Additional file 8: 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 cathepsin B with cathepsins B of S. mansoni. Whole zymogens including a signal peptide were aligned. Numbers at the end of the lines show amino acid numbering of the mature parts of particular enzymes. Position of the pro-region cleavage site is marked by an arrow. The catalytic triad of the active site (C, H, N) is marked by triangles. Conserved motifs around active site residues are shaded in grey. Tripeptides of potential N-glycosylation sites are boxed. Predicted O-glycosylated residues are marked by grey squares. The occluding loop typical of cathepsins B is underlined. The ‘haemoglobinase motif’ ascribed to cathepsins B with an assumed function in haemoglobinolysis in blood-feeding helminths, is shaded in black (it is modified in SmCB2 and EnCB). Residues within the S2 subsite of the active site involved in determining the substrate specificity are marked by a black dot and indicated with number (papain numbering). The alignment was made using sequences of Schistosoma mansoni cathepsins B1 (GenBank: CAD44624.1) and B2 (GenBank: XP_018651608.1). (PDF 1923 kb