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Protein

Cytosolic iron-sulfur protein assembly protein 1

Gene

CIA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.UniRule annotation1 Publication

GO - Biological processi

  • iron-sulfur cluster assembly Source: SGD
  • small molecule metabolic process Source: Reactome
  • tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-29837-MONOMER.
ReactomeiR-SCE-2564830. Cytosolic iron-sulfur cluster assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic iron-sulfur protein assembly protein 1
Gene namesi
Name:CIA1UniRule annotation
Ordered Locus Names:YDR267C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR267C.
SGDiS000002675. CIA1.

Subcellular locationi

GO - Cellular componenti

  • CIA complex Source: InterPro
  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271R → E: Impaired in cytosolic Fe/S protein assembly. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Cytosolic iron-sulfur protein assembly protein 1PRO_0000253806Add
BLAST

Proteomic databases

MaxQBiQ05583.

Interactioni

Subunit structurei

Interacts with NAR1.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NAR1P235032EBI-32145,EBI-11864
YHR122WP388294EBI-32145,EBI-24704

Protein-protein interaction databases

BioGridi32323. 15 interactions.
DIPiDIP-1836N.
IntActiQ05583. 56 interactions.
MINTiMINT-405749.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi17 – 237Combined sources
Beta strandi26 – 349Combined sources
Beta strandi36 – 405Combined sources
Beta strandi42 – 443Combined sources
Beta strandi47 – 526Combined sources
Beta strandi61 – 666Combined sources
Beta strandi70 – 778Combined sources
Beta strandi82 – 865Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi144 – 1496Combined sources
Beta strandi156 – 1616Combined sources
Beta strandi163 – 17210Combined sources
Beta strandi177 – 1837Combined sources
Beta strandi186 – 1938Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi208 – 2114Combined sources
Beta strandi213 – 2186Combined sources
Beta strandi223 – 2319Combined sources
Beta strandi237 – 2448Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi264 – 2685Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi282 – 2909Combined sources
Turni292 – 2954Combined sources
Beta strandi298 – 3036Combined sources
Beta strandi312 – 3165Combined sources
Beta strandi319 – 3257Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HESX-ray1.70X1-330[»]
ProteinModelPortaliQ05583.
SMRiQ05583. Positions 3-326.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05583.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati12 – 5342WD 1Add
BLAST
Repeati56 – 9540WD 2Add
BLAST
Repeati105 – 14440WD 3Add
BLAST
Repeati151 – 19040WD 4Add
BLAST
Repeati195 – 23642WD 5Add
BLAST
Repeati248 – 28639WD 6Add
BLAST
Repeati292 – 33039WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat CIA1 family.UniRule annotation
Contains 7 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00820000127115.
HOGENOMiHOG000208901.
InParanoidiQ05583.
OMAiWEVAGDD.
OrthoDBiEOG7D59XT.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03037. ciao1.
InterProiIPR028608. CIAO1/Cia1.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05583-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASINLIKSL KLYKEKIWSF DFSQGILATG STDRKIKLVS VKYDDFTLID
60 70 80 90 100
VLDETAHKKA IRSVAWRPHT SLLAAGSFDS TVSIWAKEES ADRTFEMDLL
110 120 130 140 150
AIIEGHENEV KGVAWSNDGY YLATCSRDKS VWIWETDESG EEYECISVLQ
160 170 180 190 200
EHSQDVKHVI WHPSEALLAS SSYDDTVRIW KDYDDDWECV AVLNGHEGTV
210 220 230 240 250
WSSDFDKTEG VFRLCSGSDD STVRVWKYMG DDEDDQQEWV CEAILPDVHK
260 270 280 290 300
RQVYNVAWGF NGLIASVGAD GVLAVYEEVD GEWKVFAKRA LCHGVYEINV
310 320 330
VKWLELNGKT ILATGGDDGI VNFWSLEKAA
Length:330
Mass (Da):37,275
Last modified:November 1, 1996 - v1
Checksum:iB44CCAA3125FD666
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51030 Genomic DNA. Translation: AAB64456.1.
BK006938 Genomic DNA. Translation: DAA12111.1.
PIRiS70127.
RefSeqiNP_010553.3. NM_001180575.3.

Genome annotation databases

EnsemblFungiiYDR267C; YDR267C; YDR267C.
GeneIDi851860.
KEGGisce:YDR267C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51030 Genomic DNA. Translation: AAB64456.1.
BK006938 Genomic DNA. Translation: DAA12111.1.
PIRiS70127.
RefSeqiNP_010553.3. NM_001180575.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HESX-ray1.70X1-330[»]
ProteinModelPortaliQ05583.
SMRiQ05583. Positions 3-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32323. 15 interactions.
DIPiDIP-1836N.
IntActiQ05583. 56 interactions.
MINTiMINT-405749.

Proteomic databases

MaxQBiQ05583.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR267C; YDR267C; YDR267C.
GeneIDi851860.
KEGGisce:YDR267C.

Organism-specific databases

EuPathDBiFungiDB:YDR267C.
SGDiS000002675. CIA1.

Phylogenomic databases

GeneTreeiENSGT00820000127115.
HOGENOMiHOG000208901.
InParanoidiQ05583.
OMAiWEVAGDD.
OrthoDBiEOG7D59XT.

Enzyme and pathway databases

BioCyciYEAST:G3O-29837-MONOMER.
ReactomeiR-SCE-2564830. Cytosolic iron-sulfur cluster assembly.

Miscellaneous databases

EvolutionaryTraceiQ05583.
PROiQ05583.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03037. ciao1.
InterProiIPR028608. CIAO1/Cia1.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly."
    Balk J., Aguilar Netz D.J.A., Tepper K., Pierik A.J., Lill R.
    Mol. Cell. Biol. 25:10833-10841(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NAR1, SUBCELLULAR LOCATION.
  6. "Structure of the yeast WD40 domain protein Cia1, a component acting late in iron-sulfur protein biogenesis."
    Srinivasan V., Netz D.J.A., Webert H., Mascarenhas J., Pierik A.J., Michel H., Lill R.
    Structure 15:1246-1257(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), DOMAINS WD REPEATS, MUTAGENESIS OF ARG-127.

Entry informationi

Entry nameiCIAO1_YEAST
AccessioniPrimary (citable) accession number: Q05583
Secondary accession number(s): D6VSQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5640 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.