Ferritin-like diiron domain (IPR009040)

Short name: Ferritin-like_diiron

Overlapping homologous superfamilies

Domain relationships



This entry represents a group of proteins, containing ferritin-like domain, which is an about 145-residue domain made of a four-helix bundle surrounding a non-heme, non-sulphur, oxo-bridged diiron site. The diiron site is contained within a twisted, left-handed four- helix-bundle constituted of two anti-parallel helix pairs connected through a left-handed crossover connection. Known ligand residues at non-heme, non- sulphur diiron sites in proteins include His, Asp, Glu, and Tyr. Proteins containing a ferritin-like diiron domain possess the ability to catalyze oxidation of Fe2+ to Fe2+ by O2, i.e. ferroxidase activity. The ferritin- like diiron domain occurs in stand-alone form in ferritin and bacterioferritin or in association with the rubredoxin-like domain in rubrerythrin [PMID: 8646540]. Proteins known to contain a ferritin-like diiron domain are listed below:

  • Ferritin (Ftn), an eukaryotic intracellular protein that stores iron in a soluble, nontoxic, readily available form.
  • Bacterioferritin (Bfr), a prokaryotic protein which may perform functions in iron detoxification and storage.
  • Rubrerythrin (Rr), a non-heme protein isolated from anaerobic sulphate- reducing bacteria.
  • Nigerythrin (Nr), a prokaryotic protein of unknown function.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles