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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)DescriptionActionsGraphical viewLength
Active sitei68Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Glycosidase, Hydrolase
Biological processDNA damage, DNA repair

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 databases

ChEMBLiCHEMBL1772931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001761811 – 218Uracil-DNA glycosylaseAdd BLAST218

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 interactor.
MINTiMINT-131069.

Chemistry databases

BindingDBiP04303.

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Beta strandi8 – 10Combined sources3
Beta strandi12 – 15Combined sources4
Helixi17 – 22Combined sources6
Helixi23 – 37Combined sources15
Beta strandi42 – 44Combined sources3
Helixi46 – 48Combined sources3
Helixi51 – 54Combined sources4
Beta strandi62 – 68Combined sources7
Beta strandi71 – 73Combined sources3
Helixi87 – 100Combined sources14
Beta strandi106 – 108Combined sources3
Helixi110 – 112Combined sources3
Beta strandi116 – 123Combined sources8
Turni130 – 133Combined sources4
Helixi134 – 148Combined sources15
Turni149 – 151Combined sources3
Beta strandi153 – 158Combined sources6
Turni160 – 165Combined sources6
Helixi166 – 170Combined sources5
Beta strandi174 – 179Combined sources6
Helixi188 – 191Combined sources4
Helixi194 – 204Combined sources11
Helixi212 – 215Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OWQX-ray2.40A/B1-218[»]
4QCBX-ray2.89A/B1-218[»]
5JX3X-ray2.30A/B/C/D/E/F/G/H1-218[»]
ProteinModelPortaliP04303.
SMRiP04303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the uracil-DNA glycosylase family.Curated

Phylogenomic databases

OrthoDBiVOG090000PB.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiView protein in InterPro
IPR018085. Ura-DNA_Glyclase_AS.
IPR005122. Uracil-DNA_glycosylase-like.
PfamiView protein in Pfam
PF03167. UDG. 1 hit.
SUPFAMiSSF52141. SSF52141. 1 hit.
PROSITEiView protein in PROSITE
PS00130. U_DNA_GLYCOSYLASE. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti163Y → F in AAA48258 (PubMed:3739227).Curated1
Sequence conflicti163Y → F in AAO89388 (Ref. 3) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OWQX-ray2.40A/B1-218[»]
4QCBX-ray2.89A/B1-218[»]
5JX3X-ray2.30A/B/C/D/E/F/G/H1-218[»]
ProteinModelPortaliP04303.
SMRiP04303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP04303.
ChEMBLiCHEMBL1772931.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG090000PB.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiView protein in InterPro
IPR018085. Ura-DNA_Glyclase_AS.
IPR005122. Uracil-DNA_glycosylase-like.
PfamiView protein in Pfam
PF03167. UDG. 1 hit.
SUPFAMiSSF52141. SSF52141. 1 hit.
PROSITEiView protein in PROSITE
PS00130. U_DNA_GLYCOSYLASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiUNG_VACCW
AccessioniPrimary (citable) accession number: P04303
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: July 1, 1989
Last modified: February 15, 2017
This is version 89 of the entry and version 2 of the sequence. See 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.