The domain within your query sequence starts at position 512 and ends at position 664; the E-value for the Succ_DH_flav_C domain shown below is 3.4e-43.

RLNMQKSMQNHAAVFRVGSVLQEGCEKISQLYGDLKHLKTFDRGMVWNTDLVETLELQNL
MLCALQTIYGAEARKESRGAHAREDYKVRVDEYDYSKPIQGQQKKPFGEHWRKHTLSYVD
IKTGKVTLEYRPVIDKTLNEADCATVPPAIRSY

Succ_DH_flav_C

 Succ_DH_flav_C
PFAM accession number:PF02910
Interpro abstract (IPR015939):

This entry represents a domain with a spectrin-repeat-like fold consisting of three helices in a closed bundle with a left-handed twist. This domain is found in the succinate dehydrogenase/fumarate reductase oxidoreductase family of proteins, such as:

  • L-aspartate oxidase ( EC 1.4.3.16 ), a flavoenzyme component of the bacterial quinolinate synthase system that catalyses the conversion of L-aspartate to oxaloacetate, the first step in the de novo biosynthesis of NAD+ [ (PUBMED:11863440) (PUBMED:10425677) ].

  • Fumarate reductase, which is part of the quinol-fumarate reductase (QFR) respiratory complex that catalyses the terminal step of anaerobic respiration when fumarate acts as the terminal electron acceptor [ (PUBMED:11850430) ].

  • Succinate dehydrogenase (SQR; EC 1.3.5.1 ), an iron-sulphur flavoenzyme from bacteria that is analogous to the mitochondrial respiratory complex II, forming part of the electron transport pathway from the electron acceptor (succinate) to the terminal donor (ubiquinone) [ (PUBMED:12560550) ].

  • Adenylylsulphate reductase A subunit ( EC 1.8.4 ), an iron-sulphur flavoenzyme that catalyses the reversible reduction of adenosine-5'-phosphate (APS) to sulphite and AMP [ (PUBMED:11842205) ].

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity (GO:0016491)

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