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. 2019 Dec 18;10:2953. doi: 10.3389/fimmu.2019.02953

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Copyright © 2019 Li, Wei, Zhang, Chi and Yang.

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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Sequence alignment of Ss-Raptor with its homologs from other species. (A) The structure of Raptor protein in rockfish by SMART prediction. (B) Multiple sequence alignment analyses of Heat repeat domain in Raptor. Peptide binding sites are indicated with triangle, and the conservative phosphorylation point is shown in red box. (C) Multiple sequence alignment analyses of phosphorylation sites between Heat repeat domain and WD40 domain of Raptor. The conserved phosphorylation point is shown in red box. The background of the amino acid residues conserved in 80% are shown as dark gray and the similar residues is light red. The selected protein sequences are Homo sapiens (NP_065812.1), Mus musculus (NP_065812.1), Columba livia (PKK18984.1), Chelonia mydas (XP_007056109.1), Xenopus tropicalis (XP_012827010.1), Salmo salar (XP_014032262.1), Danio rerio (XP_021327417.1).