NBP35_YEAST
ID NBP35_YEAST Reviewed; 328 AA.
AC P52920; D6VU54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
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}; OrderedLocusNames=YGL091C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JU4.2XJRZ619B;
RX PubMed=8921898; DOI=10.1016/0378-1119(96)00341-1;
RA Vitale G., Fabre E., Hurt E.C.;
RT "NBP35 encodes an essential and evolutionary conserved protein in
RT Saccharomyces cerevisiae with homology to a superfamily of bacterial
RT ATPases.";
RL Gene 178:97-106(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-44 AND LYS-86.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP FUNCTION.
RX PubMed=15667273; DOI=10.1042/bst0330086;
RA Balk J., Pierik A.J., Aguilar Netz D.J., Muehlenhoff U., Lill R.;
RT "Nar1p, a conserved eukaryotic protein with similarity to Fe-only
RT hydrogenases, functions in cytosolic iron-sulphur protein biogenesis.";
RL Biochem. Soc. Trans. 33:86-89(2005).
RN [7]
RP FUNCTION.
RX PubMed=15660135; DOI=10.1038/sj.emboj.7600540;
RA Yarunin A., Panse V.G., Petfalski E., Dez C., Tollervey D., Hurt E.C.;
RT "Functional link between ribosome formation and biogenesis of iron-sulfur
RT proteins.";
RL EMBO J. 24:580-588(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND IRON-SULFUR CLUSTER BINDING.
RX PubMed=15728363; DOI=10.1073/pnas.0406447102;
RA Hausmann A., Aguilar Netz D.J., Balk J., Pierik A.J., Muehlenhoff U.,
RA Lill R.;
RT "The eukaryotic P loop NTPase Nbp35: an essential component of the
RT cytosolic and nuclear iron-sulfur protein assembly machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3266-3271(2005).
RN [9]
RP FUNCTION, INTERACTION WITH CFD1, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS,
RP AND MUTAGENESIS OF CYS-253.
RX PubMed=17401378; DOI=10.1038/nchembio872;
RA Netz D.J.A., Pierik A.J., Stuempfig M., Muehlenhoff U., Lill R.;
RT "The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly
RT in the yeast cytosol.";
RL Nat. Chem. Biol. 3:278-286(2007).
RN [10]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-27; CYS-41; CYS-44; CYS-50;
RP CYS-234; CYS-253; CYS-256 AND CYS-295.
RX PubMed=22362766; DOI=10.1074/jbc.m111.328914;
RA Netz D.J., Pierik A.J., Stumpfig M., Bill E., Sharma A.K., Pallesen L.J.,
RA Walden W.E., Lill R.;
RT "A bridging [4Fe-4S] cluster and nucleotide binding are essential for
RT function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein
RT maturation.";
RL J. Biol. Chem. 287:12365-12378(2012).
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 ECO:0000269|PubMed:15660135, ECO:0000269|PubMed:15667273,
CC ECO:0000269|PubMed:15728363, ECO:0000269|PubMed:17401378,
CC ECO:0000269|PubMed:22362766}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
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.;
CC -!- SUBUNIT: Heterotetramer of 2 NBP35 and 2 CFD1 chains.
CC {ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:22362766}.
CC -!- INTERACTION:
CC P52920; P40558: CFD1; NbExp=9; IntAct=EBI-11880, EBI-24924;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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; X95533; CAA64779.1; -; Genomic_DNA.
DR EMBL; Z72613; CAA96797.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08015.1; -; Genomic_DNA.
DR PIR; S64098; S64098.
DR RefSeq; NP_011424.3; NM_001180956.3.
DR AlphaFoldDB; P52920; -.
DR SMR; P52920; -.
DR BioGRID; 33160; 218.
DR ComplexPortal; CPX-385; CFD1-NBP35 complex.
DR DIP; DIP-1767N; -.
DR IntAct; P52920; 10.
DR MINT; P52920; -.
DR STRING; 4932.YGL091C; -.
DR MaxQB; P52920; -.
DR PaxDb; P52920; -.
DR PRIDE; P52920; -.
DR EnsemblFungi; YGL091C_mRNA; YGL091C; YGL091C.
DR GeneID; 852789; -.
DR KEGG; sce:YGL091C; -.
DR SGD; S000003059; NBP35.
DR VEuPathDB; FungiDB:YGL091C; -.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; P52920; -.
DR OMA; QHITFKD; -.
DR BioCyc; YEAST:G3O-30591-MON; -.
DR PRO; PR:P52920; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P52920; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IDA:ComplexPortal.
DR GO; GO:1904564; C:Nbp35-Cfd1 ATPase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IMP:SGD.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:SGD.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
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 1: Evidence at protein level;
KW 4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..328
FT /note="Cytosolic Fe-S cluster assembly factor NBP35"
FT /id="PRO_0000184947"
FT BINDING 27
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 80..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 253
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 256
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT MUTAGEN 27
FT /note="C->A: Supports growth, albeit at a lower rate."
FT /evidence="ECO:0000269|PubMed:22362766"
FT MUTAGEN 41
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:22362766"
FT MUTAGEN 44
FT /note="C->A,G: Loss of function."
FT /evidence="ECO:0000269|PubMed:22362766,
FT ECO:0000269|PubMed:9290212"
FT MUTAGEN 50
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:22362766"
FT MUTAGEN 86
FT /note="K->Q: Lethal."
FT /evidence="ECO:0000269|PubMed:9290212"
FT MUTAGEN 234
FT /note="C->A: Does not impair function."
FT /evidence="ECO:0000269|PubMed:22362766"
FT MUTAGEN 253
FT /note="C->A: Loss fo function and disrupts heterotetramer
FT formation."
FT /evidence="ECO:0000269|PubMed:17401378,
FT ECO:0000269|PubMed:22362766"
FT MUTAGEN 256
FT /note="C->A: Loss of function and disrupts heterotetramer
FT formation."
FT /evidence="ECO:0000269|PubMed:22362766"
FT MUTAGEN 295
FT /note="C->A: Does not impair function."
FT /evidence="ECO:0000269|PubMed:22362766"
FT CONFLICT 58
FT /note="D -> S (in Ref. 1; CAA64779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 35253 MW; 4B2EADFD0555BCAA CRC64;
MTEILPHVND EVLPAEYELN QPEPEHCPGP ESDMAGKSDA CGGCANKEIC ESLPKGPDPD
IPLITDNLSG IEHKILVLSG KGGVGKSTFA AMLSWALSAD EDLQVGAMDL DICGPSLPHM
LGCIKETVHE SNSGWTPVYV TDNLATMSIQ YMLPEDDSAI IWRGSKKNLL IKKFLKDVDW
DKLDYLVIDT PPGTSDEHIS INKYMRESGI DGALVVTTPQ EVALLDVRKE IDFCKKAGIN
ILGLVENMSG FVCPNCKGES QIFKATTGGG EALCKELGIK FLGSVPLDPR IGKSCDMGES
FLDNYPDSPA SSAVLNVVEA LRDAVGDV
