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. Author manuscript; available in PMC: 2008 Feb 23.
Published in final edited form as: Insect Biochem Mol Biol. 2007 Nov 17;38(2):190–200. doi: 10.1016/j.ibmb.2007.10.008

Figure 2.

Figure 2

Multiple sequence alignment of the deduced Aedes aegypti JHA15 with other insect serine proteases. The sequences listed were retrieved from GenBank and the alignment was performed using MultAlin (http://bioinfo.genopoletoulouse.prd.fr/multalin/multalin.html). Solid triangles (▼) mark the active site residues of the catalytic triad (His/Asp/Ser), and the Gly residue characteristic of chymotrypsin-like serine proteases is indicated by an arrow (↓). Six conserved cysteines corresponding to the sites of the predicted disulfide bridges are denoted by asterisks (*). AaJHA15, Ae. aegypti chymotrypsin-like serine protease, AAX56968; CpiChyL, Culex pipiens chymotrypsin-like serine protease, AY958427; AaChy1, Ae. aegypti chymotrypsin 1, AAB01218; AgChyL, Anopheles gambiae chymotrypsin-like serine protease, AAC02700; AaLT1, Ae. aegypti late trypsin, AAA29356; AaChy2, Ae. aegypti chymotrypsin II-like protein, AAF43707; AgChy1, An. gambiae chymotrypsin-like protease ANCHYM1, CAA83568; AgChy2, An. gambiae chymotrypsin-like protease ANCHYM2, CAA83567; AaET1, Ae. aegypti early trypsin, 2211307A; AgTryp1, An. gambiae trypsin 1, CAA80513.