CFD1_ASPCL
ID CFD1_ASPCL Reviewed; 315 AA.
AC A1C4X8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=ACLA_001570;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027004; EAW14746.1; -; Genomic_DNA.
DR RefSeq; XP_001276172.1; XM_001276171.1.
DR AlphaFoldDB; A1C4X8; -.
DR SMR; A1C4X8; -.
DR STRING; 5057.CADACLAP00000089; -.
DR EnsemblFungi; EAW14746; EAW14746; ACLA_001570.
DR GeneID; 4708655; -.
DR KEGG; act:ACLA_001570; -.
DR VEuPathDB; FungiDB:ACLA_001570; -.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_024839_0_1_1; -.
DR OMA; QGWVPVY; -.
DR OrthoDB; 1166096at2759; -.
DR Proteomes; UP000006701; 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..315
FT /note="Cytosolic Fe-S cluster assembly factor cfd1"
FT /id="PRO_0000278869"
FT REGION 256..283
FT /note="Disordered"
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 315 AA; 33309 MW; EB9B3F9F037F072A CRC64;
MPLDGVKNIV LVLSGKGGVG KSSVTLQLAL ALSLQGKSVG ILDIDLTGPS IPRLVGLEDA
KITQAPGGWI PVPVHTAQNP SSTTQPRGSL RCMSLGFLLR DRGDAVIWRG PKKTAMIRQF
LSDVYWGPTD YLLVDTPPGT SDEHIALAEQ LLTLASTDPS ATAAGLSRLA GAVLVTTPQA
IATSDVRKEA NFCVKTKIPV LGVIENMSGY SCPCCGEVSN LFSSGGGKVM ADELGIKFLG
SVPVDVKFGE LVEGKVVDDS DSDEEEGATQ AQQQEEPVDD RPLVERYKDC WSHSRFEEFA
KTLISQIEGA SPASG
