The domain within your query sequence starts at position 68 and ends at position 161; the E-value for the Rieske domain shown below is 3.6e-18.
VEATVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVR CPWHGACFNISTGDLEDFPGLDSLHKFQVKIEKE
Rieske |
![]() |
---|
PFAM accession number: | PF00355 |
---|---|
Interpro abstract (IPR017941): | There are multiple types of iron-sulphur clusters which are grouped into three main categories based on their atomic content: [2Fe-2S], [3Fe-4S], [4Fe-4S] and other hybrid or mixed metal types. Two general types of [2Fe-2S] clusters are known and they differ in their coordinating residues. The ferredoxin-type [2Fe-2S] clusters are coordinated to the protein by four cysteine residues. The Rieske-type [2Fe-2S] cluster is coordinated to its protein by two cysteine residues and two histidine residues [ (PUBMED:16168954) (PUBMED:16271700) ]. The structure of several Rieske domains has been solved [ (PUBMED:8736555) ]. It contains three layers of antiparallel beta sheets forming two beta sandwiches. Both beta sandwiches share the central sheet 2. The metal-binding site is at the top of the beta sandwich formed by the sheets 2 and 3. The Fe1 iron of the Rieske cluster is coordinated by two cysteines while the other iron Fe2 is coordinated by two histidines. Two inorganic sulphide ions bridge the two iron ions forming a flat, rhombic cluster. Rieske-type iron-sulphur clusters are common to electron transfer chains of mitochondria and chloroplast and to non-haem iron oxygenase systems:
|
GO process: | oxidation-reduction process (GO:0055114) |
GO function: | 2 iron, 2 sulfur cluster binding (GO:0051537) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Rieske