The domain within your query sequence starts at position 708 and ends at position 1241; the E-value for the Ald_Xan_dh_C2 domain shown below is 8.7e-183.

QYESFIGPERKLEQGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKGEDKEMDI
YVSSQDAAFTQEMVARTLGIPKNRINCHVKRVGGAFGGKASKPGLLASVAAVAAQKTGRP
IRFILERRDDMLITGGRHPLLGKYKIGFMNNGKIKAADIQLYINGGCTPDDSELVIEYAL
LKLENAYKIPNLRVRGRVCKTNLPSNTAFRGFGFPQGAFVTETCMSAVAAKCRLPPEKVR
ELNMYRTIDRTIHNQEFDPTNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIP
MKFSVGFPKTFYYQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIH
LDEMSTVTVPNTVTTGASTGADVNGRAVQNACQILMKRLEPIIKQNPSGTWEEWVKEAFV
QSISLSATGYFRGYQADMDWEKGEGDIFPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDG
SFSINPAVDIGQIEGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVTDIP

Ald_Xan_dh_C2

Ald_Xan_dh_C2
PFAM accession number:PF02738
Interpro abstract (IPR008274):

Aldehyde oxidase (EC 1.2.3.1) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase (EC 1.1.1.204) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase (EC 1.1.3.22) activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.

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 Ald_Xan_dh_C2