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CFD1_KLULA
ID   CFD1_KLULA              Reviewed;         283 AA.
AC   Q6CQV4;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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};
GN   Name=CFD1 {ECO:0000255|HAMAP-Rule:MF_03039};
GN   OrderedLocusNames=KLLA0D13970g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC       assembly (CIA) machinery. Required for maturation of extramitochondrial
CC       Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold
CC       complex, mediating the de novo assembly of an Fe-S cluster and its
CC       transfer to target apoproteins. Required for biogenesis and export of
CC       both ribosomal subunits, which may reflect a role in assembly of the
CC       Fe/S clusters in RLI1, a protein which performs rRNA processing and
CC       ribosome export. {ECO:0000255|HAMAP-Rule:MF_03039}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03039};
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. {ECO:0000255|HAMAP-
CC       Rule:MF_03039};
CC   -!- SUBUNIT: Heterotetramer of 2 NBP35 and 2 CFD1 chains.
CC       {ECO:0000255|HAMAP-Rule:MF_03039}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03039}.
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; CR382124; CAH00781.1; -; Genomic_DNA.
DR   RefSeq; XP_453685.1; XM_453685.1.
DR   AlphaFoldDB; Q6CQV4; -.
DR   SMR; Q6CQV4; -.
DR   STRING; 28985.XP_453685.1; -.
DR   EnsemblFungi; CAH00781; CAH00781; KLLA0_D13970g.
DR   GeneID; 2892969; -.
DR   KEGG; kla:KLLA0_D13970g; -.
DR   eggNOG; KOG3022; Eukaryota.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   InParanoid; Q6CQV4; -.
DR   OMA; QGWVPVY; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..283
FT                   /note="Cytosolic Fe-S cluster assembly factor CFD1"
FT                   /id="PRO_0000278880"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT   BINDING         202
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT   BINDING         205
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
SQ   SEQUENCE   283 AA;  30765 MW;  C0CBA155F5ADDA60 CRC64;
     MSAETELLGM PESLKDIKHI ILVLSGKGGV GKSSVTTQTA LTLCLKGYKV GVLDIDLTGP
     SLPRMFGLEN KQVYQASKGW IPVSVPTTSG GELKLMSLGF LLDDRGNSVV WRGPKKSAMI
     KQFIKDVDWG DLDYLIIDTP PGTSDEHISI AEELRWAAPD GAIIVTTPQG VATADVRKEI
     NFCKKVNFNI LGVIENMSGF ICPHCAECTD IFSRGGGFKL ASEYNVPYLG NIPIDPTFVE
     LIEKQTGFKE SLVDLYKDSG LYVIFSKILD NVLNGEVKSG TDQ
 
 
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