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 02-SEP-2026, entry version 191. 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; DOI=10.1038/387s084; 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=11; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 258. DR ComplexPortal; CPX-385; CFD1-NBP35 Fe-S cluster assembly complex. DR FunCoup; P40558; 220. DR IntAct; P40558; 3. DR STRING; 4932.YIL003W; -. DR iPTMnet; P40558; -. DR PaxDb; 4932-YIL003W; -. DR PeptideAtlas; P40558; -. DR EnsemblFungi; YIL003W_mRNA; YIL003W; YIL003W. DR GeneID; 854814; -. DR KEGG; sce:YIL003W; -. DR AGR; SGD:S000001265; -. DR SGD; S000001265; CFD1. DR VEuPathDB; FungiDB:YIL003W; -. DR eggNOG; KOG3022; Eukaryota. DR HOGENOM; CLU_024839_0_1_1; -. DR InParanoid; P40558; -. DR OMA; WIPVFAD; -. DR OrthoDB; 3900342at2759; -. DR BioCyc; YEAST:G3O-31282-MONOMER; -. DR BioGRID-ORCS; 854814; 2 hits in 10 CRISPR screens. 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:1904564; C:cytosolic [4Fe-4S] assembly scaffold complex; IDA:ComplexPortal. DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IDA:ComplexPortal. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:ComplexPortal. DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD. DR CDD; cd02037; Mrp_NBP35; 1. DR FunFam; 3.40.50.300:FF:001300; Cytosolic Fe-S cluster assembly factor CFD1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_02040; Mrp_NBP35; 1. DR HAMAP; MF_03039; NUBP2; 1. DR InterPro; IPR000808; Mrp-like_CS. DR InterPro; IPR019591; Mrp/NBP35_ATP-bd. DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR033756; YlxH/NBP35. DR PANTHER; PTHR23264:SF19; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP2; 1. DR PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 1. DR Pfam; PF10609; ParA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 //