ID   NUBP1_DROWI             Reviewed;         310 AA.
AC   B4N1C3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 homolog {ECO:0000255|HAMAP-Rule:MF_03038};
GN   ORFNames=GK24826;
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_03038}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03038};
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_03038};
CC   -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains.
CC       {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}.
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DR   EMBL; CH963920; EDW78113.1; -; Genomic_DNA.
DR   RefSeq; XP_002067127.1; XM_002067091.1.
DR   AlphaFoldDB; B4N1C3; -.
DR   SMR; B4N1C3; -.
DR   STRING; 7260.FBpp0253969; -.
DR   EnsemblMetazoa; FBtr0255477; FBpp0253969; FBgn0226785.
DR   GeneID; 6643753; -.
DR   KEGG; dwi:6643753; -.
DR   eggNOG; KOG3022; Eukaryota.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   InParanoid; B4N1C3; -.
DR   OMA; QHITFKD; -.
DR   OrthoDB; 1166096at2759; -.
DR   PhylomeDB; B4N1C3; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0051536; F:iron-sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   HAMAP; MF_03038; NUBP1; 1.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR028601; NUBP1/Nbp35.
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.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..310
FT                   /note="Cytosolic Fe-S cluster assembly factor NUBP1
FT                   homolog"
FT                   /id="PRO_0000382611"
FT   BINDING         8
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         22
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         25
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         31
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         239
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         242
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
SQ   SEQUENCE   310 AA;  32828 MW;  6CC7623457ADC470 CRC64;
     MEAPPEHCPG VESEQAGRVS ACAGCPNQSI CSDPNKKLED PGKALVAAAL KDVKHKLLIL
     SGKGGVGKST VTTLLTRYLA RSCPDNNFGV LDIDICGPSQ PRLLGAVGEN VHQSGSGWSP
     VGIDDNVCLM SIGFLLGSVD DAIIWRGPKK NGMIRQFLSE VDWGNLDLLL LDTPPGTSDE
     HLSVVSYLKN DEIPNSVRAI IVTTPQEVAL LDVRKEINFC KKQGIPIVGV VENMSSFRCG
     HCGNSSEIFP AKTGGAAAMC TEMEVPLLGS LPLDPLIAKA CDSGEDITAM KNPTTEALAA
     ICTRIMDSFN