB domain shown below is 2e-10.
GASVEAQVASAVAILAGVYTLIIFEIVHRTLAAMLGALAALAALAVVGDRPSLTHVVEWI DFETLALLFGMMILVAVFSETGFFDYCAVKAYQLSRGRVWAMIFMLCLMAAILSAFLDNV TTMLLFTPVTIRLCEVLNLDPRQVLIAEVIFTNIGGAATAIGDPPNVIIVSNQELRKMGL DFAGFTAHMFLGICLVLLVSFPLLRLLYWNKKLYNKEPSEIVELKHEIHVWRLTAQRISP
ArsB |
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PFAM accession number: | PF02040 |
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Interpro abstract (IPR000802): | Arsenic is a toxic metalloid whose trivalent and pentavalent ions inhibit a variety of biochemical processes. Operons that encode arsenic resistance have been found in multicopy plasmids from both Gram-positive and Gram-negative bacteria [ (PUBMED:7721697) ]. The resistance mechanism is encoded from a single operon, which houses an anion pump. The pump has two polypeptide components: a catalytic subunit (the ArsA protein), which functions as an oxyanion-stimulated ATPase; and an arsenite export component (the ArsB protein), which is associated with the inner membrane [ (PUBMED:1688427) ]. The ArsA and ArsB proteins are thought to form a membrane complex that functions as an anion-translocating ATPase. The ArsB protein is distinguished by its overall hydrophobic character, in keeping with its role as a membrane-associated channel. Sequence analysis reveals the presence of 13 putative transmembrane (TM) regions. |
GO process: | arsenite transport (GO:0015700) |
GO component: | integral component of membrane (GO:0016021) |
GO function: | arsenite transmembrane transporter activity (GO:0015105) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ArsB