LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | 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 localized 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. In normal (reducing) cytosolic conditions, four conserved Cys residues are coordinated by a Zn ion. Hsp33 is homodimeric in its functional form [, , , ].This superfamily represents a helix hairpin bin domain found in Hsp33. This domain folds into three helices that pack on the other subunit of the Hsp33 dimer [ ]. |
| Short Name | Hsp33_helix_hairpin_bin_dom_sf |
