ZnF_CDGSHCDGSH-type zinc finger. Function unknown.
|SMART accession number:||SM00704|
|Interpro abstract (IPR006622):|
This entry represents iron-sulphur domain containing proteins that have a CDGSH sequence motif (although the Ser residue can also be an Ala or Thr), and is found in proteins from a wide range of organisms with the exception of fungi. The CDGSH-type domain binds a redox-active pH-labile 2Fe-2S cluster. The conserved sequence C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H is a defining feature of this family [(PUBMED:17376863)].
CDGSH-type domains are found in mitoNEET, an iron-containing integral protein of the outer mitochondrian membrane (OMM). MitoNEET forms a dimeric structure with a NEET fold, and contains two domains: a beta-cap region and a cluster-binding domain that coordinated two acid-labile 2Fe-2S clusters (one bound to each protomer) [(PUBMED: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, (IPR019610) [(PUBMED:17584744), (PUBMED:17766440)]. The whole protein regulates oxidative capacity and may function in electron transfer, for instance in redox reactions with metabolic intermediates, cofactors and/or proteins localized at the OMM.
|GO component:||intracellular membrane-bounded organelle (GO:0043231)|
|GO function:||2 iron, 2 sulfur cluster binding (GO:0051537)|
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- Evolution (species in which this domain is found)
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