InterPro : IPR009040

Name  Ferritin- like diiron domain Short Name  Ferritin-like_diiron
Type  Domain Description  This entry represents a group of proteins, containing ferritin-like domain, which is an about 145-residue domain made of a four-helixbundle 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 aleft-handed crossover connection. Known ligand residues at non-heme, non-sulphur diiron sites in proteins include His, Asp, Glu, and Tyr. Proteinscontaining a ferritin-like diiron domain possess the ability to catalyzeoxidation of Fe2+to Fe2+by O2, i.e. ferroxidase activity. The ferritin-like diiron domain occurs in stand-alone form in ferritin and bacterioferritinor in association with the rubredoxin-like domain inrubrerythrin [].Proteins known to contain a ferritin-like diiron domain are listed below: Ferritin (Ftn), an eukaryotic intracellular protein that stores iron in asoluble, nontoxic, readily available form.Bacterioferritin (Bfr), a prokaryotic protein which may perform functionsin iron detoxification and storage.Rubrerythrin (Rr), a non-heme protein isolated from anaerobic sulphate-reducing bacteria.Nigerythrin (Nr), a prokaryotic protein of unknown function.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

3 Contains

Id Name Short Name Type
IPR012347 Ferritin-related Ferritin-rel Domain
IPR014034 Ferritin, conserved site Ferritin_CS Conserved_site
IPR003251 Rubrerythrin Rubrerythrin Domain

3 Found In

Id Name Short Name Type
IPR008331 Ferritin/DPS protein domain Ferritin_DPS_dom Domain
IPR002024 Bacterioferritin Bacterioferritin Family
IPR014490 Uncharacterised conserved protein UCP018063, ferritin fold UCP018063_ferrtn Family

0 Parent Features

1 Publications

First Author Title Year Journal Volume Pages
deMaré F The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains. 1996 Nat Struct Biol 3 539-46

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)