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. 2019 Jul 29;9:10914. doi: 10.1038/s41598-019-47494-w

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© The Author(s) 2019

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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Sequence alignment of the Sp domain of human ADAMTS-1, -4, -5 and -13. Uniprot accession numbers were Q9UHI8 (ADAMTS-1, aa 725–749), O75173 (ADAMTS-4, aa|686–837), Q9UNA0 (ADAMTS-5, aa 732–874) and Q76LX8 (ADAMTS-13, aa 556–685). Percentage identities were 23.9, 17.6 and 14.2%, respectively, compared with ADAMTS-13. Beta strands and β1-β2, β3-β4 and β9-β10 loops are indicated. In ADAMTS-13, the vWF-binding exosite in loop β9-β10 is highlighted. Boxes indicate amino acids conserved in at least three of the four enzymes and are coloured according physicochemical properties (purple, positively charged; yellow, negatively charged; green, apolar; cyan, polar).