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. 2016 Oct 25;7:1590. doi: 10.3389/fpls.2016.01590

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Copyright © 2016 Van Holle, Smagghe and Van Damme.

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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(A) Domain architecture of the Nictaba-like homologs from soybean under study: NLL1 (Glyma.06G221100) and NLL2 (Glyma.20G020900) (B) Sequence alignment of the trimmed Nictaba sequence and the Nictaba domains of NLL1 and NLL2 (NLL2.1: domain one, NLL2.2: domain two) from soybean using ClustalO. The conserved Trp-residues important for the carbohydrate-binding activity of Nictaba are marked in bold and the proposed nuclear localization signal of Nictaba is underlined. ‘*’indicates fully conserved amino acid residue; ‘:’designates conserved amino acid substitution (indicating conservation between groups of strongly similar properties); ‘.’designates semi-conserved amino acid substitution (indicating conservation between groups of weakly similar properties).