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145  structures 2886  species 0  interactions 3845  sequences 30  architectures

Family: CutA1 (PF03091)

Summary: CutA1 divalent ion tolerance protein

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The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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 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_N

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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

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)
Representative proteomes UniProt
(16640)
RP15
(640)
RP35
(1853)
RP55
(3745)
RP75
(6060)
Jalview View  View  View  View  View  View  View 
HTML View  View           
PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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

Format an alignment

  Seed
(412)
Full
(3845)
Representative proteomes UniProt
(16640)
RP15
(640)
RP35
(1853)
RP55
(3745)
RP75
(6060)
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
(412)
Full
(3845)
Representative proteomes UniProt
(16640)
RP15
(640)
RP35
(1853)
RP55
(3745)
RP75
(6060)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

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: 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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.4 22.4
Trusted cut-off 22.4 22.4
Noise cut-off 22.3 22.3
Model length: 99
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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.

Protein Predicted structure External Information
A0A077Z152 View 3D Structure Click here
A0A077ZE71 View 3D Structure Click here
A0A0H3GH55 View 3D Structure Click here
A0A0H5SKM8 View 3D Structure Click here
A0A0K0DVP7 View 3D Structure Click here
A0A0N4U688 View 3D Structure Click here
A0A0P0VU22 View 3D Structure Click here
A0A0R0J2P3 View 3D Structure Click here
A0A1D6JR11 View 3D Structure Click here
A0A2K6VW42 View 3D Structure Click here
A0A2R8Q896 View 3D Structure Click here
A0A3P7FM17 View 3D Structure Click here
A8AMR3 View 3D Structure Click here
C6TLS9 View 3D Structure Click here
D3ZY56 View 3D Structure Click here
G4VBZ2 View 3D Structure Click here
I1K9N5 View 3D Structure Click here
O28301 View 3D Structure Click here
O60888 View 3D Structure Click here
P69488 View 3D Structure Click here
P69489 View 3D Structure Click here
P69678 View 3D Structure Click here
P93009 View 3D Structure Click here
Q109R6 View 3D Structure Click here
Q20051 View 3D Structure Click here
Q328D1 View 3D Structure Click here
Q4CR41 View 3D Structure Click here
Q4CR56 View 3D Structure Click here
Q4CSL6 View 3D Structure Click here
Q4CT62 View 3D Structure Click here
Q57Y36 View 3D Structure Click here
Q5CX58 View 3D Structure Click here
Q5JDG6 View 3D Structure Click here
Q6D9J5 View 3D Structure Click here
Q6MGD0 View 3D Structure Click here
Q74XD3 View 3D Structure Click here
Q7CPA2 View 3D Structure Click here
Q7SIA8 View 3D Structure Click here
Q7T3C3 View 3D Structure Click here
Q83P43 View 3D Structure Click here