The domain within your query sequence starts at position 195 and ends at position 427; the E-value for the Cu-oxidase_4 domain shown below is 1.1e-60.

TTRTGGISSVPTLSSLNLFSSSKRRDPKVVVQENVRRLANAAGFNAEKFYRIKTDHASEV
WVMGKKEPESYDGIVTNQRGVTITALGADCIPIVFADPVKKACGVAHSGWKGTLLGVAMA
TVNAMIAEYGCDVEDIIVVLGPSVGSCCFTLPKESAVSFHSLHPSCVRHFDSPRPYVDIR
KATRILLERGGILPQNIQDQKEDLDLCTSCHPEKFFSHVRDGLNFGTQIGFIS

Cu-oxidase_4

Cu-oxidase_4
PFAM accession number:PF02578
Interpro abstract (IPR003730):

Laccases are multi-copper oxidoreductases able to oxidise a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms [ (PUBMED:16740638) ].

This family consists of polyphenol oxidases with laccase activity from bacteria. They may constitute a new laccase subfamily, as they lack sequence relatedness to known laccases [ (PUBMED:16740638) ]. This family also includes laccase domain-containing protein 1 (Lacc1, FAMIN), which is thought to be a central regulator of immunometabolic function in humans [ (PUBMED:27478939) (PUBMED:28593945) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Cu-oxidase_4