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. 2018 Apr 11;9:339. doi: 10.3389/fphys.2018.00339

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Copyright © 2018 Durant and Donini.

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) and the copyright owner 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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Amino acid sequence alignment of AeAmt2 and selected members of the Amt/MEP/Rh family. A. aegypti AeAmt2 is labeled in red, and predicted transmembrane helices from 1 to 11 beginning at residue 54 are indicated by the red lines (VectorBase). Sequence number according to LeAMT1-2 of L. esculentum is indicated, and 577 (out of 585 total) amino acid residues for AeAmt2 are shown. Highly conserved residues are highlighted in yellow, mostly conserved residues (7 out of 8 members have conserved amino acid residues) are highlighted in blue, highly conserved sequences in Amt/MEP proteins but not metazoan Rh proteins are highlighted in green, and conserved residues between AeAmt1 and AeAmt2 in A. aegypti that are different to the conserved residues in the other members are highlighted in black. Species names corresponding to amino acid sequences of ammonia transporters are as follows (in parentheses): AeAmt2 (A. aegypti), AeAmt1 (A. aegypti), AmtB (E. coli), AMT1-1 (A. thaliana), MEP1 (S. cerevisiae), Le-AMT1-2 (L. esculentum), AeRh50-1 (A. aegypti), and AeRh50-2 (A. aegypti). The alignment was constructed using the ClustalW algorithm.