H9EXT7 · H9EXT7_MACMU
- ProteinEndonuclease III-like protein 1
- GeneNTHL1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids312 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
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.
Catalytic activity
- 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
Cofactor
Note: 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.
Features
Showing features for active site, site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 220 | Nucleophile; for N-glycosylase activity | ||||
Sequence: K | ||||||
Site | 239 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 290 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 297 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 300 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 306 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | DNA binding | |
Molecular Function | endonuclease activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity | |
Biological Process | base-excision repair, AP site formation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEndonuclease III-like protein 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionH9EXT7
Subcellular Location
Interaction
Subunit
Interacts with YBX1.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MCSPQESGMNSLSARMLT | ||||||
Region | 1-61 | Disordered | ||||
Sequence: MCSPQESGMNSLSARMLTRNRSLRPRAGPRGCGEEPAPPRRGEAAAEARKSHSPVKRRRKA | ||||||
Compositional bias | 36-51 | Basic and acidic residues | ||||
Sequence: PAPPRRGEAAAEARKS | ||||||
Domain | 138-288 | HhH-GPD | ||||
Sequence: LSSQTKDQVTAGAMQRLRAQGLTVDSILQTDDATLGKLIYPVGFWRSKVKYIKQTSTILQQRYGGDIPASVAELVALPGVGPKMAHLAMAVAWGTVSGIAVDTHVHRIANRLRWTKKATKSPEETRAALEEWLPRELWHEINGLLVGFGQQ |
Sequence similarities
Belongs to the Nth/MutY family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length312
- Mass (Da)34,524
- Last updated2012-05-16 v1
- ChecksumADA75479CA197264
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MCSPQESGMNSLSARMLT | ||||||
Compositional bias | 36-51 | Basic and acidic residues | ||||
Sequence: PAPPRRGEAAAEARKS |