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Protein

Cytosolic Fe-S cluster assembly factor NBP35

Gene

NBP35

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation5 Publications

Cofactori

[4Fe-4S] clusterNote: 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Iron-sulfur 1 (4Fe-4S)
Metal bindingi41 – 411Iron-sulfur 1 (4Fe-4S)
Metal bindingi44 – 441Iron-sulfur 1 (4Fe-4S)
Metal bindingi50 – 501Iron-sulfur 1 (4Fe-4S)
Metal bindingi253 – 2531Iron-sulfur 2 (4Fe-4S); shared with dimeric partner
Metal bindingi256 – 2561Iron-sulfur 2 (4Fe-4S); shared with dimeric partner

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi80 – 878ATPUniRule annotation

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: SGD
  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • iron ion binding Source: SGD

GO - Biological processi

  • iron-sulfur cluster assembly Source: SGD
  • tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Ligandi

4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30591-MONOMER.
ReactomeiR-SCE-6799198. Complex I biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic Fe-S cluster assembly factor NBP35UniRule annotation
Alternative name(s):
Nucleotide-binding protein 35UniRule annotation
Gene namesi
Name:NBP35UniRule annotation
Ordered Locus Names:YGL091C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL091C.
SGDiS000003059. NBP35.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: Reactome
  • Nbp35-Cfd1 ATPase complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271C → A: Supports growth, albeit at a lower rate. 1 Publication
Mutagenesisi41 – 411C → A: Loss of function. 1 Publication
Mutagenesisi44 – 441C → A or G: Loss of function. 2 Publications
Mutagenesisi50 – 501C → A: Loss of function. 1 Publication
Mutagenesisi86 – 861K → Q: Lethal. 1 Publication
Mutagenesisi234 – 2341C → A: Does not impair function. 1 Publication
Mutagenesisi253 – 2531C → A: Loss fo function and disrupts heterotetramer formation. 2 Publications
Mutagenesisi256 – 2561C → A: Loss of function and disrupts heterotetramer formation. 1 Publication
Mutagenesisi295 – 2951C → A: Does not impair function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Cytosolic Fe-S cluster assembly factor NBP35PRO_0000184947Add
BLAST

Proteomic databases

MaxQBiP52920.
PeptideAtlasiP52920.

Interactioni

Subunit structurei

Heterotetramer of 2 NBP35 and 2 CFD1 chains.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi33160. 15 interactions.
DIPiDIP-1767N.
IntActiP52920. 9 interactions.
MINTiMINT-407213.

Structurei

3D structure databases

ProteinModelPortaliP52920.
SMRiP52920. Positions 64-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000009735.
HOGENOMiHOG000079916.
InParanoidiP52920.
OMAiMCAEMGI.
OrthoDBiEOG70CRJC.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_02040. Mrp_NBP35.
MF_03038. NUBP1.
InterProiIPR019591. Mrp/NBP35_ATP-bd.
IPR000808. Mrp_CS.
IPR028601. NUBP1/Nbp35.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23264. PTHR23264. 1 hit.
PfamiPF10609. ParA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS01215. MRP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEILPHVND EVLPAEYELN QPEPEHCPGP ESDMAGKSDA CGGCANKEIC
60 70 80 90 100
ESLPKGPDPD IPLITDNLSG IEHKILVLSG KGGVGKSTFA AMLSWALSAD
110 120 130 140 150
EDLQVGAMDL DICGPSLPHM LGCIKETVHE SNSGWTPVYV TDNLATMSIQ
160 170 180 190 200
YMLPEDDSAI IWRGSKKNLL IKKFLKDVDW DKLDYLVIDT PPGTSDEHIS
210 220 230 240 250
INKYMRESGI DGALVVTTPQ EVALLDVRKE IDFCKKAGIN ILGLVENMSG
260 270 280 290 300
FVCPNCKGES QIFKATTGGG EALCKELGIK FLGSVPLDPR IGKSCDMGES
310 320
FLDNYPDSPA SSAVLNVVEA LRDAVGDV
Length:328
Mass (Da):35,253
Last modified:October 1, 1996 - v1
Checksum:i4B2EADFD0555BCAA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581D → S in CAA64779 (PubMed:8921898).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95533 Genomic DNA. Translation: CAA64779.1.
Z72613 Genomic DNA. Translation: CAA96797.1.
BK006941 Genomic DNA. Translation: DAA08015.1.
PIRiS64098.
RefSeqiNP_011424.3. NM_001180956.3.

Genome annotation databases

EnsemblFungiiYGL091C; YGL091C; YGL091C.
GeneIDi852789.
KEGGisce:YGL091C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95533 Genomic DNA. Translation: CAA64779.1.
Z72613 Genomic DNA. Translation: CAA96797.1.
BK006941 Genomic DNA. Translation: DAA08015.1.
PIRiS64098.
RefSeqiNP_011424.3. NM_001180956.3.

3D structure databases

ProteinModelPortaliP52920.
SMRiP52920. Positions 64-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33160. 15 interactions.
DIPiDIP-1767N.
IntActiP52920. 9 interactions.
MINTiMINT-407213.

Proteomic databases

MaxQBiP52920.
PeptideAtlasiP52920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL091C; YGL091C; YGL091C.
GeneIDi852789.
KEGGisce:YGL091C.

Organism-specific databases

EuPathDBiFungiDB:YGL091C.
SGDiS000003059. NBP35.

Phylogenomic databases

GeneTreeiENSGT00390000009735.
HOGENOMiHOG000079916.
InParanoidiP52920.
OMAiMCAEMGI.
OrthoDBiEOG70CRJC.

Enzyme and pathway databases

BioCyciYEAST:G3O-30591-MONOMER.
ReactomeiR-SCE-6799198. Complex I biogenesis.

Miscellaneous databases

NextBioi972285.
PROiP52920.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_02040. Mrp_NBP35.
MF_03038. NUBP1.
InterProiIPR019591. Mrp/NBP35_ATP-bd.
IPR000808. Mrp_CS.
IPR028601. NUBP1/Nbp35.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23264. PTHR23264. 1 hit.
PfamiPF10609. ParA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS01215. MRP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NBP35 encodes an essential and evolutionary conserved protein in Saccharomyces cerevisiae with homology to a superfamily of bacterial ATPases."
    Vitale G., Fabre E., Hurt E.C.
    Gene 178:97-106(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: JU4.2XJRZ619B.
  2. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-44 AND LYS-86.
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    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.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. "Nar1p, a conserved eukaryotic protein with similarity to Fe-only hydrogenases, functions in cytosolic iron-sulphur protein biogenesis."
    Balk J., Pierik A.J., Aguilar Netz D.J., Muehlenhoff U., Lill R.
    Biochem. Soc. Trans. 33:86-89(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Functional link between ribosome formation and biogenesis of iron-sulfur proteins."
    Yarunin A., Panse V.G., Petfalski E., Dez C., Tollervey D., Hurt E.C.
    EMBO J. 24:580-588(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The eukaryotic P loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery."
    Hausmann A., Aguilar Netz D.J., Balk J., Pierik A.J., Muehlenhoff U., Lill R.
    Proc. Natl. Acad. Sci. U.S.A. 102:3266-3271(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IRON-SULFUR CLUSTER BINDING.
  9. "The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol."
    Netz D.J.A., Pierik A.J., Stuempfig M., Muehlenhoff U., Lill R.
    Nat. Chem. Biol. 3:278-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CFD1, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS, MUTAGENESIS OF CYS-253.
  10. "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."
    Netz D.J., Pierik A.J., Stumpfig M., Bill E., Sharma A.K., Pallesen L.J., Walden W.E., Lill R.
    J. Biol. Chem. 287:12365-12378(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-27; CYS-41; CYS-44; CYS-50; CYS-234; CYS-253; CYS-256 AND CYS-295.

Entry informationi

Entry nameiNBP35_YEAST
AccessioniPrimary (citable) accession number: P52920
Secondary accession number(s): D6VU54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.