CFD1_YEAST
ID CFD1_YEAST Reviewed; 293 AA.
AC P40558; D6VVS7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor CFD1 {ECO:0000255|HAMAP-Rule:MF_03039};
DE AltName: Full=Cytosolic Fe-S cluster-deficient protein 1 {ECO:0000255|HAMAP-Rule:MF_03039};
DE AltName: Full=Ribosomal export protein 19;
GN Name=CFD1 {ECO:0000255|HAMAP-Rule:MF_03039}; Synonyms=DRE3, RIX19;
GN OrderedLocusNames=YIL003W; ORFNames=YIA3W;
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=ATCC 204508 / S288c;
RX PubMed=7762303; DOI=10.1002/yea.320110109;
RA Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT "Nucleotide sequence and analysis of the centromeric region of yeast
RT chromosome IX.";
RL Yeast 11:61-78(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12970194; DOI=10.1093/emboj/cdg455;
RA Roy A., Solodovnikova N., Nicholson T., Antholine W., Walden W.E.;
RT "A novel eukaryotic factor for cytosolic Fe-S cluster assembly.";
RL EMBO J. 22:4826-4835(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP FUNCTION, INTERACTION WITH NBP35, AND EPR SPECTROSCOPY OF IRON-SULFUR
RP CLUSTER.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-182; CYS-201; CYS-204 AND
RP CYS-207.
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).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31040179; DOI=10.1074/jbc.ra119.008600;
RA Pandey A.K., Pain J., Dancis A., Pain D.;
RT "Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm
RT for iron-sulfur cluster assembly and tRNA thiolation in yeast.";
RL J. Biol. Chem. 294:9489-9502(2019).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC assembly (CIA) machinery (PubMed:12970194, PubMed:15660135,
CC PubMed:17401378). Required for maturation of extramitochondrial Fe-S
CC proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378,
CC PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms
CC a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S
CC cluster and its transfer to target apoproteins (PubMed:17401378,
CC PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for
CC loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766).
CC Required for biogenesis and export of both ribosomal subunits, which
CC may reflect a role in assembly of the Fe/S clusters in RLI1, a protein
CC which performs rRNA processing and ribosome export (PubMed:15660135).
CC {ECO:0000255|HAMAP-Rule:MF_03039, ECO:0000269|PubMed:12970194,
CC ECO:0000269|PubMed:15660135, ECO:0000269|PubMed:17401378,
CC ECO:0000269|PubMed:22362766, ECO:0000269|PubMed:31040179}.
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_03039, ECO:0000269|PubMed:22362766}.
CC -!- INTERACTION:
CC P40558; P52920: NBP35; NbExp=9; IntAct=EBI-24924, EBI-11880;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03039,
CC ECO:0000269|PubMed:12970194}.
CC -!- DISRUPTION PHENOTYPE: Inviable (PubMed:12970194). Decreases cytosolic
CC iron-sulfur (Fe-S) protein assembly (PubMed:31040179).
CC {ECO:0000269|PubMed:12970194, ECO:0000269|PubMed:31040179}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP2/CFD1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03039}.
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DR EMBL; X79743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z38113; CAA86248.1; -; Genomic_DNA.
DR EMBL; Z38062; CAA86200.1; -; Genomic_DNA.
DR EMBL; AY558297; AAS56623.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08543.1; -; Genomic_DNA.
DR PIR; S58704; S58704.
DR RefSeq; NP_012263.1; NM_001179353.1.
DR AlphaFoldDB; P40558; -.
DR SMR; P40558; -.
DR BioGRID; 34989; 250.
DR ComplexPortal; CPX-385; CFD1-NBP35 complex.
DR IntAct; P40558; 3.
DR STRING; 4932.YIL003W; -.
DR iPTMnet; P40558; -.
DR MaxQB; P40558; -.
DR PaxDb; P40558; -.
DR PRIDE; P40558; -.
DR EnsemblFungi; YIL003W_mRNA; YIL003W; YIL003W.
DR GeneID; 854814; -.
DR KEGG; sce:YIL003W; -.
DR SGD; S000001265; CFD1.
DR VEuPathDB; FungiDB:YIL003W; -.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; P40558; -.
DR OMA; QGWVPVY; -.
DR BioCyc; YEAST:G3O-31282-MON; -.
DR PRO; PR:P40558; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40558; 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:0051539; F:4 iron, 4 sulfur cluster binding; IDA:SGD.
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:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_03039; NUBP2; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..293
FT /note="Cytosolic Fe-S cluster assembly factor CFD1"
FT /id="PRO_0000184952"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 31
FT /note="K->A: Loss of function."
FT MUTAGEN 86
FT /note="T->A: Loss of function."
FT MUTAGEN 182
FT /note="C->A: Does not impair function."
FT /evidence="ECO:0000269|PubMed:22362766"
FT MUTAGEN 201
FT /note="C->A: Loss of function and disrupts heterotetramer
FT formation."
FT /evidence="ECO:0000269|PubMed:22362766"
FT MUTAGEN 204
FT /note="C->A: Loss of function and disrupts heterotetramer
FT formation."
FT /evidence="ECO:0000269|PubMed:22362766"
FT MUTAGEN 207
FT /note="C->A: Does not impair function."
FT /evidence="ECO:0000269|PubMed:22362766"
SQ SEQUENCE 293 AA; 31922 MW; 5CDD563B51229D14 CRC64;
MEEQEIGVPA ASLAGIKHII LILSGKGGVG KSSVTTQTAL TLCSMGFKVG VLDIDLTGPS
LPRMFGLENE SIYQGPEGWQ PVKVETNSTG SLSVISLGFL LGDRGNSVIW RGPKKTSMIK
QFISDVAWGE LDYLLIDTPP GTSDEHISIA EELRYSKPDG GIVVTTPQSV ATADVKKEIN
FCKKVDLKIL GIIENMSGFV CPHCAECTNI FSSGGGKRLS EQFSVPYLGN VPIDPKFVEM
IENQVSSKKT LVEMYRESSL CPIFEEIMKK LRKQDTTTPV VDKHEQPQIE SPK
