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. 2020 Dec 1;21:851. doi: 10.1186/s12864-020-07242-1

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. 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 in a credit line to the data.

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Fig. 3 — Amino acid sequence identity comparison among the four S-layer protein homologs in KUST (kustd1514), KUST2012 (kustd1514b), strain MBR1 (KSMBR1_1301), and strain CSTR1 (KsCSTR_09970). Shown are always comparisons of the two sequences indicated on the right side. Positions (aa) refer to the amino acid (aa) positions in the alignment of the four proteins. Window size: 20 amino acids. Step: 1 amino acid