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. 2020 Aug 7;10:13424. doi: 10.1038/s41598-020-70431-1

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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 and structural features of Dsup and Dsup-like proteins. (a) Sequence alignment obtained with Clustal-Omega 1.2.4 of the 445-residue Dsup protein from R. varieornatus (Rv) and the 328-residue Dsup-like protein from H. exemplaris (He) (“*” indicates perfect alignment whereas “:” and “.” indicate sites belonging to groups showing strong and weak similarity, respectively), highlighting the sequence motifs indicated in the box below. (b) Bar chart giving the % and number of each amino acid type according to the colour code: black = non-polar, green = polar, blue = positively charged, red = negatively charged. (c) Sequence segments with their corresponding structural models obtained by homology-modelling with SwissModel. (d) Structural disorder predicted from sequence with four predictors. The disorder score is defined in the range 0–1 with values > 0.5 meaning disorder (DISOPRED 3 gives no values with score < 0.5). Conserved motifs in both proteins, segments modelled by homology-modelling, HMGN-like and NLS sequences are the regions shaded light grey, light green, light yellow and light red, respectively. (e) Structural 3D models predicted from sequence by I-TASSER. Charged amino acids are shown as balls (positive in blue and negative in red) with labels indicating the sequence segments in which they accumulate. Regions marked with orange ovals enclose the second conserved motif 262–275 and 214–228 in Rv and He proteins, respectively.