The domain within your query sequence starts at position 12 and ends at position 471; the E-value for the Amino_oxidase domain shown below is 1.7e-64.

ISGLAASYHLIRGPSPPKVILVEGSKRLGGWIRSIRGSDGAIFELGPRGIRPAGALGART
LLLVSELGLESEVLPVRGDHPAAQNRFLYVGGTLHPLPSGLRGLLRPSPPFSKPLFWAGL
RELLKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAE
QTHRSILLGLLLGAGQSPQPDSSLIRQARAERWSQWSLRGGLEVLPQALHNHLASKGVTV
LSGQPVCGLSLQPEGRWKVSLGDSSLEADHIISAIPASELSKLLPAEAAPLARILSTIKA
VSVAVVNLQYRGACLPVQGFGHLVPSSEDPTVLGIVYDSVAFPEQDGNPPSLRVTVMLGG
YWLQKLKAAGHQLSPELFQQQAQEAAATQLGLKEPPSHCLVHLHKNCIPQYTIGHWQKLD
SAMQFLTAQRLPLTLAGASYEGVAVNDCIESGRQAAVAVL

Amino_oxidase

Amino_oxidase
PFAM accession number:PF01593
Interpro abstract (IPR002937): This entry consists of various amine oxidases, including maize polyamine oxidase (PAO) [(PUBMED:9598979)], L-amino acid oxidases (LAO) and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. In vertebrates MAO plays an important role in regulating the intracellular levels of amines via their oxidation; these include various neurotransmitters, neurotoxins and trace amines [(PUBMED:9162023)]. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium [(PUBMED:7770050)]. PAOs in plants, bacteria and protozoa oxidise spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines [(PUBMED:9598979)]. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
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 Amino_oxidase