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Database: UniProt
Entry: G3W2D6_SARHA
LinkDB: G3W2D6_SARHA
Original site: G3W2D6_SARHA 
ID   G3W2D6_SARHA            Unreviewed;       320 AA.
AC   G3W2D6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 {ECO:0000256|HAMAP-Rule:MF_03038};
DE   AltName: Full=Nucleotide-binding protein 1 {ECO:0000256|HAMAP-Rule:MF_03038};
DE            Short=NBP 1 {ECO:0000256|HAMAP-Rule:MF_03038};
GN   Name=NUBP1 {ECO:0000256|HAMAP-Rule:MF_03038,
GN   ECO:0000313|Ensembl:ENSSHAP00000009591.1};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000009591.1, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000009591.1, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000009591.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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. Implicated in the regulation of
CC       centrosome duplication. {ECO:0000256|HAMAP-Rule:MF_03038}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_03038};
CC   -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts with
CC       KIFC1. {ECO:0000256|HAMAP-Rule:MF_03038}.
CC   -!- SUBCELLULAR LOCATION: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
CC       Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03038}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       NUBP1/NBP35 subfamily. {ECO:0000256|HAMAP-Rule:MF_03038}.
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DR   RefSeq; XP_003761753.1; XM_003761705.2.
DR   AlphaFoldDB; G3W2D6; -.
DR   STRING; 9305.ENSSHAP00000009591; -.
DR   Ensembl; ENSSHAT00000009675.2; ENSSHAP00000009591.1; ENSSHAG00000008299.2.
DR   GeneID; 100918184; -.
DR   KEGG; shr:100918184; -.
DR   CTD; 4682; -.
DR   eggNOG; KOG3022; Eukaryota.
DR   GeneTree; ENSGT00950000183193; -.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   InParanoid; G3W2D6; -.
DR   OMA; QIFKPTT; -.
DR   OrthoDB; 228512at2759; -.
DR   TreeFam; TF300755; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:0051642; P:centrosome localization; IEA:Ensembl.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0010826; P:negative regulation of centrosome duplication; IEA:Ensembl.
DR   GO; GO:0072697; P:protein localization to cell cortex; IEA:Ensembl.
DR   GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR   CDD; cd02037; Mrp_NBP35; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   HAMAP; MF_03038; NUBP1; 1.
DR   InterPro; IPR000808; Mrp-like_CS.
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:SF19; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP1; 1.
DR   PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_03038};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_03038};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03038};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_03038};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03038};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03038}; Reference proteome {ECO:0000313|Proteomes:UP000007648}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03038"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT   BINDING         235
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:0000256|HAMAP-Rule:MF_03038"
FT   BINDING         238
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:0000256|HAMAP-Rule:MF_03038"
SQ   SEQUENCE   320 AA;  34414 MW;  AF62A7310247C8BB CRC64;
     MEEVPQDCPG TSSTQAGKGA SCQGCPNQRL CASGAGAAPD PAIEEIKEKM RTVKHKILVL
     SGKGGVGKST FSAHLAHGLA EDESKQVALL DIDICGPSIP KMMGLEGEQV HQSGSGWSPV
     YVEENLGVMS VGFLLGSLDD AVIWRGPKKN GMIKQFLRDV DWGEIDYLIV DTPPGTSDEH
     LSIVQYLSAA HIDGAVIITT PQEVSLQDVR KEINFCHKVK LPIIGVVENM SGFICPKCKN
     ESQIFPPTTG GAEVMCQDLK VSLLGKVPLD PQIGKSCDKG QSFLTEVPDS PATLAYRNII
     QRIQDFCDIH SSKEEKLISC
//
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