The domain within your query sequence starts at position 96 and ends at position 314; the E-value for the Cytochrom_C1 domain shown below is 1.5e-100.

WSHRGLLSSLDHTSIRRGFQVYKQVCSSCHSMDYVAYRHLVGVCYTEEEAKALAEEVEVQ
DGPNDDGEMFMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRARHGGEDYVFSLL
TGYCEPPTGVSLREGLYFNPYFPGQAIGMAPPIYTEVLEYDDGTPATMSQVAKDVATFLR
WASEPEHDHRKRMGLKMLLMMGLLLPLTYAMKRHKWSVL

Cytochrom_C1

Cytochrom_C1
PFAM accession number:PF02167
Interpro abstract (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) ].

This entry also includes Nitrosomonas europaea petC, which is a subunit of the ammonia monooxygenase complex that catalyzes the oxidation of ammonia to hydroxylamine, the first reaction in the process of ammonia oxidation to nitrite [ (PUBMED:19453274) ].

GO function:electron transfer activity (GO:0009055), heme binding (GO:0020037)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Cytochrom_C1