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

4 structures for O80358

Entry ID Method Resolution Chain Position Source
3TWK X-ray 230 A A/B 1-281 PDB
3TWL X-ray 170 A A 1-304 PDB
3TWM X-ray 280 A A/B 1-304 PDB
AF-O80358-F1 Predicted AlphaFoldDB

38 variants for O80358

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH13533785 13 A>V No 1000Genomes
tmp_1_19560169_T_C 43 F>L No 1000Genomes
tmp_1_19560224_A_C 61 N>T No 1000Genomes
tmp_1_19560707_T_C 82 I>T No 1000Genomes
tmp_1_19560743_G_C 94 R>T No 1000Genomes
ENSVATH04945220 162 E>K No 1000Genomes
ENSVATH13533823 164 L>F No 1000Genomes
ENSVATH13533824 165 A>T No 1000Genomes
tmp_1_19561248_C_T 173 P>S No 1000Genomes
tmp_1_19561708_A_C 203 T>P No 1000Genomes
tmp_1_19561734_A_C 211 Q>H No 1000Genomes
ENSVATH00094502 216 H>Y No 1000Genomes
tmp_1_19561751_C_A 217 T>K No 1000Genomes
ENSVATH04945226 219 I>V No 1000Genomes
tmp_1_19561759_A_G 220 K>E No 1000Genomes
tmp_1_19561760_A_T 220 K>I No 1000Genomes
ENSVATH01356803 239 Y>N No 1000Genomes
tmp_1_19562108_G_A 240 W>* No 1000Genomes
tmp_1_19562528_C_G 282 D>E No 1000Genomes
tmp_1_19562526_G_A 282 D>N No 1000Genomes
tmp_1_19562530_C_T 283 A>V No 1000Genomes
ENSVATH04945239 291 P>L No 1000Genomes
ENSVATH04945241 309 E>A No 1000Genomes
ENSVATH04945242 315 E>K No 1000Genomes
ENSVATH01356805 321 S>L No 1000Genomes
ENSVATH04945243 323 K>N No 1000Genomes
tmp_1_19562685_C_T 335 P>S No 1000Genomes
tmp_1_19562689_C_G 336 A>G No 1000Genomes
tmp_1_19562692_C_T 337 S>L No 1000Genomes
ENSVATH13533897 341 T>I No 1000Genomes
tmp_1_19562706_G_C 342 E>Q No 1000Genomes
ENSVATH14298791 346 D>H No 1000Genomes
tmp_1_19562731_A_G 350 D>G No 1000Genomes
tmp_1_19562736_G_A 352 E>K No 1000Genomes
ENSVATH13533898 369 I>M No 1000Genomes
ENSVATH04945244 372 K>M No 1000Genomes
ENSVATH01356806 385 P>L No 1000Genomes
tmp_1_19562847_A_G 389 K>E No 1000Genomes

No associated diseases with O80358

No regional properties for O80358

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O80358

Functions

Description
EC Number 3.2.2.23 Hydrolyzing N-glycosyl compounds
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

6 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.
DNA N-glycosylase activity Catalysis of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site.
DNA-(apurinic or apyrimidinic site) endonuclease activity Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
oxidized purine nucleobase lesion DNA N-glycosylase activity Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate 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 apurinic (AP) site.
zinc ion binding Binding to a zinc ion (Zn).

3 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.
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPELPEVEAA RRAIEENCLG KKIKRVIIAD DNKVIHGISP SDFQTSILGK TIISARRKGK
70 80 90 100 110 120
NLWLELDSPP FPSFQFGMAG AIYIKGVAVT KYKRSAVKDS EEWPSKYSKF FVELDDGLEL
130 140 150 160 170 180
SFTDKRRFAK VRLLANPTSV SPISELGPDA LLEPMTVDEF AESLAKKKIT IKPLLLDQGY
190 200 210 220 230 240
ISGIGNWIAD EVLYQARIHP LQTASSLSKE QCEALHTSIK EVIEKAVEVD ADSSQFPSYW
250 260 270 280 290 300
IFHNREKKPG KAFVDGKKID FITAGGRTTA YVPELQKLYG KDAEKAAKVR PAKRGVKPKE
310 320 330 340 350 360
DDGDGEEDEQ ETEKEDESAK SKKGQKPRGG RGKKPASKTK TEESDDDGDD SEAEEEVVKP
370 380
KGRGTKPAIK RKSEEKATSQ AGKKPKGRKS