ID   CFD1_CRYNB              Reviewed;         331 AA.
AC   P0CO91; Q561C3; Q5KQ24;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
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}; OrderedLocusNames=CNBA0700;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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. {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; AAEY01000001; EAL23420.1; -; Genomic_DNA.
DR   RefSeq; XP_778067.1; XM_772974.1.
DR   AlphaFoldDB; P0CO91; -.
DR   SMR; P0CO91; -.
DR   EnsemblFungi; AAW40670; AAW40670; CNA00720.
DR   EnsemblFungi; EAL23420; EAL23420; CNBA0700.
DR   GeneID; 4933321; -.
DR   KEGG; cnb:CNBA0700; -.
DR   VEuPathDB; FungiDB:CNBA0700; -.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   Proteomes; UP000001435; Chromosome 1.
DR   GO; GO:1904564; C:Nbp35-Cfd1 ATPase complex; IEA:EnsemblFungi.
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:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
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   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:EnsemblFungi.
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.
FT   CHAIN           1..331
FT                   /note="Cytosolic Fe-S cluster assembly factor CFD1"
FT                   /id="PRO_0000410152"
FT   BINDING         25..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT   BINDING         211
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         214
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   331 AA;  35464 MW;  F304C5D1D8FC5716 CRC64;
     MADIIETPVS RRLSTVKNII IVLSGKGGVG KSSSSVQLAL SLLAQSPTNR VGLIDLDITG
     PSLPRMVGLD TPTATVHQSS AGWVPVYVDQ GRRLGVMSIG FLLKDRGDSV VWRGPKKDGM
     IRQFLSEVRW GDLDYLVIDT PPGTSDEHIS LLTHLHPLFT PTMSNATTPT SILISTPQTT
     ALNDTLKSLS FTRKLSLPVM GLVENMAGYV CPCCGEISDT FGKGGGEAMA HKEGVGFLGR
     VPIDTVLVSL LDAVSKGEVL GEGAVEHTSD EAAEGQTNGS TEHFPLLDKY LETTSSKVWK
     DITQKLVDKI EQHKSDIRAR LESSSETLAI A