P40558 (CFD1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytosolic Fe-S cluster assembly factor CFD1

Alternative name(s):
Cytosolic Fe-S cluster-deficient protein 1
Ribosomal export protein 19

Gene names

Name:	CFD1
Synonyms:	DRE3, RIX19
Ordered Locus Names:	YIL003W
ORF Names:	YIA3W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35. 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. Ref.5 Ref.6 Ref.8 Ref.10
Cofactor	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 structure	Heterotetramer of 2 NBP35 and 2 CFD1 chains. Ref.10
Subcellular location	Cytoplasm Ref.5.
Sequence similarities	Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	4Fe-4S ATP-binding Iron Iron-sulfur Metal-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	iron-sulfur cluster assembly Inferred from direct assay Ref.8. Source: SGD tRNA wobble uridine modification Inferred from mutant phenotype PubMed 18755837. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: SGD
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from direct assay Ref.8. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Traceable author statement Ref.5. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NBP35	P52920	1	EBI-24924,EBI-11880

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 293	293	Cytosolic Fe-S cluster assembly factor CFD1 HAMAP-Rule MF_03039		PRO_0000184952
Regions
	Nucleotide binding	25 – 32	8	ATP Potential
Sites
	Metal binding	201	1	Iron-sulfur (4Fe-4S); shared with dimeric partner
	Metal binding	204	1	Iron-sulfur (4Fe-4S); shared with dimeric partner
Amino acid modifications
	Modified residue	291	1	Phosphoserine Ref.7 Ref.9
Experimental info
	Mutagenesis	31	1	K → A: Loss of function.
	Mutagenesis	86	1	T → A: Loss of function.
	Mutagenesis	182	1	C → A: Does not impair function. Ref.10
	Mutagenesis	201	1	C → A: Loss of function and disrupts heterotetramer formation. Ref.10
	Mutagenesis	204	1	C → A: Loss of function and disrupts heterotetramer formation. Ref.10
	Mutagenesis	207	1	C → A: Does not impair function. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P40558 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 5CDD563B51229D14	FASTA	293	31,922
	10 20 30 40 50 60 MEEQEIGVPA ASLAGIKHII LILSGKGGVG KSSVTTQTAL TLCSMGFKVG VLDIDLTGPS 70 80 90 100 110 120 LPRMFGLENE SIYQGPEGWQ PVKVETNSTG SLSVISLGFL LGDRGNSVIW RGPKKTSMIK 130 140 150 160 170 180 QFISDVAWGE LDYLLIDTPP GTSDEHISIA EELRYSKPDG GIVVTTPQSV ATADVKKEIN 190 200 210 220 230 240 FCKKVDLKIL GIIENMSGFV CPHCAECTNI FSSGGGKRLS EQFSVPYLGN VPIDPKFVEM 250 260 270 280 290 IENQVSSKKT LVEMYRESSL CPIFEEIMKK LRKQDTTTPV VDKHEQPQIE SPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX." Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S., Schwager C., Zimmermann J., Sander C., Ansorge W. Yeast 11:61-78(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"A novel eukaryotic factor for cytosolic Fe-S cluster assembly." Roy A., Solodovnikova N., Nicholson T., Antholine W., Walden W.E. EMBO J. 22:4826-4835(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"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.
[7]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, MASS SPECTROMETRY. Strain: ADR376.
[8]	"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 NBP35, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTER.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, MASS SPECTROMETRY.
[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-182; CYS-201; CYS-204 AND CYS-207.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79743 Genomic DNA. No translation available. Z38113 Genomic DNA. Translation: CAA86248.1. Z38062 Genomic DNA. Translation: CAA86200.1. AY558297 Genomic DNA. Translation: AAS56623.1. BK006942 Genomic DNA. Translation: DAA08543.1.
PIR	S58704.
RefSeq	NP_012263.1. NM_001179353.1.
3D structure databases
ProteinModelPortal	P40558.
SMR	P40558. Positions 13-269.
ModBase	Search...
Protein-protein interaction databases
IntAct	P40558. 2 interactions.
STRING	4932.YIL003W.
Proteomic databases
PaxDb	P40558.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL003W; YIL003W; YIL003W.
GeneID	854814.
KEGG	sce:YIL003W.
Organism-specific databases
CYGD	YIL003w.
SGD	S000001265. CFD1.
Phylogenomic databases
eggNOG	COG0489.
GeneTree	ENSGT00550000075057.
HOGENOM	HOG000079916.
OMA	CTDIFSK.
OrthoDB	EOG4RV61Q.
Gene expression databases
Genevestigator	P40558.
GermOnline	YIL003W. Saccharomyces cerevisiae.
Family and domain databases
HAMAP	MF_03039. NUBP2.
InterPro	IPR025723. Anion-transp_ATPase-like_dom. IPR019591. ATPase-like_ParA/MinD. IPR000808. Mrp_CS. [Graphical view]
Pfam	PF02374. ArsA_ATPase. 1 hit. PF10609. ParA. 1 hit. [Graphical view]
PROSITE	PS01215. MRP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977648.

Entry information

Entry name

CFD1_YEAST

Accession

Primary (citable) accession number: P40558
Secondary accession number(s): D6VVS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program