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85  structures 1551  species 1  interaction 1667  sequences 8  architectures

Family: CutA1 (PF03091)

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

  1. 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

  2. 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].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 contains the following 9 members:

CutA1 DUF190 DUF2007 DUF3240 DUF3582 DUF970 HisG_C Nit_Regul_Hom P-II

Alignments

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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
(13)
Full
(1667)
Representative proteomes NCBI
(1191)
Meta
(568)
RP15
(154)
RP35
(313)
RP55
(430)
RP75
(550)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(13)
Full
(1667)
Representative proteomes NCBI
(1191)
Meta
(568)
RP15
(154)
RP35
(313)
RP55
(430)
RP75
(550)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(13)
Full
(1667)
Representative proteomes NCBI
(1191)
Meta
(568)
RP15
(154)
RP35
(313)
RP55
(430)
RP75
(550)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

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 View help on the curation process

Seed source: Pfam-B_2307 (release 6.4)
Previous IDs: none
Type: Family
Author: Mifsud W
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 information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.1 22.1
Trusted cut-off 22.2 22.1
Noise cut-off 21.9 21.9
Model length: 102
Family (HMM) version: 10
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

CutA1

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 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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