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 O59825

Entry ID Method Resolution Chain Position Source
AF-O59825-F1 Predicted AlphaFoldDB

No variants for O59825

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O59825

No associated diseases with O59825

No regional properties for O59825

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O59825

Functions

Description
EC Number 3.2.2.28 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.

5 GO annotations of molecular function

Name Definition
hypoxanthine DNA N-glycosylase activity DNA N-glycosylase activity acting on deaminated adenine (hypoxanthine).
oxanine DNA N-glycosylase activity DNA N-glycosylase activity acting on deaminated guanine where the resulting base (oxanine) is generated by NO- or HNO2-induced nitrosative deamination.
pyrimidine-specific mismatch base pair DNA N-glycosylase activity Catalysis of the removal of mismatched pyrimidine bases in DNA. Enzymes with this activity recognize and remove pyrimidines present in mismatches 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 apyrimidinic (AP) site.
uracil DNA N-glycosylase activity Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine.
xanthine DNA N-glycosylase activity DNA N-glycosylase activity acting on deaminated guanine (xanthine).

1 GO annotations of biological process

Name Definition
base-excision repair, AP site formation The formation of an AP site, a deoxyribose sugar with a missing base, by DNA glycosylase which recognizes an altered base in DNA and catalyzes its hydrolytic removal. This sugar phosphate is the substrate recognized by the AP endonuclease, which cuts the DNA phosphodiester backbone at the 5' side of the altered site to leave a gap which is subsequently repaired.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNDIETRDTG TKNDNSSEFN LSVKSHKRKR SFDDENLELE ESREETSGGI LKKAKTQSFS
70 80 90 100 110 120
ESLERFRFAH AGSNNEYRKT DVVKNSDTDN GLLKSAVETI TLENGLRNRR VNVTKKSTLK
130 140 150 160 170 180
ASVKKSTLKK KNEVDPALLQ GVPDYICENP YAIIVGLNPG ITSSLKGHAF ASPSNRFWKM
190 200 210 220 230 240
LNKSKLLEGN AEFTYLNDKD LPAHGLGITN LCARPSSSGA DLRKEEMQDG ARILYEKVKR
250 260 270 280 290 300
YRPQVGLFIS GKGIWEEMYK MLTGKKLPKT FVFGWQPEKF GDANVFVGIS SSGRAAGYSD
310 320
EKKQNLWNLF AEEVNRHREI VKHAV