The domain within your query sequence starts at position 220 and ends at position 396; the E-value for the Oxidored_molyb domain shown below is 1.2e-62.

HLPVPNLDPHTYRLHVVGAPGGQSLSLSLDDLHKFPKHEVTVTLQCAGNRRSEMSKVKEV
KGLEWRTGAISTARWAGARLCDVLAQAGHRLCDSEAHVCFEGLDSDPTGTAYGASIPLAR
AMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHW

Oxidored_molyb

Oxidored_molyb
PFAM accession number:PF00174
Interpro abstract (IPR000572):

A number of different eukaryotic oxidoreductases that require and bind a molybdopterin cofactor have been shown [(PUBMED:2015248)] to share a few regions of sequence similarity. These enzymes include xanthine dehydrogenase (EC 1.1.1.204), aldehyde oxidase (EC 1.2.3.1), nitrate reductase (EC 1.7.1.1), and sulphite oxidase (EC 1.8.3.1). The multidomain redox enzyme NAD(P)H:nitrate reductase (NR) catalyses the reduction of nitrate to nitrite in a single polypeptide electron transport chain with electron flow from NAD(P)H-FAD-cytochrome b5-molybdopterin-NO(3). Three forms of NR are known, an NADH-specific enzyme found in higher plants and algae (EC 1.7.1.1); an NAD(P)H-bispecific enzyme found in higher plants, algae and fungi (EC 1.7.1.2); and an NADPH-specific enzyme found only in fungi (EC 1.7.1.3) [(PUBMED:2204158)]. The mitochondrial enzyme sulphite oxidase (sulphite:ferricytochrome c oxidoreductase; EC 1.8.2.1) catalyses oxidation of sulphite to sulphate, using cytochrome c as the physiological electron acceptor. Sulphite oxidase consists of two structure/function domains, an N-terminal haem domain, similar to cytochrome b5; and a C-terminal molybdopterin domain [(PUBMED:9428520)].

GO process:nitrate assimilation (GO:0042128)

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