Summary: Cytochrome C oxidase copper chaperone (COX17)
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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
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
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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
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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
SCOOP: | CHCH UPF0203 |
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.
Cellular component | mitochondrial intermembrane space (GO:0005758) |
Molecular function | copper ion binding (GO:0005507) |
copper chaperone activity (GO:0016531) |
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 Ndufs5Alignments
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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Seed (91) |
Full (1429) |
Representative proteomes | UniProt (2318) |
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RP15 (260) |
RP35 (621) |
RP55 (1056) |
RP75 (1459) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (91) |
Full (1429) |
Representative proteomes | UniProt (2318) |
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RP15 (260) |
RP35 (621) |
RP55 (1056) |
RP75 (1459) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
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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.
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Curation and family details
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Curation
Seed source: | Pfam-B_5838 (release 7.7) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Moxon SJ |
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
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: | 48 | ||||||||||||
Family (HMM) version: | 16 | ||||||||||||
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 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.