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Additional file 5: 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

By Lucie Jedličková (4916755), Hana Dvořáková (537198), Jan Dvořák (2720428), Martin Kašný (654757), Lenka Ulrychová (544269), Jiří Vorel (4916752), Vojtěch Žárský (3405173) and Libor Mikeš (849776)


Multiple alignment of all the complete/incomplete amino acid sequences of E. nipponicum cathepsins L inferred from the transcriptome of adult worms. Signal peptides are shaded in dark grey, position of the pro-region cleavage site is marked by arrows. ERFNIN- and GNFD-like motifs are underlined and indicated by underlined headings. The catalytic triad of the active site (C, H, N) is marked by triangles. Conserved motifs around active site residues are shaded in light 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. (PDF 5783 kb

Topics: Biochemistry, Cell Biology, Genetics, Molecular Biology, Pharmacology, Evolutionary Biology, Ecology, Developmental Biology, Infectious Diseases, Plant Biology, Computational Biology, Environmental Sciences not elsewhere classified, Cysteine peptidase, Protease, Cathepsin, S2 subsite, Haematophagy, Blood digestion, Monogenea, Diplozoidae, Eudiplozoon nipponicum, Fish parasite
Year: 2018
DOI identifier: 10.6084/m9.figshare.5954965.v1
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Provided by: FigShare
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