The domain within your query sequence starts at position 91 and ends at position 165; the E-value for the Fer2_2 domain shown below is 1e-29.

TVEGIGSTKTRIHPVQERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGN
LCRCTGYRPIVESAK

Fer2_2

Fer2_2
PFAM accession number:PF01799
Interpro abstract (IPR002888):

The [2Fe-2S] binding domain is found in a range of enzymes including dehydrogenases, oxidases and oxidoreductases.

The aldehyde oxido-reductase (Mop) from the sulphate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas is a homodimer of 907 amino acid residues subunits and is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centres. It is folded into four domains of which the first two bind the iron sulphur centres and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to a pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands [(PUBMED:7502041)].

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity (GO:0016491), metal ion binding (GO:0046872)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Fer2_2