P04303 (UNG_VACCW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uracil-DNA glycosylase
Short name=UDG
EC=3.2.2.27

Gene names

Name:	UNG
Synonyms:	TS17
Ordered Locus Names:	VACWR109
ORF Names:	D4R

Organism

Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) [Reference proteome]

Taxonomic identifier

10254 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus › Vaccinia virus

Virus host

Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4
Catalytic activity	Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Subunit structure	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. Ref.5 Ref.6
Sequence similarities	Belongs to the uracil-DNA glycosylase family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	DNA-binding
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity, hydrolyzing N-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 218	218	Uracil-DNA glycosylase		PRO_0000176181
Sites
	Active site	68	1	Proton acceptor By similarity
Experimental info
	Sequence conflict	163	1	Y → F in AAA48258. Ref.2
	Sequence conflict	163	1	Y → F in AAO89388. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P04303 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: 6541893BA912B968	FASTA	218	25,068
	10 20 30 40 50 60 MNSVTVSHAP YTITYHDDWE PVMSQLVEFY NEVASWLLRD ETSPIPDKFF IQLKQPLRNK 70 80 90 100 110 120 RVCVCGIDPY PKDGTGVPFE SPNFTKKSIK EIASSISRLT GVIDYKGYNL NIIDGVIPWN 130 140 150 160 170 180 YYLSCKLGET KSHAIYWDKI SKLLLQHITK HVSVLYCLGK TDYSNIRAKL ESPVTTIVGY 190 200 210 HPAARDRQFE KDRSFEIINV LLELDNKAPI NWAQGFIY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and transcript organization of a region of the vaccinia virus genome which encodes a constitutively expressed gene required for DNA replication." Roseman N.A., Hruby D.E. J. Virol. 61:1398-1406(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D fragment." Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J. Virology 153:96-112(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb." Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The vaccinia virus-encoded uracil DNA glycosylase has an essential role in viral DNA replication." Millns A.K., Carpenter M.S., DeLange A.M. Virology 198:504-513(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase." Stanitsa E.S., Arps L., Traktman P. J. Biol. Chem. 281:3439-3451(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PROTEIN A20.
[6]	"Evaluation of the role of the vaccinia virus uracil DNA glycosylase and A20 proteins as intrinsic components of the DNA polymerase holoenzyme." Boyle K.A., Stanitsa E.S., Greseth M.D., Lindgren J.K., Traktman P. J. Biol. Chem. 286:24702-24713(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH A20 AND THE DNA POLYMERASE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M15058 Genomic DNA. Translation: AAA48258.1. AY243312 Genomic DNA. Translation: AAO89388.1.
PIR	QQVZ6. A93025.
3D structure databases
ProteinModelPortal	P04303.
SMR	P04303. Positions 1-218.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2182N.
MINT	MINT-131069.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
ProtClustDB	CLSP2509792.
Family and domain databases
Gene3D	3.40.470.10. 1 hit.
InterPro	IPR018085. Ura-DNA_Glyclase_AS. IPR005122. Uracil-DNA_glycosylase-like. [Graphical view]
Pfam	PF03167. UDG. 1 hit. [Graphical view]
SUPFAM	SSF52141. UDNA_glycsylseSF. 1 hit.
PROSITE	PS00130. U_DNA_GLYCOSYLASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P04303.
ChEMBL	CHEMBL1772931.

Entry information

Entry name

UNG_VACCW

Accession

Primary (citable) accession number: P04303

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program