Multiple sequence alignment of the deduced amino acid sequence of EcCLP1 from Echinococcus canadensis with the amino acid sequence of other cathepsin proteases from several species. In the upper part of the figure, the stretch of amino acids that spans the signal peptide region is indicated by a solid line. The propeptide region is indicated by a dotted line drawn above the alignment. A N-linked glycosylation site is indicated by an arrow above the alignment. The ERFNIN and the AXNXFXD conserved motifs are indicated by squares in the propeptide region. Important residues for propeptide inhibition are indicated in the propeptide region. The asparagine residues at the juncture of the propeptide and mature enzyme, which are important for trans-activation (and propeptide removal) by asparaginyl endopeptidase, are underlined. The S2 subsite conserved residues are marked by squares and numbered according to papain numbering. CT: catalytic triad. DB: cysteine involved in a disulfide bond. OAH: oxyanion hole. EmCLP1 and EmCLP2 refer to the cathepsins L proteases from E. multilocularis [34] (accession numbers BAF02516.1 and BAF02517.1, respectively). The amino acid sequences of TsCL_1 and TsolCL correspond to the cathepsins L from T. solium [20, 21] (accession numbers AAS00027.1 and AQQ11627.1, respectively). FhCL1, FhCL2, and FhCL3 correspond to the amino acid sequences of cathepsins L1, L2, and L3 from F. hepatica [11, 27, 31] (accession numbers AAB41670.2, AAC47721.1 and QPX50259.1 respectively). SsCLP corresponds to the amino acid sequence of cathepsin L from Sus scrofa [35] (accession number Q28944 ⸳ CATL1_PIG). HsCLP1 and HsCKP1 correspond to the cathepsins L and K from H. sapiens (accession numbers NP_001244900.1 and NP_000387.1, respectively). CpPAP corresponds to the papain from Carica papaya (accession number AAB02650.1).