Figure 2: Multiple amino acid sequence alignment of the two putative copper-binding sites. An analysis of sequence alignment of tyrosinase of different species and hemocyanin was performed using the multiple align show (http://www.bioinformatics.org/sms/multi_align.html) server. Five highly conserved histidine residues are indicated by asterisks. The histidine residue present in molluscan tyrosinase is indicated by the diamond. Gaps (_) have been introduced to optimize the alignment. The identical amino acid residues and similar amino acid residues are indicated as black shading and as very light gray shading, respectively. Three subclasses (α, β, and γ) were shown, as described in Aguilera et al. [2]. Abbreviations are as follows and GenBank accession numbers are in parenthesis. PfTy, Pinctada fucata tyrosinase-like protein (AB353113); Pfty1, Pinctada fucata tyrosinase-like protein 1 (AB254132); Pfty2, Pinctada fucata tyrosinase-like protein 2 (AB254133); PmaaT1, Pinctada margaritifera tyrosinase 1 (HE610377); PmaaT2, Pinctada margaritifera tyrosinase 2 (HE610378); PfT, Pinctada fucata tyrosinase (DQ112679); IllexT, Illex argentinus tyrosinase precursor 2 (AB107881); PmaiT1, Pinctada martensii tyrosinase-like protein tyr-1 (KC870906); Xenopus TRP, Xenopus laevis tyrosinase-related protein 1 (NM_001087023); HomoT, Homo sapiens tyrosinase (NM_000372); MusT, Mus musculus tyrosinase (NM_011661); SuberitesT, Suberites domuncula tyrosinase-like protein (AJ574915); ScyllaPO, Scylla serrata prophenoloxidase (ABD90511); DrosophilaPO, Drosophila melanogaster prophenol oxidase A1 (NP_476812); AnophelesPPO, Anopheles gambiae polyphenoloxidase (XM_315074); and LimulusHcII, Limulus polyphemus hemocyanin subunit II (AM260213).