<p>Proteins were aligned by MUSCLE [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0193667#pone.0193667.ref021" target="_blank">21</a>] and the alignment optimized in Jalview [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0193667#pone.0193667.ref022" target="_blank">22</a>]. The aligned sequences from top to bottom with their accession numbers are: ScUGPase-1 from <i>Saccharum</i> spp—sugarcane (A0A075E2Q1); AtUGPase from <i>Arabidopsis thaliana</i> (Q9M9P3); StUGPase from <i>Solanum tuberosum–</i>potato (P19595); SbUGPase from <i>Sorghum bicolor</i> (C5XSC5); HvUGPase from <i>Hordeum vulgare</i>–barley (Q43772); OsUGPase from <i>Oryza sativa–</i>rice (Q93X08); ZmUGPase from <i>Zea mays–</i>maize (B6T4R3); bUGPase from bovine–<i>Bos taurus</i> (Q07130); mUGPase from mouse–<i>Mus musculus</i> (Q91ZJ5-2); hUGPase from human–<i>Homo sapiens</i> (Q16851-2) and yUGPase from yeast–<i>Saccharomyces cerevisiae</i> (P32861). Region coloured in green corresponds to the residues in the C-terminal region involved in the end-to-end interactions in the yeast and human orthologs. Black asterisks (<b>*</b>) indicate the residues important for ligand binding, and red asterisks (<b>*</b>) indicate residues involved in the dimer interface in the crystal of ScUGPase-1. Elements of secondary structure are shown based on the crystal structure of ScUGPase-1. β-sheets and α-helices are shown in green and red, respectively.</p
