v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | This superfamily represents the C-terminal alpha/beta domain from the heat shock protein Hsp33. 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. Oxidizing conditions like H 2O 2cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function [ ]. |
| Short Name | Heat_shock_Hsp33_C |