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. 2018 Oct 5;8:14891. doi: 10.1038/s41598-018-33143-1

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© The Author(s) 2018

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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Predicted 3-dimensional structure of CRAM-1 indicates a UBA-like domain. Structures of the CRAM-1 C-terminal region (a) and the full-length model (b) show the same bundle of three helices connected by loops. (c) Structural comparison of the CRAM-1 C-terminal region (red) with the UBA domain of human RAD23A (green). Superimposed structures illustrate structural agreement, with RMSD (root-mean-square deviation) = 1.14 Å. (d) C-terminal region of CRAM-1 (red) superimposed on the UBA domain of ceRAD-23 (green), RMSD = 1.02 Å. (e) Sequence alignment, based on superimposition of 3-dimensional structures, showing 3 α helices with conserved hydrophobic residues (highlighted in gold) and nearby exposed hydrophobic residues (boxes).