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. 2018 Feb 13;8:2946. doi: 10.1038/s41598-018-20920-1

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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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Sequences logos of the ST conserved motifs. Four multiple sequence alignment of all the ST sequences corresponding to 102 opisthokonts, 23 Bacteria, 119 protists/Archaeplastida GT29 ST and 5 ST of GT42 CAZy family sequences was carried out with MUSCLE in MEGA7.0.18⁶⁴ (Supplemental data 1). The informative region used was restricted to the ST catalytic domain encompassing the 4 conserved sialylmotifs i.e. L (39–45 aa), S (21–23 aa), III (1–4 aa) and VS (1–6 aa) as defined previously⁴⁰. Sequence logos of each sialylmotif in the 4 groups of ST sequences show sequence conservation as the overall height of the stack and the relative frequency as the height of symbols within the stack. Symbols are colored according to their chemical properties polar amino acids (G, C, S, T, Y) are green, basic (K, R,H) are blue, acidic (D, E) are red, hydrophobic (A, V, L, I, P, W, F, M) are black and neutral polar amino acids (N, Q) are pink^95,96.