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Cytosolic Fe-S cluster assembly factor NBP35 (Nucleotide-binding protein 35)

 NBP35_YEAST             Reviewed;         328 AA.
P52920; D6VU54;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
30-AUG-2017, entry version 145.
RecName: Full=Cytosolic Fe-S cluster assembly factor NBP35 {ECO:0000255|HAMAP-Rule:MF_03038};
AltName: Full=Nucleotide-binding protein 35 {ECO:0000255|HAMAP-Rule:MF_03038};
Name=NBP35 {ECO:0000255|HAMAP-Rule:MF_03038};
OrderedLocusNames=YGL091C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JU4.2XJRZ619B;
PubMed=8921898; DOI=10.1016/0378-1119(96)00341-1;
Vitale G., Fabre E., Hurt E.C.;
"NBP35 encodes an essential and evolutionary conserved protein in
Saccharomyces cerevisiae with homology to a superfamily of bacterial
ATPases.";
Gene 178:97-106(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND
MUTAGENESIS OF CYS-44 AND LYS-86.
STRAIN=ATCC 204508 / S288c;
PubMed=9290212;
DOI=10.1002/(SICI)1097-0061(19970915)13:11<1077::AID-YEA152>3.3.CO;2-P;
Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
chromosome VII.";
Yeast 13:1077-1090(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
FUNCTION.
PubMed=15667273; DOI=10.1042/BST0330086;
Balk J., Pierik A.J., Aguilar Netz D.J., Muehlenhoff U., Lill R.;
"Nar1p, a conserved eukaryotic protein with similarity to Fe-only
hydrogenases, functions in cytosolic iron-sulphur protein
biogenesis.";
Biochem. Soc. Trans. 33:86-89(2005).
[7]
FUNCTION.
PubMed=15660135; DOI=10.1038/sj.emboj.7600540;
Yarunin A., Panse V.G., Petfalski E., Dez C., Tollervey D., Hurt E.C.;
"Functional link between ribosome formation and biogenesis of iron-
sulfur proteins.";
EMBO J. 24:580-588(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND IRON-SULFUR CLUSTER BINDING.
PubMed=15728363; DOI=10.1073/pnas.0406447102;
Hausmann A., Aguilar Netz D.J., Balk J., Pierik A.J., Muehlenhoff U.,
Lill R.;
"The eukaryotic P loop NTPase Nbp35: an essential component of the
cytosolic and nuclear iron-sulfur protein assembly machinery.";
Proc. Natl. Acad. Sci. U.S.A. 102:3266-3271(2005).
[9]
FUNCTION, INTERACTION WITH CFD1, EPR SPECTROSCOPY OF IRON-SULFUR
CLUSTERS, AND MUTAGENESIS OF CYS-253.
PubMed=17401378; DOI=10.1038/nchembio872;
Netz D.J.A., Pierik A.J., Stuempfig M., Muehlenhoff U., Lill R.;
"The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein
assembly in the yeast cytosol.";
Nat. Chem. Biol. 3:278-286(2007).
[10]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-27; CYS-41; CYS-44; CYS-50;
CYS-234; CYS-253; CYS-256 AND CYS-295.
PubMed=22362766; DOI=10.1074/jbc.M111.328914;
Netz D.J., Pierik A.J., Stumpfig M., Bill E., Sharma A.K.,
Pallesen L.J., Walden W.E., Lill R.;
"A bridging [4Fe-4S] cluster and nucleotide binding are essential for
function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur
protein maturation.";
J. Biol. Chem. 287:12365-12378(2012).
-!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
assembly (CIA) machinery. Required for maturation of
extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer
forms a Fe-S scaffold complex, mediating the de novo assembly of
an Fe-S cluster and its transfer to target apoproteins. Required
for biogenesis and export of both ribosomal subunits, which may
reflect a role in assembly of the Fe/S clusters in RLI1, a protein
which performs rRNA processing and ribosome export.
{ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:15660135,
ECO:0000269|PubMed:15667273, ECO:0000269|PubMed:15728363,
ECO:0000269|PubMed:17401378, ECO:0000269|PubMed:22362766}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two
stable clusters in the N-termini of NBP35 and two labile, bridging
clusters between subunits of the NBP35-CFD1 heterotetramer.;
-!- SUBUNIT: Heterotetramer of 2 NBP35 and 2 CFD1 chains.
{ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:22362766}.
-!- INTERACTION:
P40558:CFD1; NbExp=9; IntAct=EBI-11880, EBI-24924;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}.
-----------------------------------------------------------------------
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EMBL; X95533; CAA64779.1; -; Genomic_DNA.
EMBL; Z72613; CAA96797.1; -; Genomic_DNA.
EMBL; BK006941; DAA08015.1; -; Genomic_DNA.
PIR; S64098; S64098.
RefSeq; NP_011424.3; NM_001180956.3.
ProteinModelPortal; P52920; -.
SMR; P52920; -.
BioGrid; 33160; 191.
DIP; DIP-1767N; -.
IntAct; P52920; 10.
MINT; MINT-407213; -.
STRING; 4932.YGL091C; -.
MaxQB; P52920; -.
PRIDE; P52920; -.
EnsemblFungi; YGL091C; YGL091C; YGL091C.
GeneID; 852789; -.
KEGG; sce:YGL091C; -.
EuPathDB; FungiDB:YGL091C; -.
SGD; S000003059; NBP35.
GeneTree; ENSGT00390000009735; -.
HOGENOM; HOG000079916; -.
InParanoid; P52920; -.
OMA; CPNQAIC; -.
OrthoDB; EOG092C4BLN; -.
BioCyc; YEAST:G3O-30591-MONOMER; -.
Reactome; R-SCE-2564818; Cytosolic iron-sulfur cluster assembly (yeast).
Reactome; R-SCE-2564830; Cytosolic iron-sulfur cluster assembly.
Reactome; R-SCE-6799198; Complex I biogenesis.
PRO; PR:P52920; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:1904564; C:Nbp35-Cfd1 ATPase complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0005506; F:iron ion binding; IMP:SGD.
GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:SGD.
GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
CDD; cd02037; MRP-like; 1.
HAMAP; MF_02040; Mrp_NBP35; 1.
HAMAP; MF_03038; NUBP1; 1.
InterPro; IPR019591; Mrp/NBP35_ATP-bd.
InterPro; IPR000808; Mrp_CS.
InterPro; IPR028601; NUBP1/Nbp35.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR033756; YlxH/NBP35.
PANTHER; PTHR23264; PTHR23264; 1.
Pfam; PF10609; ParA; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS01215; MRP; 1.
1: Evidence at protein level;
4Fe-4S; ATP-binding; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
Metal-binding; Nucleotide-binding; Nucleus; Reference proteome.
CHAIN 1 328 Cytosolic Fe-S cluster assembly factor
NBP35.
/FTId=PRO_0000184947.
NP_BIND 80 87 ATP. {ECO:0000255|HAMAP-Rule:MF_03038}.
METAL 27 27 Iron-sulfur 1 (4Fe-4S).
METAL 41 41 Iron-sulfur 1 (4Fe-4S).
METAL 44 44 Iron-sulfur 1 (4Fe-4S).
METAL 50 50 Iron-sulfur 1 (4Fe-4S).
METAL 253 253 Iron-sulfur 2 (4Fe-4S); shared with
dimeric partner.
METAL 256 256 Iron-sulfur 2 (4Fe-4S); shared with
dimeric partner.
MUTAGEN 27 27 C->A: Supports growth, albeit at a lower
rate. {ECO:0000269|PubMed:22362766}.
MUTAGEN 41 41 C->A: Loss of function.
{ECO:0000269|PubMed:22362766}.
MUTAGEN 44 44 C->A,G: Loss of function.
{ECO:0000269|PubMed:22362766,
ECO:0000269|PubMed:9290212}.
MUTAGEN 50 50 C->A: Loss of function.
{ECO:0000269|PubMed:22362766}.
MUTAGEN 86 86 K->Q: Lethal.
{ECO:0000269|PubMed:9290212}.
MUTAGEN 234 234 C->A: Does not impair function.
{ECO:0000269|PubMed:22362766}.
MUTAGEN 253 253 C->A: Loss fo function and disrupts
heterotetramer formation.
{ECO:0000269|PubMed:17401378,
ECO:0000269|PubMed:22362766}.
MUTAGEN 256 256 C->A: Loss of function and disrupts
heterotetramer formation.
{ECO:0000269|PubMed:22362766}.
MUTAGEN 295 295 C->A: Does not impair function.
{ECO:0000269|PubMed:22362766}.
CONFLICT 58 58 D -> S (in Ref. 1; CAA64779).
{ECO:0000305}.
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


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