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Protein

Uracil-DNA glycosylase

Gene

UNG

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 2 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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Uracil-DNA glycosylase (EC:3.2.2.27)
Short name:
UDG
Gene namesi
Name:UNG
ORF Names:BKRF3
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007640 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 255255Uracil-DNA glycosylasePRO_0000176183Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP12888. 1 interaction.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 387Combined sources
Helixi42 – 5918Combined sources
Beta strandi64 – 663Combined sources
Turni68 – 725Combined sources
Helixi73 – 753Combined sources
Beta strandi76 – 783Combined sources
Helixi80 – 823Combined sources
Beta strandi85 – 895Combined sources
Beta strandi94 – 963Combined sources
Beta strandi100 – 1034Combined sources
Helixi113 – 12513Combined sources
Helixi138 – 1414Combined sources
Turni142 – 1443Combined sources
Beta strandi145 – 1517Combined sources
Turni159 – 1646Combined sources
Helixi167 – 18115Combined sources
Beta strandi186 – 1916Combined sources
Helixi192 – 1954Combined sources
Helixi196 – 2005Combined sources
Turni203 – 2053Combined sources
Beta strandi206 – 2116Combined sources
Helixi216 – 2205Combined sources
Helixi235 – 24511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J8XX-ray2.30A/C25-255[»]
ProteinModelPortaliP12888.
SMRiP12888. Positions 26-255.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12888.
Q777D9.

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.
HAMAPiMF_00148. UDG.
InterProiIPR018085. Ura-DNA_Glyclase_AS.
IPR002043. Ura_DNA_glycsylse.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERiPTHR11264. PTHR11264. 1 hit.
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SMARTiSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
TIGRFAMsiTIGR00628. ung. 1 hit.
PROSITEiPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRGLDLWL DEHVWKRKQE IGVKGENLLL PDLWLDFLQL SPIFQRKLAA
60 70 80 90 100
VIACVRRLRT QATVYPEEDM CMAWARFCDP SDIKVVILGQ DPYHGGQANG
110 120 130 140 150
LAFSVAYGFP VPPSLRNIYA ELHRSLPEFS PPDHGCLDAW ASQGVLLLNT
160 170 180 190 200
ILTVQKGKPG SHADIGWAWF TDHVISLLSE RLKACVFMLW GAKAGDKASL
210 220 230 240 250
INSKKHLVLT SQHPSPLAQN STRKSAQQKF LGNNHFVLAN NFLREKGLGE

IDWRL
Length:255
Mass (Da):28,605
Last modified:October 1, 1989 - v1
Checksum:iF7A26FB6F674E689
GO

Sequence cautioni

The sequence CAA24818.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24818.1. Different initiation.
AJ507799 Genomic DNA. Translation: CAD53429.1.
RefSeqiYP_401679.1. NC_007605.1.

Genome annotation databases

GeneIDi3783711.
KEGGivg:3783711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24818.1. Different initiation.
AJ507799 Genomic DNA. Translation: CAD53429.1.
RefSeqiYP_401679.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J8XX-ray2.30A/C25-255[»]
ProteinModelPortaliP12888.
SMRiP12888. Positions 26-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12888. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783711.
KEGGivg:3783711.

Phylogenomic databases

KOiK03648.

Miscellaneous databases

EvolutionaryTraceiP12888.
Q777D9.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
HAMAPiMF_00148. UDG.
InterProiIPR018085. Ura-DNA_Glyclase_AS.
IPR002043. Ura_DNA_glycsylse.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERiPTHR11264. PTHR11264. 1 hit.
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SMARTiSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
TIGRFAMsiTIGR00628. ung. 1 hit.
PROSITEiPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "New insights on the role of the gamma-herpesvirus uracil-DNA glycosylase leucine loop revealed by the structure of the Epstein-Barr virus enzyme in complex with an inhibitor protein."
    Geoui T., Buisson M., Tarbouriech N., Burmeister W.P.
    J. Mol. Biol. 366:117-131(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 25-255.

Entry informationi

Entry nameiUNG_EBVB9
AccessioniPrimary (citable) accession number: P12888
Secondary accession number(s): Q777D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 9, 2015
This is version 81 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, 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.