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. 2019 Jun 27;10:2834. doi: 10.1038/s41467-019-10760-6

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© The Author(s) 2019

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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Fig. 3 — Trp643 is located in the DUF3506 domain. a EX1 protein comprises two predicted domains, UvrB/C and DUF3506. b Multiple alignment reveals that the DUF3506 domain is highly conserved across different plant species. The sequences of the EX1-like protein from the 27 plant species reported in Phytozome v12.1 were aligned using ClustalW. Two Trp residues, Trp565 and Trp643, were highlighted in red. Aligned DUF3506 domain sequences were visualized using WEBLOGO. c Tandem MS spectra of peptides ⁵⁶²GQWKGGK⁵⁶⁹ and ⁶⁴³W^oxVDGELVILDGK⁶⁵⁴ revealed the specificity of Trp643 in the context of Oxi-PTM. This experiment was repeated using three independent biological samples with reproducible results