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. 2017 Jul 24;7:6312. doi: 10.1038/s41598-017-06395-6

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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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Minispryn bioinformatics. (a) Domain architecture of minispryn and related proteins. Minispryn, myospryn and two members of the TRIM-protein family share extensive sequence similarity at their C-termini. While the TRIM proteins are E3 ubiquitin ligases, the absence of the RING domain in minispryn and myospryn probably preclude this function. (b) Multiple sequence alignment. The complete coding sequence of minispryn aligns with amino acids 3171–3739 of myospryn (CAE02649.1), 139–706 of midline-1 (XP_017173902) and 123–366 of murf3 (NP_067422.1) spanning the BBOX/BBOX’ and BBC domains of each protein and the FN3 and SPRY domains of myospryn and midline-1.