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. 2021 Jan 14;22:51. doi: 10.1186/s12864-020-07365-5

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© The Author(s) 2021

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. 7 — The amino acid sequence of DgAPX was compared with that of other plants. Note: The black triangles indicated the heme binding site, the substrate binding site, and the K⁺ binding site in turn; the red triangles indicated the lysine crotonylation site on the amino acid sequence of DgAPX; the red rectangles indicated the ascorbate peroxidase conserved domain. AoAPX2 (XP_020276942.1) from Asparagus officinalis; CaAPX1 (NP_001311967.1) from Capsicum annuum; MsAPX2 (AIY27528.1) from Medicago sativa; NtAPX2 (NP_001311803.1) from Nicotiana tabacum; RhAPX1 (ATP66493.1) from Rosa hybrid cultivar; SiAPX2 (NP_001318094.1) from Solanum lycopersicum; SpAPX1 (XP_015079739.1) from Solanum pennellii