P53765

PR
Gene name
46
Protein name
Uracil-DNA glycosylase
Names
UDG, UNG
Species
Equine herpesvirus 2 (strain 86/87) (EHV-2)
KEGG Pathway
vg:1461089
EC number
3.2.2.27: Hydrolyzing N-glycosyl compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-52 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for P53765

Entry ID Method Resolution Chain Position Source

No variants for P53765

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P53765

No associated diseases with P53765

2 regional properties for P53765

Type Name Position InterPro Accession
domain Uracil-DNA glycosylase-like 75 - 241 IPR005122
active_site Uracil-DNA glycosylase, active site 83 - 92 IPR018085

Functions

Description
EC Number 3.2.2.27 Hydrolyzing N-glycosyl compounds
Subcellular Localization
  • Host nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
host cell nucleus A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction.

1 GO annotations of molecular function

Name Definition
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.

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
MERWLQLHVW SKDQQDQDQE HLLDEKIPIN RAWMDFLQMS PFLKRKLVTL LETVAKLRTS
70 80 90 100 110 120
TVVYPGEERV FSWSWLCEPT QVKVIILGQD PYHGGQATGL AFSVSKTDPV PPSLRNIFLE
130 140 150 160 170 180
VSACDSQFAV PLHGCLNNWA RQGVLLLNTI LTVEKGKPGS HSDLGWIWFT NYIISCLSNQ
190 200 210 220 230 240
LDHCVFMLWG SKAIEKASLI NTNKHLVLKS QHPSPLAARS NRPSLWPKFL GCGHFKQANE
250
YLELHGKCPV DWNLD