F5HI85

PR
Gene name
UL114
Protein name
Uracil-DNA glycosylase
Names
UDG, UNG
Species
Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
KEGG Pathway
vg:3077539
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)

71-146 (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 F5HI85

Entry ID Method Resolution Chain Position Source

No variants for F5HI85

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for F5HI85

No associated diseases with F5HI85

2 regional properties for F5HI85

Type Name Position InterPro Accession
domain Uracil-DNA glycosylase-like 76 - 236 IPR005122
active_site Uracil-DNA glycosylase, active site 84 - 93 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
MALKQWMLAN IADNKGSLLT PDEQARVFCL SADWIRFLSL PDHDTVLLRD TVAAVEGARQ
70 80 90 100 110 120
LEMVYPAPEH VHRWSYLCPP EQVRVVIVGQ DPYCDGSASG LAFGTLAGRP PPPSLNNVFR
130 140 150 160 170 180
ELARTVDGFQ RPASGCLDAW ARRGVLLLNT VFTVVHGQPG SHRHLGWQTL SNHVIRRLSE
190 200 210 220 230 240
RREHLVFMLW GADAHTCEYL IDRRRHLVLK SCHPSPRNTT RAFVGNDHFI LANAYLDTHY
RETMDWRLCG