Summary: Cytochrome C oxidase copper chaperone (COX17)
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This is the Wikipedia entry entitled "Cytochrome c oxidase". More...
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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.
4 Fe+2-cyochrome c + 4H+ + O2 â†’ 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.
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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 . The structure of Cox17  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.
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
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 ].
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)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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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
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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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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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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|Seed source:||Pfam-B_5838 (release 7.7)|
|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 build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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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 More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
Colouring and labels
Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.
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Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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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.