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CFD1_ASPTN
ID   CFD1_ASPTN              Reviewed;         311 AA.
AC   Q0CE30;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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; ORFNames=ATEG_08054;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476605; EAU31227.1; -; Genomic_DNA.
DR   RefSeq; XP_001216675.1; XM_001216675.1.
DR   AlphaFoldDB; Q0CE30; -.
DR   SMR; Q0CE30; -.
DR   STRING; 341663.Q0CE30; -.
DR   EnsemblFungi; EAU31227; EAU31227; ATEG_08054.
DR   GeneID; 4353396; -.
DR   VEuPathDB; FungiDB:ATEG_08054; -.
DR   eggNOG; KOG3022; Eukaryota.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   OMA; QGWVPVY; -.
DR   OrthoDB; 1166096at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..311
FT                   /note="Cytosolic Fe-S cluster assembly factor cfd1"
FT                   /id="PRO_0000278872"
FT   REGION          255..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         15..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT   BINDING         212
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         215
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   311 AA;  32781 MW;  1410F2EA36078262 CRC64;
     MPLDGVKNIV LVLSGKGGVG KSSVTLQLAL ALTLQGKSVG ILDIDLTGPS IPRLVGLEDA
     KITQSPAGWV PVPVHSATDN ATGPATGSLR CISLGFLLRD RGDAVIWRGP KKTAMIRQFL
     SDVSWGETDY LLVDTPPGTS DEHIALAEQL LTTATTDAAA AAAGGRPRLA GAVLVTTPQA
     IATSDVRKEV NFCVKTRIPT LGVIENMSGY ACPCCGEVSN IFSSGGGRAM AQEMGIKFLG
     VVPVDVKFGE LVEGGKIQDG SDSEDEGETA RQEPEPEAVD DRPLVERYKD CWSYPRFEEF
     ARTLIADIDG A
 
 
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