Additional file 4: of Cysteine peptidases of Eudiplozoon nipponicum: a broad repertoire of structurally assorted cathepsins L in contrast to the scarcity of cathepsins B in an invasive species of haematophagous monogenean of common carp

Amino acid sequence alignment of E. nipponicum cathepsins L with cathepsins L of F. hepatica. Signal peptides and pro-sequences were omitted. Numbers at the end of the lines show amino acid numbering of particular mature parts of the enzymes. Catalytic triad of the active site (C, H, N) is marked by triangles. Conserved motifs around active site residues are shaded in grey. Residues within the S2 subsite of the active site involved in determining the substrate specificity are shaded in black and indicated with numbers (papain numbering). Tripeptides of potential N-glycosylation sites are boxed. Predicted O-glycosylated residues are marked by grey squares. The alignment was made using the sequences of F. hepatica mature cathepsins L1 (GenBank: AAT76664.1) and L3 (GenBank: CAC12807.1). (PDF 1949 kb