ID A0A1A6HD01_NEOLE Unreviewed; 271 AA.
AC A0A1A6HD01;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=A6R68_17103 {ECO:0000313|EMBL:OBS76443.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS76443.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS76443.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS76443.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS76443.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS76443.1}.
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DR EMBL; LZPO01034908; OBS76443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6HD01; -.
DR STRING; 56216.A0A1A6HD01; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
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:UP000092124}.
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; 29013 MW; 91B8E1F3FA49937F CRC64;
MEAVAEPGNL ADVRNIILVL SGKGGVGKST ISTELALALR HQGKKVGILD VDLCGPSIPH
MLRAQGKAVH QCDHGWVPVF VDQEQSISLM SVGFLLENPD EAVVWRGPKK HALIKQFVSD
VAWGELDYLV VDTPPGTSDE HMATVEALRP YGPLGALVVT TPQAVSVGDV RRELTFCRKT
GLQVIGLIEN MSGFACPHCA ECTNVFSKGG GEELAQLAGV PFLGSVPLDP QLTRSLEEGR
DFIQEFPKSA AYSALSSIAQ KVLHRMPALL S
//
