A0A9P5W2Z3 · A0A9P5W2Z3_9FUNG
- ProteinEndonuclease III homolog
- GeneNTH1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids902 (go to sequence)
- Protein existenceInferred from homology
- 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
Protein has several cofactor binding sites:
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 | 704 | Nucleophile; for N-glycosylase activity | ||||
Sequence: K | ||||||
Site | 723 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 774 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 781 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 784 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 790 | [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 | DNA binding | |
Molecular Function | DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | lyase activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity | |
Molecular Function | phosphoprotein phosphatase 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 homolog
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mortierellomycotina > Mortierellomycetes > Mortierellales > Mortierellaceae > Mortierella
Accessions
- Primary accessionA0A9P5W2Z3
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 40-67 | Disordered | ||||
Sequence: GDSRTGPLQDLNSLPSETSFPVSTPSSL | ||||||
Compositional bias | 45-67 | Polar residues | ||||
Sequence: GPLQDLNSLPSETSFPVSTPSSL | ||||||
Domain | 105-174 | Ubiquitin-like | ||||
Sequence: ISLTAQWNGKKLPFEVDLDYTVGELKNKLMELTNVEPKRQKLMLVRGKLPEDHVVLSTLQLKNNQTFLMM | ||||||
Domain | 231-394 | FCP1 homology | ||||
Sequence: LRPGKRLLVLDLDYTLIDCKALNSPLGDVMRPYLHEFLTDCYRHYDIVIWSQTSWKALEAKVTTIGLLTHPDYKISFVMDITSMFYVISQRDGKPFRHQVKALDIIWEKFPQYSARNTVHIDDLSRNFAMNPKSGLKIGAYKNGAMSRHSDRELYHLARYLVDI | ||||||
Region | 522-560 | Disordered | ||||
Sequence: AAEKRSKRNSATTTGNAAKRIKSEEQDEPGLDGQAKIKR | ||||||
Compositional bias | 541-560 | Basic and acidic residues | ||||
Sequence: RIKSEEQDEPGLDGQAKIKR | ||||||
Compositional bias | 857-874 | Basic and acidic residues | ||||
Sequence: DKVEAEVKEEEQGDAIGH | ||||||
Region | 857-886 | Disordered | ||||
Sequence: DKVEAEVKEEEQGDAIGHGIKLHGRGSSVD |
Sequence similarities
Belongs to the Nth/MutY family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length902
- Mass (Da)100,435
- Last updated2023-09-13 v1
- ChecksumE25672DA3CFE5065
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 45-67 | Polar residues | ||||
Sequence: GPLQDLNSLPSETSFPVSTPSSL | ||||||
Compositional bias | 541-560 | Basic and acidic residues | ||||
Sequence: RIKSEEQDEPGLDGQAKIKR | ||||||
Compositional bias | 857-874 | Basic and acidic residues | ||||
Sequence: DKVEAEVKEEEQGDAIGH |
Keywords
- Technical term