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. 2016 Feb 3;9:65. doi: 10.1186/s13071-016-1351-6

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© Li et al. 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. 1 — Alignment of the predicted amino acid sequence of Haemonchus contortus 3-phosphoinositide-dependent protein kinase (Hc-PDK-1) with those of Caenorhabditis elegans (Ce-PDK-1; NP_001024742), Drosophila melanogaster (DSTPK61; Y07908) and Homo sapiens (Hs-PDK-1; AF017995). Functional domains are boxed, with coloured backgrounds: catalytic domain (light blue), nuclear export sequence (yellow) and pleckstrin homology domain (PH; light orange). An invariant tryptophan (W513) is coloured in grey, which is highly conserved in the PH domain and might be involved in interaction(s) with downstream signalling proteins [42]