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NUBP1_DROMO
ID   NUBP1_DROMO             Reviewed;         310 AA.
AC   B4KHX1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 homolog {ECO:0000255|HAMAP-Rule:MF_03038};
GN   ORFNames=GI17051;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22;
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; CH933807; EDW11253.1; -; Genomic_DNA.
DR   RefSeq; XP_002001811.1; XM_002001775.2.
DR   AlphaFoldDB; B4KHX1; -.
DR   SMR; B4KHX1; -.
DR   STRING; 7230.FBpp0166268; -.
DR   EnsemblMetazoa; FBtr0167776; FBpp0166268; FBgn0139796.
DR   GeneID; 6575807; -.
DR   KEGG; dmo:Dmoj_GI17051; -.
DR   eggNOG; KOG3022; Eukaryota.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   InParanoid; B4KHX1; -.
DR   OMA; QHITFKD; -.
DR   OrthoDB; 1166096at2759; -.
DR   PhylomeDB; B4KHX1; -.
DR   Proteomes; UP000009192; 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_0000382605"
FT   BINDING         9
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         23
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         26
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         32
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         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         240
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         243
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;  32822 MW;  85B6A3E65B1A84C1 CRC64;
     MQAPPPEHCP GVESEQAGLV SACAGCPNQR ICSDPNKKLE DPGKALVAAA MKDVKHKLLI
     LSGKGGVGKS TVTTLLTRYL ARSYPDSNFG VLDIDICGPS QPRLLGAVGE NVHQSGSGWS
     PVGIDDNVCL MSIGFLLGSV DDAIIWRGPK KNGMIRQFLS EVDWGTLDLL LLDTPPGTSD
     EHLSVVSYLR DDSAPDSLKA IIVTTPQEVA LLDVRKEINF CKKQRIPIVG VVENMSSFRC
     GNCGNSSEIF PAKTGGAAAM CQEMDVPLLG SLPLDPQVTR ACDSGEDITA INNSTTEALA
     TICSKIMASL
 
 
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