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. 2022 Dec 19;25(1):56–67. doi: 10.1038/s41556-022-01035-2

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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 — Multiple sequence alignment of Kar9 homologues of closely and distantly related yeast species. Conserved amino acid residues are indicated by the background color from strong (red) to no (blue) conservation, as well as by grey bars below the alignment. Consensus amino acids are indicated by the size of the letters below the alignment. Kar9 self-oligomerization interfaces are denoted by magenta (α), blue (β) and green (γ) arrowheads. Interface residues that were mutated in this study are indicated by asterisk in identical color. Related to Fig. 2.