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. 2013 Feb 8;14(2):3786–3801. doi: 10.3390/ijms14023786

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© 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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(A) Domain architecture of R2d2 in A. glycines. Both DS_RBD1 and DS_RBD2 domains are indicated; (B) and (C) Multiple sequence alignment of DS_RBD1 (B) and DS_RBD2 (C) domain sequences from insect R2d2 proteins. The conserved and similar amino acid residues are labeled in black and grey backgrounds respectively. The figures in the parentheses indicate the percent identity to the respective domain of AyR2d2. R2d2 proteins were from Acyrthosiphon pisum (Ap), Aphis glycines (Ay), Apis mellifera (Am), Bombyx mori (Bm), Drosophila melanogaster (Dm), and Tribolium castaneum (Tc).