The domain within your query sequence starts at position 21 and ends at position 156; the E-value for the FAD_binding_4 domain shown below is 7.6e-36.

PEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDK
EKKQVTVEAGILLTDLHPQLDKHGLALSNLGAVSDVTVGGVIGSGTHNTGIKHGILATQV
VALTLMKADGTVLECS

FAD_binding_4

 FAD_binding_4
PFAM accession number:PF01565
Interpro abstract (IPR006094):

Various enzymes use FAD as a co-factor, most of these enzymes are oxygen-dependent oxidoreductases, containing a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. One of the enzymes Vanillyl-alcohol oxidase (VAO, EC 1.1.3.38 ) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [ (PUBMED:10984479) ]. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging from aromatic amines to 4-alkylphenols.

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity (GO:0016491), flavin adenine dinucleotide binding (GO:0050660)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry FAD_binding_4