Figure 3.. Sequence-based relationships among T.

Figure 3.

Sequence-based relationships among T. gondii cathepsins. A) Molecular phylogenetic relationships among cathepsin proteases in apicomplexan parasites. The tree was generated by neighbor-joining analysis using POWER ( Subgroups are shaded according to their similarity to cathepsins based on homology and the presence of an ERFNIN motif (cathepsin L-like) or occluding loop (cathepsin B-like). The analysis was restricted to apicomplexan parasites with complete or nearly complete genome sequences. One species from each genera was selected based on the maximal genome sequence coverage. Plasmodium SERA proteins were excluded due to their substantial divergence. The Plasmodium falcipains PfFP2a and PfFP2b are identical in sequence and thus are shown in the same dendrite. Note that the Babesia and Theileria proteases have not been systematically named previously and hence are designated here according to the nomenclature adopted for the Plasmodium and Cryptosporidium cathepsins. An asterisk indicates a protease missing at least one amino acid involved in catalysis. Abbreviations used: Bb, Babesia bovis; BP, Bovipain; Cp, Cryptosporidium parvum; CP, Cryptopain; Pf, Plasmodium falciparum; FP, falcipain; Tg, Toxoplasma gondii; Tp, Theileria parva; PP, parvapain. B) Multiple sequence alignment of apicomplexan cathepsin catalytic-proximal sequences. Sequences obtained from the MEROPS database ( include only the catalytic domain beginning six amino acids upstream of the catalytic cysteine and ending two amino acids downstream of the active site asparagine. Sequence alignment was compiled using ClustalW ( Fully conserved residues are indicated by asterisks and highly similar and similar residues are indicated by two dots and one dot, respectively. TpPP3 lacks the conserved cysteine residue in the catalytic site, which is replaced with an alanine.


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