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. 2016 Jan 8;6:1228. doi: 10.3389/fpls.2015.01228

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Copyright © 2016 Teng, Chen and Xiao.

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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Characterization of deduced amino acid sequence of cloned cDNA. The amino acid sequences identical to the peptide fragments determined by nano-LC-MS/MS were underlined. The conserved catalase catalytic amino acid residues (active site), 65-H (His), 104-S (Ser), and 138-N (Asn), were white and black-marked. The distal heme binding domain [64-V (Val), 102-R (Arg), 105-T (Thr), 143-F (Phe), and 151-F] and proximal heme binding domain [326-P (Pro), 344-R, and 348-Y (Tyr)] were gray-marked. A putative conserved internal peroxisomal targeting signal (PTM) was in white and black at the C-terminal [490-P, 491-T, and 492-M (Met)]. The stop signal was represented by “Stop”. The sequence has been deposited in GenBank as Accession No. KP710221.