Figure 1.

Multiple alignment of the deduced amino acid sequences of Miamiensis avidus cysteine peptidases. The deduced amino acid sequences of Miamiensis avidus cysteine peptidases MaPro 1 to - MaPro 7 were aligned with Papain (the type peptidase of C1A superfamily, GenBank: AAB02650), Uronema marinum cathepsin L-like protein (UmCatL, GenBank: AAX51228), Homo sapiens cathepsin B protein (HsCatB, GenBank: AAH10240) and Uronema marinum cathepsin B protein (UmCatB, GenBank: AAR19103). The signal peptide, I29 (Inhibitor 29)/ Propeptide, Peptidase C1A domains are boxed. Conserved signatures of cathepsin L family proteins (ERFNIN and GNFD) with slight modifications in I-29 peptide of the cathepsin L-like proteins (MaPro 1- MaPro 5) are highlighted in bold, italic, grey shaded and indicated by ERFNIN and GNFD above the alignment. The catalytic triad residues (C, H and N) are marked in bold, grey shaded and indicated by sharp (#). Conserved proline residues at position 2 of the mature proteins are indicated by asterisk (*) and cysteine residues forming disulphide bonds are in bold, grey shaded and indicated by C above the alignment. S2 subsite determining enzyme substrate specificity is indicated by a black vertical arrow above the alignment. The predicted ‘occluding loop’, which is the specific feature of cathepsin B-like peptidases, is presented in only MaPro 6 and is indicated with a black thick underline.

Seo et al. BMC Veterinary Research 2013 9:10   doi:10.1186/1746-6148-9-10
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