Figure 1. Alignments of the deduced amino acid sequences. (A) Homology shared among all three Mayetiola destructor GSTs, MdesGST-1 (AAS00666), MdesGST-2 (DQ662542) and MdesGST-3 (DQ662543). The boxed sequence of MdesGST-2 represents the N-terminal extension constituted by a hydrophobic/acidic motif. (B) Homology of MdesGST-2 with sequences from other insect Sigma GSTs: Musca domestica (P46437), and Drosophila melanogaster (AAM48357). Filled and open circles represent residues that constitute the putative glutathione (GSH) and electrophilic-substrate binding sites, respectively. The putative H-site residue of MdesGST-2 (L62), which also contacts GSH, is indicated by an asterisk. The bulge-inducing residue (G205) of MdesGST-2 is marked with an inverted filled triangle. C) Homology of MdesGST-3 with sequences from other insect Delta GSTs: Anopheles gambiae (40889324), and Episyrphus balteatus (CAH58743). S11 and N49 of MdesGST-3, which represent the catalytic pocket, are indicated with an asterisk. Amino acid residues determining folding are marked with open circles. In all three panels, identical residues among all taxa are highlighted in black and identical residues in two of the three taxa are highlighted in gray. Gaps in the alignment are indicated by dashes.