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. 2016 Jan 19;6:1560. doi: 10.3389/fmicb.2015.01560

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Copyright © 2016 Li, Wang, Liu, Hao, Ma and Liu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Sequences-structure alignment of metacaspases. (A) TGGT1_206490, TGGT1_278975, and TGGT1_243298 protein sequence were aligned with sequences of human Caspase3, Caspase9, and yeast Yca1. The positions of identical and conserved residues in p20 domain are indicated by red-filled and non-filled rectangular frames, respectively. The conserved histidine and cysteine are indicated with red asterisk. Dots indicate gaps or missing residues. (B) The ternary structure of TgMCA was predicted by a model based on Yca1 (C) according to SWISS-Model and exhibited by Pymol. (D) Model pattern of the three ICE family proteins containing p20 domains in T. gondii, from top to bottom of the pattern, in order, TGGT1_206490, TGGT1_278975, and TGGT1_243298.