CFD1_SCHPO
ID CFD1_SCHPO Reviewed; 608 AA.
AC Q9UT57;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable cytosolic Fe-S cluster assembly factor SPAC806.02c;
GN ORFNames=SPAC806.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Fusion protein of two essential components of the cytosolic
CC iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for
CC maturation of extramitochondrial Fe-S proteins. May form a
CC heterotetramer with nubp35, functioning as a Fe-S scaffold complex,
CC mediating the de novo assembly of an Fe-S cluster and its transfer to
CC target apoproteins (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
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-SPAC806.02c heterotetramer.
CC {ECO:0000250};
CC -!- SUBUNIT: Heterotetramer of 2 nbp35 and 2 SPAC806.02c chains.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- MISCELLANEOUS: Results from a fusion of two genes coding for two
CC proteins which both play a role in assembly of Fe-S clusters in other
CC species (CFD1 and CIA1 in S.cerevisiae).
CC -!- SIMILARITY: In the N-terminal section; belongs to the Mrp/NBP35 ATP-
CC binding proteins family. NUBP2/CFD1 subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the WD repeat CIA1
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB55281.1; -; Genomic_DNA.
DR PIR; T39094; T39094.
DR RefSeq; NP_592852.1; NM_001018253.2.
DR AlphaFoldDB; Q9UT57; -.
DR SMR; Q9UT57; -.
DR STRING; 4896.SPAC806.02c.1; -.
DR iPTMnet; Q9UT57; -.
DR MaxQB; Q9UT57; -.
DR PaxDb; Q9UT57; -.
DR PRIDE; Q9UT57; -.
DR EnsemblFungi; SPAC806.02c.1; SPAC806.02c.1:pep; SPAC806.02c.
DR GeneID; 2542122; -.
DR KEGG; spo:SPAC806.02c; -.
DR PomBase; SPAC806.02c; -.
DR VEuPathDB; FungiDB:SPAC806.02c; -.
DR eggNOG; KOG0645; Eukaryota.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_030983_0_0_1; -.
DR InParanoid; Q9UT57; -.
DR OMA; IDDDWEC; -.
DR PhylomeDB; Q9UT57; -.
DR PRO; PR:Q9UT57; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0097361; C:CIA complex; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; ISO:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
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:0044572; P:[4Fe-4S] cluster assembly; ISO:PomBase.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; ISO:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03037; ciao1; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03039; NUBP2; 1.
DR InterPro; IPR028608; CIAO1/Cia1.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264; PTHR23264; 1.
DR Pfam; PF10609; ParA; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..608
FT /note="Probable cytosolic Fe-S cluster assembly factor
FT SPAC806.02c"
FT /id="PRO_0000278883"
FT REPEAT 288..327
FT /note="WD 1"
FT REPEAT 331..371
FT /note="WD 2"
FT REPEAT 376..415
FT /note="WD 3"
FT REPEAT 421..460
FT /note="WD 4"
FT REPEAT 465..504
FT /note="WD 5"
FT REPEAT 529..567
FT /note="WD 6"
FT REPEAT 576..608
FT /note="WD 7"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 608 AA; 67680 MW; 151FD4B532E81357 CRC64;
MDKVQHVILV LSGKGGVGKS SVTTQLALSL HDSKVYSRPL KTGILDIDLT GPSIPRMFGK
DAERNRIHQS SAGWVPVYTD ETKEIGLMSL GFLLTSKNDS VVWRGPKKAA MIRQFISDVS
WGELDFLIID TPPGTGDEHL TIVESLLSET STVRDVPIDG AVIVTTPQGI ATLDVQKEID
FCKKASIKIL GIVENMSGYI CPHCADCTNI FSSGGGLTLS EKYKLPFLGS VPIDPKFGEM
IENLTPDSNI VHLYSKTEMS KKFSFITNEF LNQLYGPRKL DTITTISGHT GRLWSVAAHP
MLPLFATSSQ DKSVRIYNSN TYNLVHVIDG FHTRSIRRVA WRPIERPVLA VASFDSVVSI
NEKIDDDWEC TAALEGHENE VKCIAWSCNG NYLATCSRDK SVWIWEATED DEFDCLAVLQ
EHTQDVKVVT WHPTEDLLVS GSYDNSICFW RDDGDDWALT CQLQGHTNTV WALAFSPNGN
TLASADNDGN VFLWIKISSN EDVATIDSTN ILRPALQEEW KQQTSLPHIH KGAVYTISWM
NDATLCSAGG DGKIVVYQRE KHDEALWHVA YEQDHAHGVY EINSLEYLRD DRLLSGGDDG
ECRVWSFK
