A9MJM8
Gene name |
nei |
Protein name |
Endonuclease 8 |
Names |
DNA glycosylase/AP lyase Nei, DNA-(apurinic or apyrimidinic site) lyase Nei, Endonuclease VIII |
Species |
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) |
KEGG Pathway |
ses:SARI_02219 |
EC number |
4.2.99.18: Other carbon-oxygen lyases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A9MJM8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A9MJM8-F1 | Predicted | AlphaFoldDB |
No variants for A9MJM8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A9MJM8 | |||||
No associated diseases with A9MJM8
6 regional properties for A9MJM8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, DNA glycosylase/AP lyase-type | 229 - 263 | IPR000214 |
| domain | Zinc finger, FPG/IleRS-type | 235 - 263 | IPR010663 |
| domain | Formamidopyrimidine-DNA glycosylase, catalytic domain | 1 - 111 | IPR012319 |
| domain | DNA glycosylase/AP lyase, H2TH DNA-binding | 126 - 221 | IPR015886 |
| binding_site | DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site | 238 - 262 | IPR015887 |
| domain | Nei, N-terminal | 2 - 116 | IPR044091 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.99.18 | Other carbon-oxygen lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| class I DNA-(apurinic or apyrimidinic site) endonuclease activity | Catalysis of the cleavage of an AP site 3' of the baseless site by a beta-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate. |
| damaged DNA binding | Binding to damaged DNA. |
| oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity | Catalysis of the removal oxidized pyrimidine bases by cleaving the N-C1' glycosidic bond between the oxidized pyrimidine and the deoxyribose sugar. The reaction involves formation of a covalent enzyme-pyrimidine base intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apyrimidinic (AP) site. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| base-excision repair | In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPEGPEIRRA | ADHLEAAIKG | KLLTDVWFAF | AQLKPYESQL | TGQMVTRIET | RGKALLTHFS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NGLTLYSHNQ | LYGVWRVIDT | GEIPHTTRIL | RVRLQTADKT | ILLYSASDIE | MLTAEQLTTH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PFLQRVGPDV | LDARLTPEEV | KARLLSPRFR | NRQFSGLLLD | QAFLAGLGNY | LRVEILWQSE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LTGQHKAKDL | SEAQLNTLSH | ALLDIPRLSY | ATRGQTDENK | HHGAQFRFKV | FHRDGEACER |
| 250 | 260 | ||||
| CGGIIEKTTL | SSRPFYWCPH | CQK |