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Protein

Uracil-DNA glycosylase

Gene

UNG

Organism
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA (By similarity).By similarity1 Publication

Catalytic activityi

Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei68 – 681Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Uracil-DNA glycosylase (EC:3.2.2.27)
Short name:
UDG
Gene namesi
Name:UNG
Synonyms:TS17
Ordered Locus Names:VACWR109
ORF Names:D4R
OrganismiVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Taxonomic identifieri10254 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000000344 Componenti: Genome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1772931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Uracil-DNA glycosylasePRO_0000176181Add
BLAST

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with protein A20. Component of the Uracil-DNA glycosylase(UDG)-A20-polymerase complex; A20 and UDG form a heterodimeric processivity factor that associates with E9 to form the processive polymerase holoenzyme.By similarity2 Publications

Protein-protein interaction databases

DIPiDIP-2182N.
IntActiP04303. 1 interaction.
MINTiMINT-131069.

Chemistry

BindingDBiP04303.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi12 – 154Combined sources
Helixi17 – 193Combined sources
Helixi20 – 3718Combined sources
Beta strandi42 – 443Combined sources
Helixi46 – 483Combined sources
Helixi51 – 544Combined sources
Beta strandi62 – 687Combined sources
Turni71 – 733Combined sources
Helixi87 – 10014Combined sources
Beta strandi106 – 1083Combined sources
Helixi110 – 1123Combined sources
Beta strandi116 – 1238Combined sources
Turni130 – 1334Combined sources
Helixi134 – 14916Combined sources
Beta strandi153 – 1586Combined sources
Helixi160 – 1634Combined sources
Helixi166 – 1694Combined sources
Beta strandi175 – 1795Combined sources
Helixi190 – 20415Combined sources
Helixi212 – 2154Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QCBX-ray2.89A/B1-218[»]
ProteinModelPortaliP04303.
SMRiP04303. Positions 1-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the uracil-DNA glycosylase family.Curated

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiIPR018085. Ura-DNA_Glyclase_AS.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
PROSITEiPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSVTVSHAP YTITYHDDWE PVMSQLVEFY NEVASWLLRD ETSPIPDKFF
60 70 80 90 100
IQLKQPLRNK RVCVCGIDPY PKDGTGVPFE SPNFTKKSIK EIASSISRLT
110 120 130 140 150
GVIDYKGYNL NIIDGVIPWN YYLSCKLGET KSHAIYWDKI SKLLLQHITK
160 170 180 190 200
HVSVLYCLGK TDYSNIRAKL ESPVTTIVGY HPAARDRQFE KDRSFEIINV
210
LLELDNKAPI NWAQGFIY
Length:218
Mass (Da):25,068
Last modified:July 1, 1989 - v2
Checksum:i6541893BA912B968
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631Y → F in AAA48258 (PubMed:3739227).Curated
Sequence conflicti163 – 1631Y → F in AAO89388 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15058 Genomic DNA. Translation: AAA48258.1.
AY243312 Genomic DNA. Translation: AAO89388.1.
PIRiA93025. QQVZ6.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15058 Genomic DNA. Translation: AAA48258.1.
AY243312 Genomic DNA. Translation: AAO89388.1.
PIRiA93025. QQVZ6.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QCBX-ray2.89A/B1-218[»]
ProteinModelPortaliP04303.
SMRiP04303. Positions 1-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-2182N.
IntActiP04303. 1 interaction.
MINTiMINT-131069.

Chemistry

BindingDBiP04303.
ChEMBLiCHEMBL1772931.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiIPR018085. Ura-DNA_Glyclase_AS.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
PROSITEiPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUNG_VACCW
AccessioniPrimary (citable) accession number: P04303
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: July 1, 1989
Last modified: December 9, 2015
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.