CIAO1_YEAST
ID CIAO1_YEAST Reviewed; 330 AA.
AC Q05583; D6VSQ1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Cytosolic iron-sulfur protein assembly protein 1;
GN Name=CIA1 {ECO:0000255|HAMAP-Rule:MF_03037}; OrderedLocusNames=YDR267C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, INTERACTION WITH NAR1, AND SUBCELLULAR LOCATION.
RX PubMed=16314508; DOI=10.1128/mcb.25.24.10833-10841.2005;
RA Balk J., Aguilar Netz D.J.A., Tepper K., Pierik A.J., Lill R.;
RT "The essential WD40 protein Cia1 is involved in a late step of cytosolic
RT and nuclear iron-sulfur protein assembly.";
RL Mol. Cell. Biol. 25:10833-10841(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), DOMAINS WD REPEATS, AND MUTAGENESIS
RP OF ARG-127.
RX PubMed=17937914; DOI=10.1016/j.str.2007.08.009;
RA Srinivasan V., Netz D.J.A., Webert H., Mascarenhas J., Pierik A.J.,
RA Michel H., Lill R.;
RT "Structure of the yeast WD40 domain protein Cia1, a component acting late
RT in iron-sulfur protein biogenesis.";
RL Structure 15:1246-1257(2007).
CC -!- FUNCTION: Essential component of the cytosolic iron-sulfur (Fe/S)
CC protein assembly machinery. Required for the maturation of
CC extramitochondrial Fe/S proteins. {ECO:0000255|HAMAP-Rule:MF_03037,
CC ECO:0000269|PubMed:16314508}.
CC -!- SUBUNIT: Interacts with NAR1. {ECO:0000255|HAMAP-Rule:MF_03037,
CC ECO:0000269|PubMed:16314508}.
CC -!- INTERACTION:
CC Q05583; P40469: MET18; NbExp=3; IntAct=EBI-32145, EBI-11492;
CC Q05583; P23503: NAR1; NbExp=2; IntAct=EBI-32145, EBI-11864;
CC Q05583; P38829: YHR122W; NbExp=4; IntAct=EBI-32145, EBI-24704;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Preferentially localized
CC to the nucleus.
CC -!- MISCELLANEOUS: Present with 5640 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat CIA1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03037}.
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DR EMBL; U51030; AAB64456.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12111.1; -; Genomic_DNA.
DR PIR; S70127; S70127.
DR RefSeq; NP_010553.3; NM_001180575.3.
DR PDB; 2HES; X-ray; 1.70 A; X=1-330.
DR PDBsum; 2HES; -.
DR AlphaFoldDB; Q05583; -.
DR SMR; Q05583; -.
DR BioGRID; 32323; 67.
DR DIP; DIP-1836N; -.
DR IntAct; Q05583; 73.
DR MINT; Q05583; -.
DR STRING; 4932.YDR267C; -.
DR iPTMnet; Q05583; -.
DR MaxQB; Q05583; -.
DR PaxDb; Q05583; -.
DR PRIDE; Q05583; -.
DR EnsemblFungi; YDR267C_mRNA; YDR267C; YDR267C.
DR GeneID; 851860; -.
DR KEGG; sce:YDR267C; -.
DR SGD; S000002675; CIA1.
DR VEuPathDB; FungiDB:YDR267C; -.
DR eggNOG; KOG0645; Eukaryota.
DR GeneTree; ENSGT00940000158670; -.
DR HOGENOM; CLU_000288_57_8_1; -.
DR InParanoid; Q05583; -.
DR OMA; DDWECAA; -.
DR BioCyc; YEAST:G3O-29837-MON; -.
DR EvolutionaryTrace; Q05583; -.
DR PRO; PR:Q05583; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05583; protein.
DR GO; GO:0097361; C:CIA complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:SGD.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03037; ciao1; 1.
DR InterPro; IPR028608; CIAO1/Cia1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19920; PTHR19920; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..330
FT /note="Cytosolic iron-sulfur protein assembly protein 1"
FT /id="PRO_0000253806"
FT REPEAT 12..53
FT /note="WD 1"
FT REPEAT 56..95
FT /note="WD 2"
FT REPEAT 105..144
FT /note="WD 3"
FT REPEAT 151..190
FT /note="WD 4"
FT REPEAT 195..236
FT /note="WD 5"
FT REPEAT 248..286
FT /note="WD 6"
FT REPEAT 292..330
FT /note="WD 7"
FT MUTAGEN 127
FT /note="R->E: Impaired in cytosolic Fe/S protein assembly."
FT /evidence="ECO:0000269|PubMed:17937914"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:2HES"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:2HES"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:2HES"
SQ SEQUENCE 330 AA; 37275 MW; B44CCAA3125FD666 CRC64;
MASINLIKSL KLYKEKIWSF DFSQGILATG STDRKIKLVS VKYDDFTLID VLDETAHKKA
IRSVAWRPHT SLLAAGSFDS TVSIWAKEES ADRTFEMDLL AIIEGHENEV KGVAWSNDGY
YLATCSRDKS VWIWETDESG EEYECISVLQ EHSQDVKHVI WHPSEALLAS SSYDDTVRIW
KDYDDDWECV AVLNGHEGTV WSSDFDKTEG VFRLCSGSDD STVRVWKYMG DDEDDQQEWV
CEAILPDVHK RQVYNVAWGF NGLIASVGAD GVLAVYEEVD GEWKVFAKRA LCHGVYEINV
VKWLELNGKT ILATGGDDGI VNFWSLEKAA
