Home ScanProsite ProRule Documents Downloads Links Funding
	PROSITE documentation PDOC50905 [for PROSITE entry PS50905]

Ferritin-like diiron domain profile

The ferritin-like domain is an about 145-residue domain made of a four-helix bundle surrounding a non-heme, non-sulfur, oxo-bridged diiron site (see <PDB:1RYT>). 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-sulfur diiron sites in proteins include His, Asp, Glu, and Tyr. Proteins containing a ferritin-like diiron domain possess the ability to catalyze oxidation of Fe(2+) to Fe(3+) 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 (see <PDOC50903>) in rubrerythrin [1,2,3].

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 (see <PDOC00181>).
• Bacterioferritin (Bfr), a prokaryotic protein which may perform functions in iron detoxification and storage.
• Rubrerythrin (Rr), a non-heme protein isolated from anaerobic sulfate- reducing bacteria.
• Nigerythrin (Nr), a prokaryotic protein of unknown function.

The profile we developed covers the entire ferritin-like diiron domain.

Last update:

April 2003 / First entry.

PROSITE method (with tools and information) covered by this documentation:

FERRITIN_LIKE, PS50905; Ferritin-like diiron domain profile  (MATRIX)

• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 150
  • detected by PS50905: 148 (true positives)
  • undetected by PS50905: 2 (0 false negative and 2 'partials')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS50905:
  NONE.
• Domain architecture view of Swiss-Prot proteins matching PS50905
  
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS50905
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS50905
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS50905
• View ligand binding statistics of PS50905
• Matching PDB structures: 1AEW 1B71 1BCF 1BFR ... [ALL]

1	Authors	deMare F., Kurtz D.M. Jr., Nordlund P.
	Title	The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains.
	Source	Nat. Struct. Biol. 3:539-546(1996).
	PubMed ID	8646540

2	Authors	Bonomi F., Kurtz D.M. Jr., Cui X.
	Source	J. Biol. Inorg. Chem. 1:67-72(1996).

3	Authors	Kurtz D.M. Jr.
	Source	J. Biol. Inorg. Chem. 2:159-167(1997).

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to

Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)