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. 2017 Nov 16;8:1541. doi: 10.1038/s41467-017-01642-w

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© The Author(s) 2017

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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Fig. 1 — Sequence and structural analysis of human NUDIX hydrolases. a Consensus phylogenetic tree of full length Human NUDIX proteins with posterior probabilities of each branch provided. Distinct groups with known structures are overlaid for comparison. MTH1 (purple) and NUDT15 (light blue); NUDT5 (gray) and NUDT14 (black); NUDT21 (pink) and NUDT2 (brown); NUDT6 (firebrick red), NUDT3 (yellow), and NUDT10 (orange). b Known structures of human NUDIX proteins modeled in cartoon format with the NUDIX box colored in blue, NUDIX fold domain in green, and remaining structure colored in gray. c Graphical representation of the different domains within the human NUDIX hydrolases