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. 2018 Sep 10;8:13563. doi: 10.1038/s41598-018-31634-9

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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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Analyses of ETT domains, order-disorder prediction and secondary structure prediction. (A) Protein sequence alignment by SIM between ETT/ARF3 and its closest homologue ARF4. Different colours indicate percentage similarity. Below, schematic representation of the ETT showing limit of DNA binding domain (cyan) as determined by alignment with ARF4 and the following ETT-Specific (ES) domain (dark green). (B) Y2H assay between the ETT and IND, an A. thaliana transcription factor previously identified as ETT interactor⁸, and ETT-ES domain and IND. Interaction is observed on the selective plate -W-L-H-A. Yeast growth is inhibited by IAA in the media (lower panel). (C) A disorder prediction and putative protein binding regions for full-length ETT by PrDos and DISOPRED3 servers. (D) Secondary structure prediction by SOPMA.