pfam01430: HSP33 (This model is not part of the current CDD release)
Hsp33 protein
Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localised protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidising conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.
Jiyao W et al.(2023). "The conserved domain database in 2023.",