ID A0A3Q7R2Z6_VULVU Unreviewed; 271 AA.
AC A0A3Q7R2Z6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP2 {ECO:0000256|HAMAP-Rule:MF_03039};
DE AltName: Full=Nucleotide-binding protein 2 {ECO:0000256|HAMAP-Rule:MF_03039};
DE Short=NBP 2 {ECO:0000256|HAMAP-Rule:MF_03039};
GN Name=NUBP2 {ECO:0000256|HAMAP-Rule:MF_03039,
GN ECO:0000313|RefSeq:XP_025840654.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025840654.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025840654.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025840654.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025840654.1};
RG RefSeq;
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. {ECO:0000256|HAMAP-Rule:MF_03039}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_03039};
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts with
CC KIFC1. {ECO:0000256|HAMAP-Rule:MF_03039}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03039}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000256|HAMAP-
CC Rule:MF_03039}. Note=Enriched at the centrosomes during mitosis.
CC {ECO:0000256|HAMAP-Rule:MF_03039}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP2/CFD1 subfamily. {ECO:0000256|HAMAP-Rule:MF_03039}.
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DR RefSeq; XP_025840654.1; XM_025984869.1.
DR AlphaFoldDB; A0A3Q7R2Z6; -.
DR STRING; 9627.ENSVVUP00000013565; -.
DR KEGG; vvp:112909077; -.
DR OrthoDB; 228512at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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 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_03039; NUBP2; 1.
DR InterPro; IPR000808; Mrp-like_CS.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264:SF38; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP2; 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_03039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03039};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03039};
KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03039};
KW Iron {ECO:0000256|HAMAP-Rule:MF_03039};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03039};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03039}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03039};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03039"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03039"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03039"
SQ SEQUENCE 271 AA; 28646 MW; 68EE0F383DBA77FE CRC64;
MGTAAGPGNL AGVRHILLVL SGKGGVGKST ISTELALALR HAGKKVGILD VDLCGPSIPR
MLRAQGRAVH QCDGGWVPVF VDQEQSISLM SVGFLLENPD EALVWRGPKK NALIKQFVSD
VAWGQLDYLV VDTPPGTSDE HMATVDALRP YSPLGALVVT TPQAVSVGDV RRELTFCRKT
GLQVLGVVEN MSGFVCPHCA ECTNVFSRGG GEELATLAGV PFLGSVPLDP ELCGSLEEGR
DFIRDFPKSS AFPALFSIAQ KVLSQAPARL S
//
