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. 2019 Apr 16;10(1):292–314. doi: 10.1080/21505594.2019.1598172

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© 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Sequences of Pex13 homologs and Pex14 homologs in fungal species. (a-b) The putative protein sequences of Pex13 and Pex14 homologs, Anpex13 (XP_659115) and Anpex14 (CBF76374.1) from Aspergillus nidulans, Copex13 (ENH77396.1) and Copex14 (ENH79683.1) from Colletotrichum orbiculare, Fgpex13 (XP_011316361) and Fgpex14 (XP_011328505.1) from Fusarium graminearum, Mopex13 (XP_003718970.1) and Mopex14 (XP_003717914.1) from Magnaporthe oryzae, Ncpex13 (XP_965021.3) and Ncpex14 (XP_957540.1) from Neurospora crassa, and Scpex13 (KZV09435.1) and Scpex14 (KZV11075.1) from Saccharomyces cerevisiae were retrieved and aligned using ClustalX. Identical amino acids are highlighted against a black background, conserved residues against a dark gray background, and similar residues against a light gray background. The putative conserved transmembrane domain 1 (TMD1) and 2 (TMD2) domain and SH3 domain in the Pex13 proteins are underlined in blue. The putative hydrophobic region and coiled-coil structure in the Pex14 proteins are underlined in red. The phylogenetic relationships of the Pex13 homologs (c) and the Pex14 homologs (d) respectively were calculated using the neighbor joining method in the MEGA 6.0 software.