Mrp/NBP35 ATP-binding protein (IPR019591)

Short name: Mrp/NBP35_ATP-bd

Overlapping homologous superfamilies

Family relationships


This entry contains cytosolic Fe-S cluster assembling factors NBP35 and CFD1. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Nucleotide binding and hydrolysis seems to be critical for loading of Fe-S clusters onto CFD1 and NBP35 [PMID: 15728363, PMID: 15667273, PMID: 15660135]. In higher eukaryotes NBP35 and CFD1 are known as NUBP1 and NUBP2, and NUBP1 is also involved in iron regulation [PMID: 18573874].

Bacterial homologues ApbC and MRP (Multiple Resistance and pH adaptation in E. coli) have been shown to contain an ATP-binding domain at the N terminus and have ATPase activity. MRP is a membrane-spanning protein and functions as a Na+/H+ antiporter [PMID: 10198001, PMID: 15601724]. Archaeal homologues function as iron-sulfur cluster carriers [PMID: 19114487].

Contributing signatures

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