The domain within your query sequence starts at position 530 and ends at position 730; the E-value for the Lysyl_oxidase domain shown below is 3.9e-103.

SDLLLHSALVQETAYIEDRPLHMLYCAAEENCLASSARSANWPYGHRRLLRFSSQIHNLG
RADFRPKAGRHSWVWHECHGHYHSMDIFTHYDILTPNGTKVAEGHKASFCLEDTECQEDV
SKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVKPGNYILQVVINPNFEVAESDFTN
NAMKCNCKYDGHRIWVHNCHI

Lysyl_oxidase

Lysyl_oxidase
PFAM accession number:PF01186
Interpro abstract (IPR001695):

Lysyl oxidase (EC 1.4.3.13) (LOX) [(PUBMED:8104038)] is an extracellular copper-dependent enzyme that catalyses the oxidative deamination of peptidyl lysine residues in precursors of various collagens and elastins, yielding alpha-aminoadipic-delta-semialdehyde. The deaminated lysines are then able to form semialdehyde cross-links, resulting in the formation of insoluble collagen and elastin fibres in the extracellular matrix [(PUBMED:1357535)].

The active site of LOX resides towards the C terminus: this region also binds a single copper atom in an octahedral coordination complex involving at least 3 His residues [(PUBMED:1352776)]. Four histidine residues are clustered in a central region of the enzyme. This region is thought to be involved in cooper-binding and is called the 'copper-talon' [(PUBMED:8104038)].

GO process:oxidation-reduction process (GO:0055114)
GO function:copper ion binding (GO:0005507), oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor (GO:0016641)

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