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. 2019 May 21;46(8):1225–1235. doi: 10.1007/s10295-019-02189-z

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© The Author(s) 2019

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.

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Fig. 5 — a Prediction of conserved residues through Shannon entropy measurements on a multiple sequence alignment of modular type I DH domains taken from ClusterCAD. Low Shannon entropy measurements correspond to low levels of amino acid substitution. The secondary structure of the FluA DH M1 was used to give a relative position within the MSA. Regions highlighted in red display the His/Asp catalytic dyad and the regions highlighted in yellow correspond the two most highly variable regions amongst the known modular type I DH domain structures. b Close-up of the region between α3 and β11. The overall height of the stack indicates the sequence conservation at that position (colour figure online)