Additional file 4: Table S3. of Evolutionary loss of peroxisomes – not limited to parasites

Table of putative peroxisomal enzymes and the prediction of their localization. (XLS 7288 kb

Additional file 3: Figure S1. of Evolutionary loss of peroxisomes – not limited to parasites

Phylogeny of Pex10 and other zinc-finger domain containing proteins showing, that O. dioica GSOIDT00013970001 sequence isn't monophyletic with eukaryotic Pex10 sequences. Bootsrap supports are shown. (PDF 351 kb

Additional file 4: Table S2. of Evolution of the Tim17 protein family

The overall distribution of Tim17 family protein in eukaryotes. (XLS 135 kb

Additional file 6: Table S4. of Evolution of the Tim17 protein family

Prokaryotic proteins carrying a PRAT motif [(G/A)X2(F/Y)X10RX3DX6(G/A/S)GX3G]. (PDF 133 kb

Additional file 2: Table S2. of Evolutionary loss of peroxisomes – not limited to parasites

Table of peroxins identified. (XLS 677 kb

Additional file 3: Figure S1. of Evolution of the Tim17 protein family

Protein sequence alignment of Tim22 from Homo sapiens, Saccharomyces cerevisiae and Neurospora crassa and HP20 and HP30 from Arabidopsis thaliana as performed by MAFFT [38]. The identical and similar residues were highlighted by turquoise and green color, respectively. The threshold value for shading was set to 50 %. (PDF 41 kb

Additional file 5: Figure S2. of Evolution of the Tim17 protein family

Protein sequence alignment of Romo1/Mgr2, Tim17 and Tim23 from Saccharomyces cerevisiae, Allomyces macrogynus, Homo sapiens, Monodelphis domestica and Trichoplax adherens as performed by MAFFT [38]. The grey cylinders denote the transmembrane regions. The identical and similar residues were highlighted by turquoise and green color, respectively. The threshold value for shading was set to 50 %. (PDF 25 kb

Raw multibeam EM122 data: transits of Maria S. Merian cruise MSM60/2 (South Atlantic)

Specific EnCL1/EnCL3 primers for the synthesis of probes for RNA in situ hybridisation. (PDF 84 kb

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

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

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