CFD1_EMENI
ID CFD1_EMENI Reviewed; 334 AA.
AC P0C8Q1; C8V7E8; Q5AU02;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=AN11060;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA58884.1; Type=Erroneous gene model prediction; Note=The predicted gene AN8228 has been split into 2 genes: AN11055 and AN11060.; Evidence={ECO:0000305};
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DR EMBL; AACD01000144; EAA58884.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF74155.1; -; Genomic_DNA.
DR AlphaFoldDB; P0C8Q1; -.
DR SMR; P0C8Q1; -.
DR STRING; 162425.CADANIAP00004278; -.
DR EnsemblFungi; CBF74155; CBF74155; ANIA_11060.
DR EnsemblFungi; EAA58884; EAA58884; AN8228.2.
DR VEuPathDB; FungiDB:AN11060; -.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_391091_0_0_1; -.
DR InParanoid; P0C8Q1; -.
DR OMA; QGWVPVY; -.
DR OrthoDB; 1166096at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
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; 2.
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..334
FT /note="Cytosolic Fe-S cluster assembly factor cfd1"
FT /id="PRO_0000363398"
FT REGION 274..302
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 234
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 237
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 334 AA; 35807 MW; 9894835A60116525 CRC64;
MPLEGIKNII LILSGKGGVG KSSVTLQLAL ALTLQGKSVG VLDIDLTGPS IPRLVGLEGA
KITQSSNGWV PVPVHEAEAQ TASGNDAAVA LSDDGGDENK DVERAKPRGS LRCMSLGFLL
RDRGDAVIWR GPKKTAMIRQ FLTDVYWGDT DYLLVDTPPG TSDEHIALAE ELLKLSTTSP
SSTGVGALPR LTGAVLVTTP QAIATSDVRK EVNFCVKTNI PTLGVIENMS GYTCPCCGEV
SNLFSSGGGE VMAREMGVRF LGKVPVDVQF GALVEGKSQE ESDDEDEDRE RNKVEEEKGQ
DFVDERPLVE RYKECWSYGQ FEGFAKTLIG EIEG
