Domain

Ferritin-like superfamily (IPR009078)

Short name: Ferritin-like_SF

Domain relationships

Description

Ferritin is one of the major non-haem iron storage proteins in animals, plants, and microorganisms. It is a multisubunit protein with a hollow interior, which contains a mineral core of hydrated ferric oxide, thereby ensuring its solubility in an aqueous environment [PMID: 9668036]. Each subunit consists of a closed, four-helical bundle with a left-handed twist and one crossover connection.

This entry represents the ferritin-like superfamily. Proteins with this structure include ferritin and other ferritin-like proteins such as bacterioferritin (cytochrome b1) that binds haem between two subunits, non-haem ferritin, dodecameric ferritin homologue (DPS) that binds to and protects DNA, and the N-terminal domain of rubrerythrin that is found in many air-sensitive bacteria and archaea [PMID: 12175244]. In addition, ribonucleotide reductase-like proteins show a similar structure to the ferritin-like fold; these di-iron carboxylate proteins constitute a diverse class of non-haem iron enzymes performing a multitude of redox reactions [PMID: 11315567]. The superfamily also includes the alpha and beta subunits of methane monooxygenase hydrolase, delta 9-stearoyl-acyl carrier protein desaturase and manganese catalase.

Contributing signatures

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