This entry represents the TRX domain found in DNAJC16. DNAJC16 contains an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network [].
