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. 2019 May 21;10:610. doi: 10.3389/fpls.2019.00610

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Copyright © 2019 Zhang, Burel, Plasson, Kiefer-Meyer, Ovide, Gügi, Wan, Teo, Mak, Song, Driouich, Lerouge and Bardor.

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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Phaeodactylum tricornutum putative FuT exhibits strong amino acid identities with α(1,3)-fucosyltransferases. Amino acids sequences comparison with the T-coffee program (http://tcoffee.crg.cat/, Di Tommaso et al., 2011) of the C-terminal GT10 domains of the three putative fucosyltransferases encoded, respectively, by the Phatr3_J46109, Phatr3_J46110 and Phatr3_J54599 genes from Phaeodactylum tricornutum with biochemically characterized α(1,3)-fucosyltransferases from Arabidopsis thaliana (FUT11_ARATH and FUT12_ARATH), Medicago sativa (Q5DTC8_MEDSA), Oryza sativa (Q6ZDE5_ORYSJ), Zea mays Q0VH31_MAIZE), Vigna radiata (Q9ST51_VIGRR), Physcomitrella patens (Q8L5D1_PHYPA), Drosophila melanogaster (FUCTA_DROME), Caenorhabditis elegans (G5EDR5_CAEEL), Apis mellifera (Q05GU3_APICA) and Bombyx mori (H9JL25_BOMMO). The graphic output reflects the level of consistency of the alignment of a considered residue (from blue/green: badly or poorly supported to pink which corresponds to strongly supported). Conserved motifs of the GT10 domain are indicated on the top of the alignment.