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Protein

Uracil-DNA glycosylase

Gene

UNG

Organism
Vaccinia virus (strain Ankara) (VACV)
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.

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

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
Ordered Locus Names:MVA101R, ACAM3000_MVA_101
OrganismiVaccinia virus (strain Ankara) (VACV)
Taxonomic identifieri126794 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi179G → R: Defective DNA replication, reduced ability to interact with A20. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001761791 – 218Uracil-DNA glycosylaseAdd BLAST218

Interactioni

Subunit structurei

Homodimer. 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 similarity).By similarity

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi12 – 14Combined sources3
Helixi17 – 22Combined sources6
Helixi23 – 37Combined sources15
Beta strandi42 – 44Combined sources3
Helixi46 – 48Combined sources3
Helixi51 – 54Combined sources4
Beta strandi62 – 68Combined sources7
Turni71 – 73Combined sources3
Helixi87 – 100Combined sources14
Beta strandi106 – 108Combined sources3
Helixi110 – 112Combined sources3
Beta strandi116 – 123Combined sources8
Turni130 – 133Combined sources4
Helixi134 – 149Combined sources16
Beta strandi153 – 158Combined sources6
Turni160 – 165Combined sources6
Helixi166 – 170Combined sources5
Beta strandi173 – 179Combined sources7
Helixi185 – 187Combined sources3
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[»]
3NT7X-ray2.40A/C1-218[»]
4DOFX-ray2.80A/B/C/D1-218[»]
4DOGX-ray2.30A1-218[»]
4IRBX-ray2.30A/B/C/D1-218[»]
4LZBX-ray2.03A/B/C/D/E/F/G/H/I/J/K/L1-218[»]
4QC9X-ray2.26A/B/C/D1-218[»]
4QCAX-ray1.90A/B/C/D1-218[»]
5JX3X-ray2.30A/B/C/D/E/F/G/H1-218[»]
ProteinModelPortaliQ91UM2.
SMRiQ91UM2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91UM2.

Family & Domainsi

Sequence similaritiesi

Belongs to the uracil-DNA glycosylase family.Curated

Phylogenomic databases

KOiK03648.

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.

Q91UM2-1 [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 TDFSNIRAKL ESPVTTIVGY HPAARDRQFE KDRSFEIINV
210
LLELDNKAPI NWAQGFIY
Length:218
Mass (Da):25,052
Last modified:December 1, 2001 - v1
Checksum:i6A419624A912B97F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94848 Genomic DNA. Translation: AAB96513.1.
AY603355 Genomic DNA. Translation: AAT10499.1.
PIRiT37377.
RefSeqiYP_232991.1. NC_006998.1.

Genome annotation databases

GeneIDi3707565.
KEGGivg:3707565.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94848 Genomic DNA. Translation: AAB96513.1.
AY603355 Genomic DNA. Translation: AAT10499.1.
PIRiT37377.
RefSeqiYP_232991.1. NC_006998.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OWQX-ray2.40A/B1-218[»]
3NT7X-ray2.40A/C1-218[»]
4DOFX-ray2.80A/B/C/D1-218[»]
4DOGX-ray2.30A1-218[»]
4IRBX-ray2.30A/B/C/D1-218[»]
4LZBX-ray2.03A/B/C/D/E/F/G/H/I/J/K/L1-218[»]
4QC9X-ray2.26A/B/C/D1-218[»]
4QCAX-ray1.90A/B/C/D1-218[»]
5JX3X-ray2.30A/B/C/D/E/F/G/H1-218[»]
ProteinModelPortaliQ91UM2.
SMRiQ91UM2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3707565.
KEGGivg:3707565.

Phylogenomic databases

KOiK03648.

Miscellaneous databases

EvolutionaryTraceiQ91UM2.

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_VACCA
AccessioniPrimary (citable) accession number: Q91UM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.