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Protein

Uracil-DNA glycosylase

Gene

UL2

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
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 deamination of cytosine. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly, in terminally differentiated neurons which lack DNA repair enzymes.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei178 – 1781Proton acceptor

GO - Molecular functioni

  1. uracil DNA N-glycosylase activity Source: InterPro

GO - Biological processi

  1. base-excision repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BRENDAi3.2.2.27. 2647.
SABIO-RKP10186.

Names & Taxonomyi

Protein namesi
Recommended name:
Uracil-DNA glycosylase (EC:3.2.2.27)
Short name:
UDG
Alternative name(s):
UNG
Gene namesi
ORF Names:UL2
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000009294 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Uracil-DNA glycosylasePRO_0000176185Add
BLAST

Interactioni

Protein-protein interaction databases

MINTiMINT-1506602.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi108 – 1169Combined sources
Helixi120 – 1223Combined sources
Helixi123 – 1308Combined sources
Helixi133 – 14816Combined sources
Beta strandi151 – 1533Combined sources
Turni155 – 1606Combined sources
Helixi161 – 1644Combined sources
Helixi167 – 1693Combined sources
Beta strandi172 – 1765Combined sources
Turni183 – 1853Combined sources
Beta strandi187 – 1915Combined sources
Helixi201 – 21313Combined sources
Helixi226 – 2305Combined sources
Beta strandi233 – 2397Combined sources
Turni247 – 2526Combined sources
Helixi255 – 26915Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi274 – 2796Combined sources
Helixi280 – 2856Combined sources
Turni290 – 2923Combined sources
Beta strandi293 – 2986Combined sources
Beta strandi305 – 3073Combined sources
Helixi309 – 3113Combined sources
Helixi314 – 32310Combined sources
Turni324 – 3263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LAUX-ray1.80E91-334[»]
1UDGX-ray1.75A91-334[»]
1UDHX-ray1.75A91-334[»]
1UDIX-ray2.70E91-334[»]
2C53X-ray1.80A91-334[»]
2C56X-ray2.10A91-334[»]
4L5NX-ray2.16A/B96-334[»]
SMRiP10186. Positions 107-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10186.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi198 – 2014Poly-Pro

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.

P10186-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRACSRSPS PRRRPSSPRR TPPRDGTPPQ KADADDPTPG ASNDASTETR
60 70 80 90 100
PGSGGEPAAC RSSGPAALLA ALEAGPAGVT FSSSAPPDPP MDLTNGGVSP
110 120 130 140 150
AATSAPLDWT TFRRVFLIDD AWRPLMEPEL ANPLTAHLLA EYNRRCQTEE
160 170 180 190 200
VLPPREDVFS WTRYCTPDEV RVVIIGQDPY HHPGQAHGLA FSVRANVPPP
210 220 230 240 250
PSLRNVLAAV KNCYPEARMS GHGCLEKWAR DGVLLLNTTL TVKRGAAASH
260 270 280 290 300
SRIGWDRFVG GVIRRLAARR PGLVFMLWGT HAQNAIRPDP RVHCVLKFSH
310 320 330
PSPLSKVPFG TCQHFLVANR YLETRSISPI DWSV
Length:334
Mass (Da):36,328
Last modified:July 1, 1989 - v1
Checksum:i7CD3B74FB43F00CD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381T → I in strain: Nonneuroinvasive mutant HF10.
Natural varianti49 – 491T → N in strain: Nonneuroinvasive mutant HF10.
Natural varianti53 – 531S → L in strain: Nonneuroinvasive mutant HF10.
Natural varianti67 – 759ALLAALEAG → GAPRRPRGC in strain: Nonneuroinvasive mutant HF10 and 17 syn+.
Natural varianti126 – 1261M → L in strain: Nonneuroinvasive mutant HF10.
Natural varianti280 – 2801T → A in strain: Nonneuroinvasive mutant HF10.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32338.1.
DQ889502 Genomic DNA. Translation: ABI63464.1.
FJ593289 Genomic DNA. Translation: ACM62224.1.
PIRiB28133. DGBEX2.
RefSeqiNP_044603.1. NC_001806.1.

Genome annotation databases

GeneIDi2703370.
KEGGivg:2703370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32338.1.
DQ889502 Genomic DNA. Translation: ABI63464.1.
FJ593289 Genomic DNA. Translation: ACM62224.1.
PIRiB28133. DGBEX2.
RefSeqiNP_044603.1. NC_001806.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LAUX-ray1.80E91-334[»]
1UDGX-ray1.75A91-334[»]
1UDHX-ray1.75A91-334[»]
1UDIX-ray2.70E91-334[»]
2C53X-ray1.80A91-334[»]
2C56X-ray2.10A91-334[»]
4L5NX-ray2.16A/B96-334[»]
SMRiP10186. Positions 107-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1506602.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703370.
KEGGivg:2703370.

Phylogenomic databases

KOiK03648.

Enzyme and pathway databases

BRENDAi3.2.2.27. 2647.
SABIO-RKP10186.

Miscellaneous databases

EvolutionaryTraceiP10186.

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. "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
    McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
    J. Gen. Virol. 69:1531-1574(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
    Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
    Microbes Infect. 9:142-149(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Nonneuroinvasive mutant HF10.
  3. "Herpes simplex virus type 1 bacterial artificial chromosome."
    Cunningham C., Davison A.J.
    Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 17 syn+.
  4. "The structural basis of specific base-excision repair by uracil-DNA glycosylase."
    Savva R., McAuley-Hecht K., Brown T., Pearl L.
    Nature 373:487-493(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 91-334.
  5. "Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex."
    Savva R., Pearl L.H.
    Nat. Struct. Biol. 2:752-757(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 91-334, FUNCTION.
  6. "A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1."
    Krusong K., Carpenter E.P., Bellamy S.R., Savva R., Baldwin G.S.
    J. Biol. Chem. 281:4983-4992(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 91-334, FUNCTION.

Entry informationi

Entry nameiUNG_HHV11
AccessioniPrimary (citable) accession number: P10186
Secondary accession number(s): B9VQC9, Q09ID1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 1, 2015
This is version 93 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

External Data

Dasty 3

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 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.