The recently discovered CDGSH iron-sulfur domains (CISDs) are classified into seven major types and are widely distributed throughout the three domains of life PMID:21949752. Members of this superfamily share the structure of the human CISD protein mitoNEET, also designated CSD1, an iron-containing integral protein of the outer mitochondrian membrane (OMM). MitoNEET contains two domains: a beta-cap region and a cluster-binding domain, containing the CDGSH motif, that coordinates two acid-labile 2Fe-2S clusters (one bound to each protomer) PMID:17766440. The CDGSH iron-sulphur domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates, (INTERPRO:IPR019610) PMID:17584744,PMID:17766440. The whole protein regulates oxidative capacity and might be involved in electron transfer.