Putative tyrosinase-like, Tyr-3 (IPR015559)

Short name: Tyr_3

Overlapping homologous superfamilies


Family relationships



Copper active sites play a major role in biological dioxygen activation. Oxygen intermediates have been studied in detail for the proteins and enzymes involved in reversible O(2) binding (hemocyanin), activation (tyrosinase), and four-electron reduction to water (multicopper oxidases). Tyrosinase binds two copper ions (CuA and CuB). Each of the two copper ions has been shown to be bound by three conserved histidines residues. The regions around these copper-binding ligands are well-conserved and also shared by some hemocyanins, which are copper-containing oxygen carriers from the hemolymph of many molluscs and arthropods [PMID: 12404359].

GO terms

Biological Process

GO:0042438 melanin biosynthetic process
GO:0055114 oxidation-reduction process

Molecular Function

GO:0005507 copper ion binding
GO:0016716 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen

Cellular Component

GO:0033162 melanosome membrane

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.