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. 2012 Oct 25;8(10):1323–1334. doi: 10.7150/ijbs.4189

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© Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.

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Nucleotide and deduced amino acid sequences of AyCHS cDNA from Aphis glycines. The start codon (ATG), stop codon (TGA) and putative polyadenylation signal (AATAAA) are highlighted in black. The 16 hydrophobic, membrane-spanning α-helices predicted by TMHMM Server v. 2.0 are highlighted in gray. The amino acid sequence of the putative catalytic domain predicted by SMART tool ²⁸ is boxed. The 12 putative N-glycosylation sites predicted by PROSCAN are underlined. The cDNA sequence was deposited in the GenBank with accession number JQ246352.

Nucleotide and deduced amino acid sequences of AyCHS cDNA from Aphis glycines. The start codon (ATG), stop codon (TGA) and putative polyadenylation signal (AATAAA) are highlighted in black. The 16 hydrophobic, membrane-spanning α-helices predicted by TMHMM Server v. 2.0 are highlighted in gray. The amino acid sequence of the putative catalytic domain predicted by SMART tool ²⁸ is boxed. The 12 putative N-glycosylation sites predicted by PROSCAN are underlined. The cDNA sequence was deposited in the GenBank with accession number JQ246352.