NBP35_KLULA
ID NBP35_KLULA Reviewed; 326 AA.
AC Q6CMN0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NBP35 {ECO:0000255|HAMAP-Rule:MF_03038};
DE AltName: Full=Nucleotide-binding protein 35 {ECO:0000255|HAMAP-Rule:MF_03038};
GN Name=NBP35 {ECO:0000255|HAMAP-Rule:MF_03038};
GN OrderedLocusNames=KLLA0E19074g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 NBP35-CFD1 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. Required for biogenesis and export of
CC both ribosomal subunits, which may reflect a role in assembly of the
CC Fe/S clusters in RLI1, a protein which performs rRNA processing and
CC ribosome export. {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 NBP35 and two labile, bridging clusters
CC between subunits of the NBP35-CFD1 heterotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_03038};
CC -!- SUBUNIT: Heterotetramer of 2 NBP35 and 2 CFD1 chains.
CC {ECO:0000255|HAMAP-Rule:MF_03038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038}.
CC Nucleus {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; CR382125; CAG99896.1; -; Genomic_DNA.
DR RefSeq; XP_454809.1; XM_454809.1.
DR AlphaFoldDB; Q6CMN0; -.
DR SMR; Q6CMN0; -.
DR STRING; 28985.XP_454809.1; -.
DR EnsemblFungi; CAG99896; CAG99896; KLLA0_E18987g.
DR GeneID; 2893970; -.
DR KEGG; kla:KLLA0_E18987g; -.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; Q6CMN0; -.
DR OMA; QHITFKD; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:1904564; C:Nbp35-Cfd1 ATPase complex; IEA:EnsemblFungi.
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:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:EnsemblFungi.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:EnsemblFungi.
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; IPR000808; Mrp_CS.
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.
DR PROSITE; PS01215; MRP; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..326
FT /note="Cytosolic Fe-S cluster assembly factor NBP35"
FT /id="PRO_0000278899"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 39
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 42
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 48
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 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 251
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 254
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 326 AA; 35300 MW; 833F558E0B1C9F2C CRC64;
MTEIANGQQI LPPDYTLKEP EPEHCPGPES ENAGKGDSCQ GCANKEVCES LPKGPDPDLP
LIKENLANIK HKILILSGKG GVGKSTFTTM LSWALSADED LQVGAMDLDI CGPSLPHMLG
CVRETIHESN TGWTPVYVTD NLATMSIQYM LPDTDSAIIW RGSKKNALIK KFLKDVDWDY
LDYLLIDTPP GTSDEHISIN NYLKESQIDG ALIVTTPQEV ALLDVRKEIN FCRKAGINIL
GLVENMSGFV CPNCKGESKI FKATTGGGKA LCNELGIDFL GSVPLDPRIG RCCETGESFL
DEFPDSPAST AILEVIESLR DAVGDV
