Summary: Cytochrome C1 family
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Cytochrome C1 Edit Wikipedia article
native structure of bovine mitochondrial cytochrome bc1 complex
Cytochrome C1 is formed in the cytosol and targeted to the mitochondrial intermembrane space. It is one of the constituents of complex III, which forms the third proton pump in the mitochondrial electron transport chain.
Cytochrome c1 is a subunit of the electron transport chain protein Ubiquinol Cytochrome c Reductase (UQCR, Complex III or Cytochrome bc1 complex), which consists of the products of one mitochondrially encoded gene, MTCYTB (mitochondrial cytochrome b) and ten nuclear genes: UQCRC1, UQCRC2, Cytochrome c1, UQCRFS1 (Rieske protein), UQCRB, UQCRQ ("11kDa protein"), UQCRH (cyt c1 Hinge protein), Rieske Protein presequence, "cyt. c1 associated protein", and UQCR ("Rieske-associated protein").
Ubiquinol:ferricytochrome c oxidoreductase is found in mitochondria, photosynthetic bacteria and other prokaryotes. The general function of the complex is electron transfer between two mobile redox carriers, ubiquinol and cytochrome c; the electron transfer is coupled with proton translocation across the membrane, thus generating proton-motive force in the form of an electrochemical potential difference that can drive ATP synthesis. In its structure and functions, the cytochrome bc1 complex bears extensive analogy to the cytochrome b6f complex of chloroplasts and cyanobacteria; cyt c1 plays an analogous role to cytochrome f, in spite of their different structures.
- http://www.ncbi.nlm.nih.gov/nuccore/98986462[full citation needed]
- http://www.ncbi.nlm.nih.gov/nucleotide/19923785[full citation needed]
- Prince, Roger C.; George, Graham N. (1995). "Cytochrome f revealed". Trends in Biochemical Sciences 20 (6): 217–8. doi:10.1016/S0968-0004(00)89018-0. PMID 7631417.
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Cytochrome C1 family Provide feedback
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Internal database links
|SCOOP:||CCP_MauG DHOR DUF1924 Dehyd-heme_bind GSu_C4xC__C2xCH Cytochrome_CBB3 Haem_bd Cytochrom_C550|
|Similarity to PfamA using HHSearch:||Cytochrom_C Cytochrome_CBB3|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002326
Cytochrome bc1 complex (ubiquinol:ferricytochrome c oxidoreductase) is found in mitochondria, photosynthetic bacteria and other prokaryotes. It is minimally composed of three subunits: cytochrome b, carrying a low- and a high-potential haem group; cytochrome c1 (cyt c1); and a high-potential Rieske iron-sulphur protein. The general function of the complex is electron transfer between two mobile redox carriers, ubiquinol and cytochrome c; the electron transfer is coupled with proton translocation across the membrane, thus generating proton-motive force in the form of an electrochemical potential that can drive ATP synthesis. In its structure and functions, the cytochrome bc1 complex bears extensive analogy to the cytochrome b6f complex of chloroplasts and cyanobacteria; cyt c1 plays an analogous role to cytochrome f, in spite of their different structures [PUBMED:7631417].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||electron carrier activity (GO:0009055)|
|heme binding (GO:0020037)|
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This family includes proteins where a covalently-bound haem completes the core. The core is three helices in an open folded leaf formation. The members are monodomain cytochromes.
The clan contains the following 13 members:CCP_MauG Cytochrom_C Cytochrom_C1 Cytochrom_C550 Cytochrome-c551 Cytochrome_CBB3 Dehyd-heme_bind DHC DHOR DUF1924 FixO Haem_bd PSCyt1
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Curation and family details
|Author:||Mian N, Bateman A|
|Number in seed:||59|
|Number in full:||1315|
|Average length of the domain:||207.10 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||71.38 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There are 15 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Cytochrom_C1 domain has been found. There are 91 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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