The domain within your query sequence starts at position 51 and ends at position 457; the E-value for the DAO domain shown below is 1.9e-72.

DIVIVGGGIVGLASARTLILKHPGLSIGVVEKEKDLALHQTGHNSGVIHSGIYYKPESLK
AKLCVEGAALIYEYCNLKGIPYRQCGKLIVAVEQEEIPRLQALYERGLQNGVEGLRLIQQ
EDIKKKEPYCRGLMAIDCPYTGIVNYQQVALSFAQDFQEAGGSILRDFEVKGIEIAKENS
SRSKDGMNYPIAVKNSKGKEIRCRYVVTCAGLYSDRISELSGCNPDPQIVPFRGDYLVLK
PEKGYLVKGNIYPVPDSRFPFLGVHFTPRLDGTIWLGPNAVLAFKREGYRPFDFDARDVM
EVILKSGFINLVFQHFSYGVNEMYKACFLSETVKHLQKFIPEITISDVLRGPAGVRAQAL
DRDGNLVEDFVFDGGTGEIADRVLHVRNAPSPAATSSLAISRMIAEE

DAO

 DAO
PFAM accession number:PF01266
Interpro abstract (IPR006076):

This entry includes various FAD dependent oxidoreductases: glycerol-3-phosphate dehydrogenase ( EC 1.1.99.5 ), sarcosine oxidase beta subunit ( EC 1.5.3.1 ), D-amino acid dehydrogenase ( EC 1.4.99.1 ), D-aspartate oxidase ( EC 1.4.3.1 ).

D-amino acid oxidase ( EC 1.4.3.3 ) (DAMOX or DAO) is an FAD flavoenzyme that catalyzes the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have been characterised and sequenced in fungi and vertebrates where they are known to be located in the peroxisomes. D-aspartate oxidase ( EC 1.4.3.1 ) (DASOX) [ (PUBMED:1601857) ] is an enzyme, structurally related to DAO, which catalyzes the same reaction but is active only toward dicarboxylic D-amino acids. In DAO, a conserved histidine has been shown [ (PUBMED:1673125) ] to be important for the enzyme's catalytic activity.

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 DAO