The domain within your query sequence starts at position 67 and ends at position 165; the E-value for the CutA1 domain shown below is 6.9e-44.

SAAFVTCPNEKVAKEIARAVVEKRLAACVNLIPQITSIYEWKGKIEEDSEVLMMIKTQSS
LVPALTEFVRSVHPYEVAEVIALPVEQGNPPYLHWVHQV

CutA1

CutA1
PFAM accession number:PF03091
Interpro abstract (IPR004323):

The CutA family of proteins which exhibit ion tolerance are found in a large variety of species [(PUBMED:12949080)]. In E.Coli, two operons on the cutA locus contain genes that encode three proteins, CutA1, CutA2 and CutA3. CutA1 proteins are found in the cytoplasm while CutA2 (50kDa) and CutA3 (24kDa) are located in the inner membrane. Although the role of E. Coli CutA1 is not clear, studies on E. coli cutA locus describe some mutations that lead to an increase in copper sensitivity, thus suggesting a role in ion tolerance [(PUBMED:9260936)].

To date, the structure of CutA proteins from several species have been solved [(PUBMED:15351719), (PUBMED:14705033)]. The crystal structures of the E.Coli and rat CutA1 proteins show both these proteins to be trimeric in the crystal as well as in solution[(PUBMED:12949080)].Trimerisation seems to supported by the formation of beta sheets between the subunit. This trimeric structure suggests the protein may be involved in signal transduction due to architectural similarities with PII signal transducer proteins [(PUBMED:12949080)]. Recent studies propose that mammalian CutA1 in the neuronal cell membrane acts as an anchor for acetylcholinesterase (AChE)1 [(PUBMED:10954708)].

GO process:response to metal ion (GO:0010038)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry CutA1