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. 2013 Apr 5;5(5):860–875. doi: 10.1093/gbe/evt056

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© The Author(s) 2013. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Fig. 2.— — Protein sequence alignment of MPP domains responsible for catalytic activity (zinc-binding site) and substrate recognition (glycine-rich loop). Positions of functionally important AA are marked by asterisks; conserved AA are in boxes. Accession numbers for protein sequences of α-MPP (Euglena gracilis, P43265; Trypanosoma brucei, XP_951618; Leishmania major, XP_001682967; Saccharomyces cerevisiae, NP_011889; Homo sapiens, NP_055975; Caenorhabditis elegans, NP_490888), β-MPP (E. gracilis, P43264; T. brucei, XP_803756; L. major, XP_003721587; S. cerevisiae, NP_013264; H. sapiens, NP_004270.2; C. elegans, NP_501576), cp1 (T. brucei, XP_844780; L. major, XP_001686023; S. cerevisiae, NP_009508; H. sapiens, NP_003356; Arabidopsis thaliana, NP_186858; C. elegans, NP_498202), and cp2 (E. gracilis, EC675176; T. brucei, XP_828477; L. major, XP_001681831; S. cerevisiae, NP_015517; H. sapiens, NP_003357; A. thaliana, NP_175610; C. elegans, NP_510011).