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. 2018 Jul 3;9:896. doi: 10.3389/fpls.2018.00896

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Copyright © 2018 Wang, Sun, Pei, Li, Zhang, Li and Hou.

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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Alignment of conserved domains of GhSNAP33 and other SNAP25-type t-SNARE proteins. HsSNAP25a (AAH10647.1) from Homo sapiens, OsSNAP32 (AAW82752.1) from Oryza sativa, HvSNAP34 (AAP79417.1) from Hordeum vulgare, AtSNAP33 (Q9S7P9.1) from Arabidopsis thaliana, CkSNAP33 (KR011961) from Cynanchum komarovii and GsSNAP33 from Glycine soja. Conserved and similar residues are shaded in black and gray, respectively. The well conserved heptad repeat layers –7 to +8 are indicated. The four cysteine residues involved in palmitoylation of SNAP25 are indicated using arrow. The asterisks (^∗) and dots (.) under the sequence are indicated the completely conserved and highly conserved amino acids, respectively. Multiple amino acid sequence analyses were performed using Clustal Omega and the multiple alignment file was shaded using the BoxShade program.