UniProt ID: A0A0R4I9D1 |
FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. {ECO:0000256|HAMAP-Rule:MF_03038}. COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000256|HAMAP-Rule:MF_03038}; Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer. {ECO:0000256|HAMAP- Rule:MF_03038}; SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. {ECO:0000256|HAMAP-Rule:MF_03038}. SUBCELLULAR LOCATION: Cell projection {ECO:0000256|ARBA:ARBA00004316}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03038}. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily. {ECO:0000256|HAMAP-Rule:MF_03038}. |
UniProt ID: Q6P298 |
FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nubp1-nubp2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. {ECO:0000255|HAMAP-Rule:MF_03038}. COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_03038}; Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nubp1 and two labile, bridging clusters between subunits of the nubp1-nubp2 heterotetramer. {ECO:0000255|HAMAP- Rule:MF_03038}; SUBUNIT: Heterotetramer of 2 nubp1 and 2 nubp2 chains. {ECO:0000255|HAMAP-Rule:MF_03038}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038}. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |