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. 2022 Mar 14;54(3):227–231. doi: 10.1038/s41588-022-01022-1

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© The Author(s) 2022

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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Extended Data Fig. 5 — a, Polymorphic residues encoded by Yr27 alleles present in various wheat cultivars. Blue asterisks indicate residues that are polymorphic between Lr13 and Yr27. Functional motifs are indicated in different colors. b, Shannon entropy plot showing amino acid diversity across Yr27 based on the alignment of 20 different haplotypes. c, Yr27-specific KASP marker tested on Yr27 positive, Yr27 negative and heterozygous wheat plants (Avocet 2B x Avocet S F2 population). d, Yr27 model superimposed to the Arabidopsis thaliana RPP1-ATR1 cryo-EM structure. The close-up view shows the RPP1-ATR1 contact interface in the LRR domain. The labeled residues are the ones that were polymorphic between Lr13 and Yr27. The three residues Q871, N895 and T899 are predicted to locate on the inner surface of the LRR domain and the corresponding residues in RPP1 have been shown to form polar interactions with the ATR1 effector (indicated by green dashed lines).