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. 2020 May 14;10:7990. doi: 10.1038/s41598-020-64820-9

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Sequence alignment and molecular phylogenetic analysis of the PkanSP15 proteins. (A,B) Protein sequence alignment and similarity and identity percentages of PkanSP15 using Muscle. Black shading and gray shading represent identical and similar amino acids, respectively. (C) The evolutionary history was inferred by using the Maximum Likelihood method based on the Whelan and Goldman model⁵⁸. The tree with the highest log likelihood (−8196.26) is shown. The percentage of trees in which the associated taxa clustered together is shown above the branches. The tree is drawn to scale, with branch lengths measured in protein sequences number of substitutions per site. The analysis involved 78 amino acid sequences. All positions with less than 95% site coverage were eliminated. Evolutionary analyses were conducted in MEGA7⁵⁷. Red asterisks highlight PkanSP15 proteins and the black asterisk the PdSP15 protein. (D) Protein sequence alignment of PdSP15 and PkanSP15 using Muscle. Black shading and gray shading represent identical and similar amino acids, respectively.