Summary: CutA1 divalent ion tolerance protein
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CutA1 divalent ion tolerance protein Provide feedback
Several gene loci with a possible involvement in cellular tolerance to copper have been identified . One such locus in eubacteria and archaebacteria, cutA, is thought to be involved in cellular tolerance to a wide variety of divalent cations other than copper. The cutA locus consists of two operons, of one and two genes. The CutA1 protein is a cytoplasmic protein, encoded by the single-gene operon and has been linked to divalent cation tolerance. It has no recognised structural motifs . This family also contains putative proteins from eukaryotes (human and Drosophila).
Gupta SD, Wu HC, Rick PD; , J Bacteriol 1997;179:4977-4984.: A Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli. PUBMED:9260936 EPMC:9260936
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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].
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|Biological process||response to metal ion (GO:0010038)|
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The members of this clan are characterised by the fact the domains, each comprised of four beta-strand and two alpha helices, tend to form tetrameric structures .
The clan contains the following 9 members:CutA1 DUF190 DUF2007 DUF3240 DUF3582 DUF970 HisG_C Nit_Regul_Hom P-II
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Curation and family details
|Seed source:||Pfam-B_2307 (release 6.4)|
|Number in seed:||13|
|Number in full:||1667|
|Average length of the domain:||99.10 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||84.17 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CutA1 domain has been found. There are 85 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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