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 |
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PFAM accession number: | PF02578 |
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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