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. Author manuscript; available in PMC: 2016 Apr 1.
Published in final edited form as: Insect Biochem Mol Biol. 2015 Feb 17;59:58–71. doi: 10.1016/j.ibmb.2015.02.005

Figure 1.

Figure 1

Alignment of four MCO1 orthologs. Predicted signal peptides are indicated by bold italics. Von Willebrand factor domains are in purple text. Cysteine-rich regions are in green. Putative carboxyl-terminal transmembrane regions are in blue. Predicted copper binding residues are in orange. Three predicted cupredoxin-like domains are delineated with blue vertical lines. The sequences that were used to express recombinant enzymes are between red vertical lines. The extra residues present in the longer versions of TcMCO1 and MsMCO1 are in red. The arginine residue that was mutated in DmMCO1 and AgMCO1 to generate uncleaved recombinant protein is highlighted in black. Three putative iron binding residues are indicated by highlighting. Asp380 (magenta) and Glu552 (green) were identified by their alignment with iron binding residues in Fet3p. His374 (yellow) was identified by analyzing a homology model of DmMCO1 (see section 3.9).