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. 2018 Jul 21;75(23):4341–4356. doi: 10.1007/s00018-018-2875-z

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© The Author(s) 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Fig. 1 — Drosophila melanogaster Hsp67Bc is a highly conserved member of the sHSP family and is related to the vertebrate HSPB8. Protein sequence alignment of Drosophila melanogaster (D.m._Hsp67BC), zebrafish (D.r._HSPB8), Xenopus laevis (X.l._HSPB8), mouse (M.m_HSPB8), and human HSPB8 (H.s._HSPB8) proteins. Conserved functional domain and amino acid residues (hot-spots) are highlighted by boxes: alpha-crystallin domain (ACD)—transparent with green frame, arginine 126 (R126) in D. melanogaster Hsp67Bc and lysine (K141) in human HSPB8—red with black frame. Consensus symbols in a sequence alignment have the following meaning: an asterisk (*) indicates a position which has a single, fully conserved residue, a colon (:) indicates conservation between groups of strongly similar properties, and a period (.) indicates conservation between groups of weakly similar properties. Sequence alignment: ClustalW2, http://www.ebi.ac.uk