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. 2016 Sep 13;9(1):497. doi: 10.1186/s13071-016-1785-x

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© The Author(s). 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 5 — Alignment of myoglobin orthologs from Paragonimus species and other trematodes. Although assembly fragmentation resulted in a truncated sequence from P. skrjabini, it had greater 90 % similarity with Paragonimus myoglobin (at the amino acid level), with much less similarity to myoglobins from other trematodes. Abbreviations: Pk, Pk34178_txpt1 [16]; Pw, comp20873_c0_seq2; Ps, comp80973_c0_seq3; Cs, C. sinensis gi:349998765; Ov, Opisthorchis viverrini gi: 663047528; Fh, F. hepatica gi:159461074; Sm, S. mansoni gi:256084837; Sj, S. japonicum gi:226487206