NUBP2_DROWI
ID NUBP2_DROWI Reviewed; 261 AA.
AC B4N4D9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP2 homolog {ECO:0000255|HAMAP-Rule:MF_03039};
GN ORFNames=GK12055;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC assembly (CIA) machinery. Required for maturation of extramitochondrial
CC Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold
CC complex, mediating the de novo assembly of an Fe-S cluster and its
CC transfer to target apoproteins. {ECO:0000255|HAMAP-Rule:MF_03039}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03039};
CC Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable
CC clusters in the N-termini of NUBP1 and two labile, bridging clusters
CC between subunits of the NUBP1-NUBP2 heterotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_03039};
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains.
CC {ECO:0000255|HAMAP-Rule:MF_03039}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03039}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP2/CFD1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03039}.
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DR EMBL; CH964095; EDW79013.1; -; Genomic_DNA.
DR RefSeq; XP_002068027.1; XM_002067991.2.
DR AlphaFoldDB; B4N4D9; -.
DR SMR; B4N4D9; -.
DR STRING; 7260.FBpp0241198; -.
DR EnsemblMetazoa; FBtr0242706; FBpp0241198; FBgn0214066.
DR GeneID; 6645503; -.
DR KEGG; dwi:6645503; -.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; B4N4D9; -.
DR OMA; QGWVPVY; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; B4N4D9; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03039; NUBP2; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264; PTHR23264; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..261
FT /note="Cytosolic Fe-S cluster assembly factor NUBP2
FT homolog"
FT /id="PRO_0000382718"
FT BINDING 14..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT BINDING 188
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
SQ SEQUENCE 261 AA; 28055 MW; 4614CB29C1D0BD41 CRC64;
MLDKVKNVIV VLSGKGGVGK STVSTQLALA LRHTGHKVGL LDIDLCGPSV PYLLGLEGSD
IYQCDDGWVP IYTDESKTLA VMSIGFLLKS RTDPVIWRGP KKTMMIKQFL QDVKWDELDY
LIIDTPPGTS DEHITVMECL REVPCNGAII VTTPQGVALD DVRKEITFCK KTGIKLLGIV
ENMSGFVCPH CTTCTNIFSS NGGIELANLA QIPHLGTLPI DPRVGILAGT TASVLSELPE
SSTAEVLKGL VQHLDTLTAQ G