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Protein

Peroxiredoxin DOT5

Gene

DOT5

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

Has a role in telomere silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes. Also has a role in the regulation of telomere length. Acts as an alkyl-hydroperoxide reductase in the nucleus during post-diauxic growth. Preferentially reduces alkyl-hydroperoxides rather than hydrogen preoxide. Acts as an antioxidant necessary for stationary phase survival.3 Publications

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.2 Publications

pH dependencei

Optimum pH is 6.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei107 – 1071Cysteine sulfenic acid (-SOH) intermediate1 Publication

GO - Molecular functioni

  • thioredoxin peroxidase activity Source: SGD

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:YIL010W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin DOT5 (EC:1.11.1.15)
Alternative name(s):
Disrupter of telomere silencing protein 5
Nuclear thiol peroxidase
Short name:
nTPx
Thioredoxin reductase
Gene namesi
Name:DOT5
Ordered Locus Names:YIL010W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL010W.
SGDiS000001272. DOT5.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB-SubCell
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071C → S: No TPx activity, no effect on DOT activity. 3 Publications
Mutagenesisi112 – 1121C → S: No TPx activity, no effect on DOT activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Peroxiredoxin DOT5PRO_0000135152Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi107 ↔ 112Redox-activePROSITE-ProRule annotation1 Publication

Post-translational modificationi

The Cys-107-SH group is the primary site of oxidation, and the oxidized Cys-107 (probably Cys-SOH) rapidly reacts with Cys-112-SH to form an intramolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme (By similarity).By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP40553.

PTM databases

iPTMnetiP40553.

Expressioni

Inductioni

During the diauxic shift. In response to oxidative stress.1 Publication

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi34980. 33 interactions.
DIPiDIP-4762N.
IntActiP40553. 1 interaction.
MINTiMINT-485714.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi73 – 753Combined sources
Beta strandi81 – 833Combined sources
Helixi84 – 907Combined sources
Beta strandi92 – 987Combined sources
Beta strandi100 – 1045Combined sources
Helixi105 – 12117Combined sources
Turni122 – 1243Combined sources
Beta strandi126 – 1327Combined sources
Helixi135 – 14511Combined sources
Beta strandi148 – 1536Combined sources
Helixi158 – 1636Combined sources
Beta strandi166 – 1716Combined sources
Beta strandi176 – 1816Combined sources
Beta strandi184 – 1918Combined sources
Helixi194 – 21118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A4VX-ray1.80A57-215[»]
ProteinModelPortaliP40553.
SMRiP40553. Positions 59-214.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40553.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 211149ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000022344.
InParanoidiP40553.
KOiK03564.
OMAiVYPRAST.
OrthoDBiEOG092C5CGU.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40553-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEALRRSTR IAISKRMLEE EESKLAPIST PEVPKKKIKT GPKHNANQAV
60 70 80 90 100
VQEANRSSDV NELEIGDPIP DLSLLNEDND SISLKKITEN NRVVVFFVYP
110 120 130 140 150
RASTPGCTRQ ACGFRDNYQE LKKYAAVFGL SADSVTSQKK FQSKQNLPYH
160 170 180 190 200
LLSDPKREFI GLLGAKKTPL SGSIRSHFIF VDGKLKFKRV KISPEVSVND
210
AKKEVLEVAE KFKEE
Length:215
Mass (Da):24,120
Last modified:February 1, 1995 - v1
Checksum:iEB78A216891946C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38113 Genomic DNA. Translation: CAA86239.1.
AY558298 Genomic DNA. Translation: AAS56624.1.
BK006942 Genomic DNA. Translation: DAA08535.1.
PIRiS48445.
RefSeqiNP_012255.3. NM_001179360.3.

Genome annotation databases

EnsemblFungiiYIL010W; YIL010W; YIL010W.
GeneIDi854805.
KEGGisce:YIL010W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38113 Genomic DNA. Translation: CAA86239.1.
AY558298 Genomic DNA. Translation: AAS56624.1.
BK006942 Genomic DNA. Translation: DAA08535.1.
PIRiS48445.
RefSeqiNP_012255.3. NM_001179360.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A4VX-ray1.80A57-215[»]
ProteinModelPortaliP40553.
SMRiP40553. Positions 59-214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34980. 33 interactions.
DIPiDIP-4762N.
IntActiP40553. 1 interaction.
MINTiMINT-485714.

PTM databases

iPTMnetiP40553.

Proteomic databases

MaxQBiP40553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL010W; YIL010W; YIL010W.
GeneIDi854805.
KEGGisce:YIL010W.

Organism-specific databases

EuPathDBiFungiDB:YIL010W.
SGDiS000001272. DOT5.

Phylogenomic databases

HOGENOMiHOG000022344.
InParanoidiP40553.
KOiK03564.
OMAiVYPRAST.
OrthoDBiEOG092C5CGU.

Enzyme and pathway databases

BioCyciYEAST:YIL010W-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40553.
PROiP40553.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDOT5_YEAST
AccessioniPrimary (citable) accession number: P40553
Secondary accession number(s): D6VVR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 148 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 1840 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: 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.