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. 2018 Feb 5;8:2435. doi: 10.1038/s41598-018-20802-6

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© The Author(s) 2018

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 structural comparison of aaNATs from Ae. aegypti and Eis proteins. (A) Multiple sequence alignment of N-acyltransferase superfamily region of Eis_Mtb, Eis_Msm, and Eis_Sen with the region of aaNAT2 from Ae. aegypti. (B) Superimposition of the N-acyltransferase superfamily structure within Eis_Mtb (colored in red) onto the structure within aaNAT2 (colored in yellow). (C) Superimposition of the 71–119 sequences of N-acyltransferase superfamily structure within Eis_Mtb (colored in red) onto the structure within aaNAT2 (colored in yellow). (D) Superimposition of the N-acyltransferase superfamily structure within Eis_Msm (colored in red) onto the structure within aaNAT2 (colored in yellow). (E) Superimposition of the 71–119 sequences of the N-acyltransferase superfamily structure within Eis_Mtb (colored in red) and the structure within Eis_Msm (colored in blue) onto the structure within aaNAT2 (colored in yellow).