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Protein

Superoxide dismutase 1 copper chaperone

Gene

CCS1

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

Copper chaperone for apo superoxide dismutase 1 (SOD1). Binds copper ions and delivers them specifically to apo-SOD1.1 Publication

Cofactori

Cu2+PROSITE-ProRule annotationNote: Binds 2 copper ions per subunit.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi16Zinc; shared with apo-SOD1PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi17Copper 1PROSITE-ProRule annotation1
Metal bindingi20Copper 1PROSITE-ProRule annotation1
Metal bindingi229Copper 2PROSITE-ProRule annotation1
Metal bindingi231Copper 2PROSITE-ProRule annotation1

GO - Molecular functioni

  • superoxide dismutase copper chaperone activity Source: SGD
  • zinc ion binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32743-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase 1 copper chaperone
Gene namesi
Name:CCS1
Synonyms:LYS7
Ordered Locus Names:YMR038C
ORF Names:YM9532.03C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR038C.
SGDiS000004641. CCS1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • mitochondrial inner membrane Source: SGD
  • mitochondrial intermembrane space Source: Reactome
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002135421 – 249Superoxide dismutase 1 copper chaperoneAdd BLAST249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 64Combined sources1 Publication
Disulfide bondi229Interchain (with C-58 in apo-SOD1)Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP40202.
PRIDEiP40202.

PTM databases

iPTMnetiP40202.

Interactioni

Subunit structurei

Homodimer, and heterodimer with apo-SOD1. Zinc-binding at His-16 of CCS1 and 'Glu-43' of apo-SOD1 is required for this heterodimerization.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SOD1P004452EBI-10287,EBI-17635

Protein-protein interaction databases

BioGridi35210. 177 interactors.
DIPiDIP-4507N.
IntActiP40202. 2 interactors.
MINTiMINT-429630.

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi7 – 12Combined sources6
Beta strandi17 – 19Combined sources3
Helixi20 – 28Combined sources9
Beta strandi34 – 40Combined sources7
Turni41 – 44Combined sources4
Beta strandi45 – 52Combined sources8
Helixi54 – 63Combined sources10
Beta strandi69 – 71Combined sources3
Beta strandi79 – 85Combined sources7
Beta strandi100 – 110Combined sources11
Beta strandi113 – 125Combined sources13
Beta strandi127 – 135Combined sources9
Helixi142 – 145Combined sources4
Beta strandi148 – 152Combined sources5
Beta strandi157 – 159Combined sources3
Beta strandi161 – 164Combined sources4
Turni165 – 168Combined sources4
Beta strandi169 – 179Combined sources11
Helixi182 – 184Combined sources3
Turni185 – 187Combined sources3
Beta strandi188 – 195Combined sources8
Helixi199 – 201Combined sources3
Beta strandi202 – 205Combined sources4
Beta strandi208 – 214Combined sources7
Beta strandi216 – 218Combined sources3
Helixi236 – 243Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJ8X-ray1.55A78-217[»]
1JK9X-ray2.90B/D1-249[»]
1QUPX-ray1.80A/B2-223[»]
ProteinModelPortaliP40202.
SMRiP40202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40202.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 70HMAPROSITE-ProRule annotationAdd BLAST64

Sequence similaritiesi

Belongs to the CCS1 family.Curated
Contains 1 HMA domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00810000126870.
HOGENOMiHOG000263450.
InParanoidiP40202.
KOiK04569.
OMAiDNDKMVC.
OrthoDBiEOG092C5MKI.

Family and domain databases

CDDicd00371. HMA. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024142. Ccs1.
IPR006121. HMA_dom.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF27. PTHR10003:SF27. 1 hit.
PfamiPF00403. HMA. 1 hit.
PF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
SSF55008. SSF55008. 1 hit.
PROSITEiPS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTNDTYEAT YAIPMHCENC VNDIKACLKN VPGINSLNFD IEQQIMSVES
60 70 80 90 100
SVAPSTIINT LRNCGKDAII RGAGKPNSSA VAILETFQKY TIDQKKDTAV
110 120 130 140 150
RGLARIVQVG ENKTLFDITV NGVPEAGNYH ASIHEKGDVS KGVESTGKVW
160 170 180 190 200
HKFDEPIECF NESDLGKNLY SGKTFLSAPL PTWQLIGRSF VISKSLNHPE
210 220 230 240
NEPSSVKDYS FLGVIARSAG VWENNKQVCA CTGKTVWEER KDALANNIK
Length:249
Mass (Da):27,330
Last modified:February 1, 1995 - v1
Checksum:i81DB7E728CDF9366
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17378 Genomic DNA. Translation: AAC49068.1.
Z48502 Genomic DNA. Translation: CAA88404.1.
AY558398 Genomic DNA. Translation: AAS56724.1.
BK006946 Genomic DNA. Translation: DAA09937.1.
PIRiS50245.
RefSeqiNP_013752.1. NM_001182535.1.

Genome annotation databases

EnsemblFungiiYMR038C; YMR038C; YMR038C.
GeneIDi855054.
KEGGisce:YMR038C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17378 Genomic DNA. Translation: AAC49068.1.
Z48502 Genomic DNA. Translation: CAA88404.1.
AY558398 Genomic DNA. Translation: AAS56724.1.
BK006946 Genomic DNA. Translation: DAA09937.1.
PIRiS50245.
RefSeqiNP_013752.1. NM_001182535.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJ8X-ray1.55A78-217[»]
1JK9X-ray2.90B/D1-249[»]
1QUPX-ray1.80A/B2-223[»]
ProteinModelPortaliP40202.
SMRiP40202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35210. 177 interactors.
DIPiDIP-4507N.
IntActiP40202. 2 interactors.
MINTiMINT-429630.

PTM databases

iPTMnetiP40202.

Proteomic databases

MaxQBiP40202.
PRIDEiP40202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR038C; YMR038C; YMR038C.
GeneIDi855054.
KEGGisce:YMR038C.

Organism-specific databases

EuPathDBiFungiDB:YMR038C.
SGDiS000004641. CCS1.

Phylogenomic databases

GeneTreeiENSGT00810000126870.
HOGENOMiHOG000263450.
InParanoidiP40202.
KOiK04569.
OMAiDNDKMVC.
OrthoDBiEOG092C5MKI.

Enzyme and pathway databases

BioCyciYEAST:G3O-32743-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiP40202.
PROiP40202.

Family and domain databases

CDDicd00371. HMA. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024142. Ccs1.
IPR006121. HMA_dom.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF27. PTHR10003:SF27. 1 hit.
PfamiPF00403. HMA. 1 hit.
PF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
SSF55008. SSF55008. 1 hit.
PROSITEiPS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCCS1_YEAST
AccessioniPrimary (citable) accession number: P40202
Secondary accession number(s): D6VZL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 157 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 12000 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.