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. 2023 Jan 25;14:11. doi: 10.1007/s12672-023-00618-1

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© The Author(s) 2023

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/.

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Fig. 2 — The amino acid sequence alignment of three hyaluronan synthases. CLUSTAL X was used for analyzing the multiple alignments of the amino acid sequence of HAS1, HAS2, HAS3. Then the result of alignment was visualized by ESPript 3.0. The transcript label listed on the left was the code from NCBI database of the amino acid sequence of HAS1, HAS2, and HAS3, respectively. The amino acid abbreviation in white color with red background presents the aligned sequences are identical, and words in red color present the aligned sequences have similar hydrophobicity, hydrophilicity or similar side chain. Word in black presents the aligned sequences that are not conservation