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. 2018 Jul 4;8:10108. doi: 10.1038/s41598-018-28214-2

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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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Comparison of activating enzymes for Ubiquitin and Ubl proteins with those for the MoaD and ThiF. The four Ubls whose E1s are most closely related are ubiquitin, SUMO, NEDD8 and ISG15 and their family members. The Ubl E1s are 110–120 kDa and are either single polypeptides or heterodimers of two polypeptides, corresponding to the sequence and structure of MoeB. The E1s of ubiquitin and ISG15 are single polypeptides. In case of heterodimeric E1s (SUMO and NEDD8 cascade), one subunit corresponds to N terminal half of the single-chain E1s and other subunit of the heterodimer corresponds to C-terminal of half. The N- and C-terminal halves of the E1s for ubiquitin, SUMO, NEDD8 and ISG15 are partially homologous to each other, and the region of sequence homology between the two halves is also the region of sequence homology to MoeB and ThiF.