| Type: | Domain | Name: | Ferritin-like superfamily |
| 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 []. 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 []. 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 []. The superfamily also includes the alpha and beta subunits of methane monooxygenase hydrolase, delta 9-stearoyl-acyl carrier protein desaturase and manganese catalase. | Short Name: | Ferritin-like_SF |
| DB identifier | Type | Name |
|---|---|---|
| IPR008434 | Family | Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase |
| IPR011566 | Family | Ubiquinone biosynthesis protein Coq7 |
| IPR011971 | Family | Conserved hypothetical protein CHP02284 |
| IPR010386 | Family | tRNA-hydroxylase MiaE |
| IPR017022 | Family | Uncharacterised conserved protein UCP033860 |
| IPR017635 | Family | Benzoyl-CoA oxygenase, B subunit |
