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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)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
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi179 – 1791G → R: Defective DNA replication, reduced ability to interact with A20. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Uracil-DNA glycosylasePRO_0000176179Add
BLAST

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

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi7 – 104Combined 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 – 14815Combined sources
Turni149 – 1513Combined sources
Beta strandi153 – 1586Combined sources
Helixi160 – 16910Combined sources
Beta strandi172 – 1798Combined sources
Helixi185 – 1917Combined sources
Helixi194 – 20411Combined sources
Helixi212 – 2154Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OWQX-ray2.40A/B1-218[»]
2OWRX-ray2.30A/B/C/D/E/F/G/H1-218[»]
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[»]
ProteinModelPortaliQ91UM2.
SMRiQ91UM2. Positions 1-218.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
2OWQX-ray2.40A/B1-218[»]
2OWRX-ray2.30A/B/C/D/E/F/G/H1-218[»]
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[»]
ProteinModelPortaliQ91UM2.
SMRiQ91UM2. Positions 1-218.
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: October 14, 2015
This is version 60 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.