cd01041: rubrerythrin-like (This model is not part of the current CDD release)
ferritin-like diiron-binding domain found in the rubrerythrin-like family proteins
Rubrerythrin-like proteins are members of the ferritin-like diiron-carboxylate protein superfamily and comprise a diverse group of non-heme iron proteins involved in cellular redox processes and protection against oxidative stress. Members contain a conserved ferritin-like four-helix bundle that coordinates a dinuclear non-heme iron center, while some subfamilies also possess a rubredoxin-like domain containing a mononuclear Fe(Cys)4 center. This family includes classical rubrerythrins, nigerythrins, reverse rubrerythrins (rubperoxins), symerythrins, and sulerythrins, which differ in domain organization and metal coordination but share a common ferritin-like structural core. Many characterized members function as peroxide reductases or participate in peroxide detoxification, although the physiological roles of some subfamilies remain incompletely understood.
Feature 1:dinuclear metal center [ion binding site]
Evidence:
Comment:The diiron site resembles those found in O2-activating diiron enzymes
Comment:Rubrerythrin appears to be able to change the ligand arrangements of one of its binding sites to bind different metals under different conditions.
Structure:1LKO; Desulfovibrio vulgaris Rubrerythrin binds two iron atoms [diferric (oxidized) Rubrerythrin]
Jiyao W et al.(2023). "The conserved domain database in 2023.",