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Protein

Endonuclease III homolog 2

Gene

NTG2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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 as well as abasic sites. Can also repair the oxidation products of 8-oxoguanine.UniRule annotation10 Publications

Miscellaneous

Present with 125 molecules/cell in log phase SD medium.1 Publication

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 annotation1 Publication

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.UniRule annotation

Kineticsi

  1. KM=160 nM for dihydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  2. KM=178 nM for 5-hydroxy-6-hydrothymine containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  3. KM=557 nM for 5-hydroxy-6-hydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  4. KM=431 nM for 5-hydroxyuracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  5. KM=419 nM for 5-hydroxycytosine containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  6. KM=1000 nM for thymine glycol containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  7. KM=824 nM for 2,6-diamino-4-hydroxy-5-formamidopyrimidine FapyAde) containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  8. KM=2529 nM for 4,6-diamino-5-formamidopyrimidine (FapyGua) containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  1. Vmax=0.2 nmol/min/ng enzyme for dihydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei248Nucleophile; for N-glycosylase activityUniRule annotation1
Sitei267Important for catalytic activityUniRule annotation1
Metal bindingi319Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi326Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi329Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi335Iron-sulfur (4Fe-4S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • base-excision repair Source: SGD
  • base-excision repair, AP site formation Source: SGD
  • nucleotide-excision repair, DNA incision, 5'-to lesion Source: GO_Central

Keywordsi

Molecular functionGlycosidase, Hydrolase, Lyase
Biological processDNA damage, DNA repair
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33457-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 2UniRule 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 2UniRule annotation
Short name:
DNA glycosylase/AP lyase 2UniRule annotation
Endonuclease III-like glycosylase 2
Redoxyendonuclease 2
Gene namesi
Name:NTG2
Synonyms:SCR2
Ordered Locus Names:YOL043C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL043C
SGDiS000005403 NTG2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Greatly increases spontaneous and hydrogen peroxide-induced mutation frequency.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24S → A: Abolishes interaction with MLH1. 1 Publication1
Mutagenesisi26Y → A: Abolishes interaction with MLH1. 1 Publication1
Mutagenesisi27F → A: Abolishes interaction with MLH1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001022381 – 380Endonuclease III homolog 2Add BLAST380

Amino acid modifications

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

Post-translational modificationi

Monosumoylated.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ08214
PaxDbiQ08214
PRIDEiQ08214
TopDownProteomicsiQ08214

Expressioni

Inductioni

Constitutively expressed.2 Publications

Interactioni

Subunit structurei

Interacts with MLH1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MLH1P389203EBI-12303,EBI-11003

Protein-protein interaction databases

BioGridi34359, 158 interactors
DIPiDIP-2956N
IntActiQ08214, 9 interactors
MINTiQ08214
STRINGi4932.YOL043C

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FMNX-ray2.69C22-29[»]
ProteinModelPortaliQ08214
SMRiQ08214
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini228 – 252HhHUniRule annotationAdd BLAST25

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni15 – 40Interaction with MLH11 PublicationAdd BLAST26

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi8 – 12Nuclear localization signalSequence analysis5
Motifi376 – 380Nuclear localization signalSequence analysis5

Sequence similaritiesi

Belongs to the Nth/MutY family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000047513
HOGENOMiHOG000252209
InParanoidiQ08214
KOiK10773
OMAiDAKKCKT
OrthoDBiEOG092C3TX5

Family and domain databases

CDDicd00056 ENDO3c, 1 hit
Gene3Di1.10.1670.10, 1 hit
HAMAPiMF_03183 Endonuclease_III_Nth, 1 hit
InterProiView protein in InterPro
IPR011257 DNA_glycosylase
IPR004036 Endonuclease-III-like_CS2
IPR003651 Endonuclease3_FeS-loop_motif
IPR003265 HhH-GPD_domain
IPR023170 HTH_base_excis_C
IPR030841 NTH1
PfamiView protein in Pfam
PF00730 HhH-GPD, 1 hit
SMARTiView protein in SMART
SM00478 ENDO3c, 1 hit
SM00525 FES, 1 hit
SUPFAMiSSF48150 SSF48150, 1 hit
PROSITEiView protein in PROSITE
PS01155 ENDONUCLEASE_III_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q08214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREESRSRKR KHIPVDIEEV EVRSKYFKKN ERTVELVKEN KINKDLQNYG
60 70 80 90 100
GVNIDWIKAL KPIEYFEWIE SRTCDDPRTW GRPITKEEMI NDSGAKVPES
110 120 130 140 150
FLPIYNRVRL MRSKVKTPVD AMGCSMIPVL VSNKCGIPSE KVDPKNFRLQ
160 170 180 190 200
FLIGTMLSAQ TRDERMAQAA LNITEYCLNT LKIAEGITLD GLLKIDEPVL
210 220 230 240 250
ANLIRCVSFY TRKANFIKRT AQLLVDNFDS DIPYDIEGIL SLPGVGPKMG
260 270 280 290 300
YLTLQKGWGL IAGICVDVHV HRLCKMWNWV DPIKCKTAEH TRKELQVWLP
310 320 330 340 350
HSLWYEINTV LVGFGQLICM ARGKRCDLCL ANDVCNARNE KLIESSKFHQ
360 370 380
LEDKEDIEKV YSHWLDTVTN GITTERHKKK
Length:380
Mass (Da):43,844
Last modified:November 1, 1996 - v1
Checksum:i517F81C3BA3DDCF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74785 Genomic DNA Translation: CAA99045.1
BK006948 Genomic DNA Translation: DAA10739.1
PIRiS66728
RefSeqiNP_014599.1, NM_001183297.1

Genome annotation databases

EnsemblFungiiYOL043C; YOL043C; YOL043C
GeneIDi854114
KEGGisce:YOL043C

Similar proteinsi

Entry informationi

Entry nameiNTH2_YEAST
AccessioniPrimary (citable) accession number: Q08214
Secondary accession number(s): D6W223
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 150 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health