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. 2017 Jan 26;8:44. doi: 10.3389/fpls.2017.00044

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Copyright © 2017 Luo, Tang, Mei, Peng, Li, Li, Yan, Zeng, Liu, Wu and Wu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Conserved domain in the deduced BnSIP1-1 protein. (A) Structure of the deduced BnSIP1-1 protein of Brassica napus. The trihelix DNA binding domains are shown in yellow. The fourth amphipathic a-helix is shown in orange. The long, uninterrupted α-helical sequence in the C terminus is shown in blue. (B) Amino acid alignments of the conserved domain trihelix in BnSIP1-1 with orthologous sequences from B. rapa (accession No. XP_009116124), Eutrema salsugineum (accession No. XP_006403581.1) and Arabidopsis thaliana ASIL1 (accession No. NP_564648.1). The conserved tryptophan (or isoleucine) in each helix is indicated by the boxes. The asterisks denote the conserved amino acids.