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. 2018 Jun 15;9:1316. doi: 10.3389/fmicb.2018.01316

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Copyright © 2018 Jain, Wiemann, Thill, Williams, Keller and Kabbage.

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 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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Domain architecture and multiple alignment of Bag proteins. (A) The domain archeture of Arabidopsis thaliana (At) Bag1-7, human (h) Bag1-6, and putative Bag proteins of Aspergillus nidulans, A. fumigatus, and A. flavus are compared. The number of amino acids for each protein are shown under the name. Abbreviations: Bag, Bcl-2 associated athanogene; UBL, Ubiquitin-like domain; CAM, Calmodulin; ER, Endoplasmic reticulum; NLS, Nuclear localization signal. (B) Bag domains of AtBag1-4, hBag1, S. cerevisiae Snl1, and Aspergillus spp. were aligned using ClustalW MSA program. The amino acid residues essential for Hsp70 binding are marked by asterisks “^*”. The predicted secondary structure of A. nidulans BagA BD is shown with three alpha helices (H) highlighted in Red and coil (C) in black.