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. 2020 Feb 4;11:7. doi: 10.3389/fpls.2020.00007

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Copyright © 2020 Davies, Jibran, Zhou, Albert, Brummell, Jordan, Bowman and Schwinn

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(s) 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 features of polyphenol oxidases (PPOs) in Marchantia polymorpha. (A) Number of expressed PPO gene models found and their PPO type. RNA-seq data from Berland et al. (2019) were used to check for expression. The top structure (not to scale) is standard for plant PPOs. Transit/signal peptide (P), copper binding domain TYR : PFAM 00264 (CuA/CuB), PPO1_DWL: PFAM 12142 domain (DWL), tyrosine motif (YxY), PPO1_KFDV : PFAM12143 domain (KFDV). (B) Weblogo display of conserved residues of DWL and KFDV domains based on all gene models having an intact region (generated using https://weblogo.berkeley.edu/logo.cgi). DWL, tyrosine, and KFDV core motifs are underlined in black. Residues for the regions identified by Tran et al. (2012) with core motifs of EEEVLV (left) and EFAGSF (right) are underlined in blue.