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7  structures 1184  species 0  interactions 1429  sequences 24  architectures

Family: COX17 (PF05051)

Summary: Cytochrome C oxidase copper chaperone (COX17)

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Cytochrome c oxidase". More...

Cytochrome c oxidase Edit Wikipedia article

The enzyme cytochrome c oxidase is a large transmembrane protein found in the mitochondrion and is the terminal electron acceptor in the electron transfer chain, taking four reducing equivalents from cytochrome c and converting molecular oxygen to water. In the process, it translocates protons, helping to establish a chemiosmotic potential that ATP synthase then uses to synthesize ATP.

Summary reaction:

4 Fe+2-cyochrome c + 4H+ + O2 → 4 Fe+3-cytochrome c + H20.

The complex is a large lipoprotein comprised of a number of metal prosthetic sites and 13 protein subunits, which in mammals, 10 are nuclear in origin and 3 are synthesized mitochondrially. The complex contains 2 cytochromes, the a and a3 cytochromes, and two copper centers, the CuA and CuB centers. In fact, the cytochrome a3 and CuB are a binuclear center and this is the site of oxygen reduction. The mechanism of action of this large complex is still an active research topic.

Further information

The Cytochrome Oxidase home page

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Cytochrome C oxidase copper chaperone (COX17) Provide feedback

Cox17 is essential for the assembly of functional cytochrome c oxidase (CCO) and for delivery of copper ions to the mitochondrion for insertion into the enzyme in yeast [1]. The structure of Cox17 [2] shows the protein to have an unstructured N-terminal region followed by two helices and several unstructured C-terminal residues. The Cu(I) binding site has been modelled as two-coordinate with ligation by conserved residues Cys23 and Cys26.

Literature references

  1. Takahashi Y, Kako K, Kashiwabara S, Takehara A, Inada Y, Arai H, Nakada K, Kodama H, Hayashi J, Baba T, Munekata E; , Mol Cell Biol 2002;22:7614-7621.: Mammalian copper chaperone cox17p has an essential role in activation of cytochrome C oxidase and embryonic development. PUBMED:12370308 EPMC:12370308

  2. Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC; , J Biol Chem 2004;279:53584-53592.: Yeast cox17 solution structure and Copper(I) binding. PUBMED:15465825 EPMC:15465825


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007745

Cox17p is essential for the assembly of functional cytochrome c oxidase (CCO). Binds and delivers two copper ions to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2) [ PUBMED:12370308 , PUBMED:19393246 ].

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 CHCH (CL0351), which has the following description:

The conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain) superfamily members include NADH-ubiquinone oxidoreductases, some cytochrome oxidases and yeast mitochondrial ribosomal proteins. Within each helix of the CHCH domain there are two cysteines present in a C-X9-C motif.

The clan contains the following 8 members:

CHCH Cmc1 COX17 COX6B CX9C MTCP1 NDUF_B7 Ndufs5

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...

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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
(91)
Full
(1429)
Representative proteomes UniProt
(2318)
RP15
(260)
RP35
(621)
RP55
(1056)
RP75
(1459)
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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
(91)
Full
(1429)
Representative proteomes UniProt
(2318)
RP15
(260)
RP35
(621)
RP55
(1056)
RP75
(1459)
Alignment:
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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
(91)
Full
(1429)
Representative proteomes UniProt
(2318)
RP15
(260)
RP35
(621)
RP55
(1056)
RP75
(1459)
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_5838 (release 7.7)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Moxon SJ , Mistry J , Wood V
Number in seed: 91
Number in full: 1429
Average length of the domain: 46.7 aa
Average identity of full alignment: 50 %
Average coverage of the sequence by the domain: 50.79 %

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 24.9 24.9
Trusted cut-off 24.9 25.0
Noise cut-off 24.8 24.8
Model length: 48
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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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 COX17 domain has been found. There are 7 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
A0A077Z184 View 3D Structure Click here
A0A0D2GEY0 View 3D Structure Click here
A0A175W4T1 View 3D Structure Click here
A0A1C1CAZ8 View 3D Structure Click here
A0A1D8PGA3 View 3D Structure Click here
A0A3P7EV95 View 3D Structure Click here
A0A5K4EZL7 View 3D Structure Click here
A4HRW2 View 3D Structure Click here
A4I0C1 View 3D Structure Click here
B6SNB3 View 3D Structure Click here
C0NKR2 View 3D Structure Click here
I1KDW4 View 3D Structure Click here
I1LT50 View 3D Structure Click here
P56394 View 3D Structure Click here
P81045 View 3D Structure Click here
Q12287 View 3D Structure Click here
Q14061 View 3D Structure Click here
Q4CYP3 View 3D Structure Click here
Q4D7M5 View 3D Structure Click here
Q4D970 View 3D Structure Click here
Q4E5Z7 View 3D Structure Click here
Q54ID0 View 3D Structure Click here
Q57XD6 View 3D Structure Click here
Q582X7 View 3D Structure Click here
Q66I53 View 3D Structure Click here
Q69Q87 View 3D Structure Click here
Q6J3Q7 View 3D Structure Click here
Q6K670 View 3D Structure Click here
Q76MV3 View 3D Structure Click here
Q8IJE6 View 3D Structure Click here
Q94FT1 View 3D Structure Click here
Q9LJQ9 View 3D Structure Click here
Q9P7Z7 View 3D Structure Click here
Q9TZ68 View 3D Structure Click here
Q9VXY5 View 3D Structure Click here
R4GF18 View 3D Structure Click here
U7Q612 View 3D Structure Click here
X1WCS1 View 3D Structure Click here