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Protein

Endonuclease III homolog 1

Gene

NTG1

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

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines, but also purine-derived lesions, alkylation damage and cytosine photoproducts generated by UV irradiation as well as abasic sites. Has also 8-oxoguanine DNA glycosylase activity. The AP lyase can incise AP sites opposite all four bases. May also play a role in the regulation of mtDNA copy number by introducing a double-stranded break (DSB) at the mtDNA replication origin ori5, initiating the rolling-circle mtDNA replication.UniRule annotation13 Publications

Catalytic activityi

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.UniRule annotation3 Publications

Kineticsi

  1. KM=227 nM for dihydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  2. KM=250 nM for 5-hydroxy-6-hydrothymine containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  3. KM=721 nM for 5-hydroxy-6-hydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  4. KM=755 nM for 5-hydroxy-5-methylhydantoin containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  5. KM=997 nM for 5-hydroxyuracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  6. KM=1380 nM for 5-hydroxycytosine containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  7. KM=3250 nM for thymine glycol containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  8. KM=1305 nM for 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyAde) containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  9. KM=2460 nM for 4,6-diamino-5-formamidopyrimidine (FapyGua) containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  10. KM=24.86 nM for AP/G abasic-site containing duplex oligonucleotides (AP lyase activity)3 Publications
  11. KM=11.37 nM for AP/A abasic-site containing duplex oligonucleotides (AP lyase activity)3 Publications
  12. KM=6.67 nM for AP/T abasic-site containing duplex oligonucleotides (AP lyase activity)3 Publications
  13. KM=36.58 nM for AP/C abasic-site containing duplex oligonucleotides (AP lyase activity)3 Publications
  1. Vmax=1.9 nmol/min/ng enzyme for dihydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei243Nucleophile; for N-glycosylase activityUniRule annotation1
Sitei262Important for catalytic activityUniRule annotation1

GO - Molecular functioni

  • DNA-(apurinic or apyrimidinic site) lyase activity Source: SGD
  • DNA binding Source: UniProtKB-HAMAP
  • oxidized purine nucleobase lesion DNA N-glycosylase activity Source: SGD
  • oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity Source: SGD

GO - Biological processi

  • base-excision repair Source: SGD
  • base-excision repair, AP site formation Source: SGD
  • cellular response to oxidative stress Source: SGD
  • DNA repair Source: SGD
  • nucleotide-excision repair, DNA incision, 5'-to lesion Source: GO_Central
  • positive regulation of mitochondrial DNA replication Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciYEAST:G3O-28827-MONOMER.
ReactomeiR-SCE-110329. Cleavage of the damaged pyrimidine.
R-SCE-110357. Displacement of DNA glycosylase by APEX1.

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease III homolog 1UniRule annotation (EC:3.2.2.-UniRule annotation, EC:4.2.99.18UniRule annotation)
Alternative name(s):
Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1UniRule annotation
Short name:
DNA glycosylase/AP lyase 1UniRule annotation
Endonuclease III-like glycosylase 1
Redoxyendonuclease 1
Gene namesi
Name:NTG1UniRule annotation
Synonyms:OGG2, SCR1
Ordered Locus Names:YAL015C
ORF Names:FUN33
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL015C.
SGDiS000000013. NTG1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Greatly increases spontaneous and hydrogen peroxide-induced mutation frequency. Causes mitochondrial genome instability. Suppresses mitochondrial point mutation rates, frameshifts and recombination rates, probably because NTG1 can generate mutagenic intermediates in yeast mitochondrial DNA.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3 – 6KISK → EISE in NTG1(mts); reduces mitochondrial localization by 40%. 1 Publication4
Mutagenesisi15 – 16KR → AA in NTG1(nls1); reduces nuclear localization by 60%. 1 Publication2
Mutagenesisi33 – 34KR → AA in NTG1(nls2); reduces nuclear localization by 60%. 1 Publication2
Mutagenesisi243K → Q: Abolishes cleavage of substrate oligonucleotides. 1 Publication1
Mutagenesisi364K → R: Cannot properly relocalize in response to oxidative stress. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 26MitochondrionUniRule annotationAdd BLAST26
ChainiPRO_000000174427 – 399Endonuclease III homolog 1Add BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated

Post-translational modificationi

Monosumoylated. Sumoylation is associated with targeting of NTG1 to nuclei containing oxidative DNA damage.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP31378.
PRIDEiP31378.
TopDownProteomicsiP31378.

Expressioni

Inductioni

By oxidizing agents.3 Publications

Interactioni

Protein-protein interaction databases

BioGridi31751. 41 interactors.
DIPiDIP-6614N.
MINTiMINT-673918.

Structurei

3D structure databases

ProteinModelPortaliP31378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini223 – 247HhHUniRule annotationAdd BLAST25

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi14 – 37Bipartite nuclear localization signalSequence analysisAdd BLAST24

Sequence similaritiesi

Belongs to the Nth/MutY family.UniRule annotation
Contains 1 HhH domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00510000047513.
HOGENOMiHOG000252209.
InParanoidiP31378.
KOiK10773.
OMAiFGQVICM.
OrthoDBiEOG092C3TX5.

Family and domain databases

CDDicd00056. ENDO3c. 1 hit.
Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPiMF_03183. Endonuclease_III_Nth. 1 hit.
InterProiIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR030841. NTH1.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
PROSITEiPS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31378-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKISKYSSM AILRKRPLVK TETGPESELL PEKRTKIKQE EVVPQPVDID
60 70 80 90 100
WVKSLPNKQY FEWIVVRNGN VPNRWATPLD PSILVTPAST KVPYKFQETY
110 120 130 140 150
ARMRVLRSKI LAPVDIIGGS SIPVTVASKC GISKEQISPR DYRLQVLLGV
160 170 180 190 200
MLSSQTKDEV TAMAMLNIMR YCIDELHSEE GMTLEAVLQI NETKLDELIH
210 220 230 240 250
SVGFHTRKAK YILSTCKILQ DQFSSDVPAT INELLGLPGV GPKMAYLTLQ
260 270 280 290 300
KAWGKIEGIC VDVHVDRLTK LWKWVDAQKC KTPDQTRTQL QNWLPKGLWT
310 320 330 340 350
EINGLLVGFG QIITKSRNLG DMLQFLPPDD PRSSLDWDLQ SQLYKEIQQN
360 370 380 390
IMSYPKWVKY LEGKRELNVE AEINVKHEEK TVEETMVKLE NDISVKVED
Length:399
Mass (Da):45,577
Last modified:July 1, 1993 - v1
Checksum:iA3C878A3004908F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05146 Genomic DNA. Translation: AAC04942.1.
BK006935 Genomic DNA. Translation: DAA06973.1.
PIRiS36719.
RefSeqiNP_009387.1. NM_001178160.1.

Genome annotation databases

EnsemblFungiiYAL015C; YAL015C; YAL015C.
GeneIDi851218.
KEGGisce:YAL015C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05146 Genomic DNA. Translation: AAC04942.1.
BK006935 Genomic DNA. Translation: DAA06973.1.
PIRiS36719.
RefSeqiNP_009387.1. NM_001178160.1.

3D structure databases

ProteinModelPortaliP31378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31751. 41 interactors.
DIPiDIP-6614N.
MINTiMINT-673918.

Proteomic databases

MaxQBiP31378.
PRIDEiP31378.
TopDownProteomicsiP31378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL015C; YAL015C; YAL015C.
GeneIDi851218.
KEGGisce:YAL015C.

Organism-specific databases

EuPathDBiFungiDB:YAL015C.
SGDiS000000013. NTG1.

Phylogenomic databases

GeneTreeiENSGT00510000047513.
HOGENOMiHOG000252209.
InParanoidiP31378.
KOiK10773.
OMAiFGQVICM.
OrthoDBiEOG092C3TX5.

Enzyme and pathway databases

BioCyciYEAST:G3O-28827-MONOMER.
ReactomeiR-SCE-110329. Cleavage of the damaged pyrimidine.
R-SCE-110357. Displacement of DNA glycosylase by APEX1.

Miscellaneous databases

PROiP31378.

Family and domain databases

CDDicd00056. ENDO3c. 1 hit.
Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPiMF_03183. Endonuclease_III_Nth. 1 hit.
InterProiIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR030841. NTH1.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
PROSITEiPS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNTH1_YEAST
AccessioniPrimary (citable) accession number: P31378
Secondary accession number(s): D6VPK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Does not possess a consensus sequence for a C-terminal iron-sulfur center typical of all other endonuclease III homologs.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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