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. 2021 Jul 9;12:699756. doi: 10.3389/fpls.2021.699756

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Copyright © 2021 Zhang, Xia and Zhu.

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 alignment of carboxy-terminal Hsp70-interacting protein (CHIP) ubiquitin E3 ligase proteins from human and plants. The accession numbers of the CHIP proteins used in the alignment are: HsCHIP from Homo sapiens (AAD33400); CrCHIP from Chlamydomonas reinhardtii (Cre.11g479650.t1.2); SmCHIP from Selaginella moellendorffii (Selaginella74711); PpCHIP1 and PpCHIP2 from Physcomitrium patens (Pp3c14_2850V3.7 and Pp3c10_2570V3.5, respectively); OsCHIP from Oryza sativa (LOC_Os05g01460.1); SlCHIP from Solanum lycopersicum (Solyc06g083150.2.1); and AtCHIP from Arabidopsis thaliana (AT3G07370.1). Identical amino acid residues are indicated in green. Highly similar amino acid residues are indicated in pink. The N-terminal tetratricopeptide repeat (TPR) motifs and the C-terminal B-box domain are also indicated.