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. 2024 Jul 1;25(8):3348–3372. doi: 10.1038/s44319-024-00183-w

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© The Author(s) 2024

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 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/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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Figure EV1 — (A, B) Domain architecture and amino acid conservation of (A) Mis18α and (B) Mis18β. Alignments include Homo sapiens (hs), Bos taurus (bt), Mus musculus (mm) and Gallus gallus (gg). The conservation score is mapped from red to cyan, where red corresponds to highly conserved and cyan to poorly conserved. Secondary structures as annotated/predicted by Conserved Domain Database [CDD] and PsiPred, http://bioinf.cs.ucl.ac.uk/psipred. Multiple sequence alignments were performed with MUSCLE (Madeira et al, 2019) and edited with Aline (Bond and Schüttelkopf, 2009). Dashed boxes highlight Yippee domains whilst solid boxes highlight C-terminus α-helices. (C) Superposition of Mis18β_Yippee structures predicted by AlphaFold (light pink) and RaptorX (green). RaptorX generated five models and the model with the lowest estimated error (1.9 Å) is shown here. The AlphaFold and RaptorX models superpose well with an RMSD of 0.95 Å. (D) The PAE plot corresponding to the Mis18α/β_Yippee AlphaFold model shown in Fig. 1D.