ID   G0SH86_CHATD            Unreviewed;       310 AA.
AC   G0SH86;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   11-JUN-2014, entry version 10.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor CFD1;
DE   AltName: Full=Cytosolic Fe-S cluster-deficient protein 1;
GN   Name=CFD1; ORFNames=CTHT_0069100;
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=759272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R.,
RA   Devos D.P., Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC       assembly (CIA) machinery. Required for maturation of
CC       extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer
CC       forms a Fe-S scaffold complex, mediating the de novo assembly of
CC       an Fe-S cluster and its transfer to target apoproteins (By
CC       similarity).
CC   -!- COFACTOR: Binds 4 4Fe-4S clusters per heterotetramer. Contains two
CC       stable clusters in the N-termini of NBP35 and two labile, bridging
CC       clusters between subunits of the NBP35-CFD1 heterotetramer (By
CC       similarity).
CC   -!- SUBUNIT: Heterotetramer of 2 NBP35 and 2 CFD1 chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       NUBP2/CFD1 subfamily.
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DR   EMBL; GL988047; EGS17575.1; -; Genomic_DNA.
DR   RefSeq; XP_006697193.1; XM_006697130.1.
DR   GeneID; 18260948; -.
DR   OrthoDB; EOG70CRJC; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03039; NUBP2; 1.
DR   InterPro; IPR019591; ATPase-like_ParA/MinD.
DR   InterPro; IPR015223; ATPase_MipZ/NubP2/Cfd1.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF09140; MipZ; 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; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding.
FT   NP_BIND      15     22       ATP (By similarity){EA3}.
FT   METAL       199    199       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner (By similarity){EA3}.
FT   METAL       202    202       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner (By similarity){EA3}.
SQ   SEQUENCE   310 AA;  33239 MW;  0F3BE634AEB4BD6E CRC64;
     MSLSQVKHII LVLSGKGGVG KSSVTTQLAL SLSQAGYSVG VLDVDLTGPS IPRMFAVEDA
     KVKQGSGGWL PVVVHEANPS TGIGSLRVMS LGFLLPRRGD AVIWRGPKKT AMVRQFMSDV
     LWDELDFLLV DTPPGTSDEH ISLAETLLQE ARPGQLSGAI VVTTPQAVAT ADVRKELNFC
     KKTGIRVLGV VENMSGFVCP NCSECTNIFS SGGGEIMAND FNVRFLGRVP IDPQFLVLIE
     TGKRPRYPEG TKVNSQDLSF QHLEQVDNAD NPETPNSSLL VDKYRDCSLA PIFRAITADV
     VVAVEQASGS
//