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. 2016 Sep 30;3:63. doi: 10.3389/fmolb.2016.00063

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Copyright © 2016 Ruggieri, Saredi, Zanotti, Pasanisi, Maggi and Mora.

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) or licensor 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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The DNAJ protein family. Based on their structure, DNAJs are divided into three subtypes. Type I, or A, has an N-terminal J domain (with a conserved histidine, proline, and aspartic acid tripeptide), followed by a glycine/phenylalanine-rich domain (G/F), by a zinc finger region rich in cysteine, and by a C-terminal domain, responsible for client binding and presenting two barrel domains, CTDI and CDTII. Type II, or B, is similar to type I, but lacks the zinc finger region. Type III, or C, has only the conserved J domain which is variably located in the protein (Fan et al., 2003).