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 [1]. 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 [2]. This family also contains putative proteins from eukaryotes (human and Drosophila).
Literature references
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Fong ST, Camakaris J, Lee BT; , Mol Microbiol 1995;15:1127-1137.: Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. PUBMED:7623666 EPMC:7623666
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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
SCOP: | 1p1l |
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 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Biological process | response to metal ion (GO:0010038) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan GlnB-like (CL0089), which has the following description:
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 [1].
The clan contains the following 12 members:
CBD_PlyG CdAMP_rec CutA1 DUF190 DUF2007 DUF2179 DUF3240 HisG_C Nit_Regul_Hom NRho P-II Rhomboid_NAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (412) |
Full (3845) |
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RP15 (640) |
RP35 (1853) |
RP55 (3745) |
RP75 (6060) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (412) |
Full (3845) |
Representative proteomes | UniProt (16640) |
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RP15 (640) |
RP35 (1853) |
RP55 (3745) |
RP75 (6060) |
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Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_2307 (release 6.4) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Mifsud W |
Number in seed: | 412 |
Number in full: | 3845 |
Average length of the domain: | 95.5 aa |
Average identity of full alignment: | 34 % |
Average coverage of the sequence by the domain: | 74.4 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 99 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 145 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 sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.