ID   UNG_VZVO                Reviewed;         305 AA.
AC   Q9J3N2; Q4JQR6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   07-APR-2021, entry version 73.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_04046};
DE            Short=UDG {ECO:0000255|HAMAP-Rule:MF_04046};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_04046};
DE   AltName: Full=UNG {ECO:0000255|HAMAP-Rule:MF_04046};
GN   ORFNames=ORF59;
OS   Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=341980;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=10720545; DOI=10.1086/315335;
RA   Argaw T., Cohen J.I., Klutch M., Lekstrom K., Yoshikawa T., Asano Y.,
RA   Krause P.R.;
RT   "Nucleotide sequences that distinguish Oka vaccine from parental Oka and
RT   other varicella-zoster virus isolates.";
RL   J. Infect. Dis. 181:1153-1157(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC   Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA   Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT   "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT   its parental virus.";
RL   J. Virol. 76:11447-11459(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC   Oka varicella vaccine Varivax (V-Oka-Merk);
RX   PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA   Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA   Vassilev V.;
RT   "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL   J. Virol. 82:11023-11044(2008).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC       result of misincorporation of dUMP residues by DNA polymerase or
CC       deamination of cytosines. Therefore may reduce deleterious uracil
CC       incorporation into the viral genome, particularly in terminally
CC       differentiated cells which lack DNA repair enzymes. {ECO:0000255|HAMAP-
CC       Rule:MF_04046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC         DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04046};
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04046}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000255|HAMAP-Rule:MF_04046}.
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DR   EMBL; AF206304; AAF61660.1; -; Genomic_DNA.
DR   EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ008354; AAY57668.1; -; Genomic_DNA.
DR   EMBL; DQ008355; AAY57739.1; -; Genomic_DNA.
DR   SMR; Q9J3N2; -.
DR   IntAct; Q9J3N2; 6.
DR   MINT; Q9J3N2; -.
DR   Proteomes; UP000002603; Genome.
DR   Proteomes; UP000008504; Genome.
DR   Proteomes; UP000008505; Genome.
DR   Proteomes; UP000008506; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR002043; UDG_fam1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Host nucleus; Hydrolase.
FT   CHAIN           1..305
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000385166"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
FT   CONFLICT        44
FT                   /note="P -> L (in Ref. 2; AB097933)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   305 AA;  34360 MW;  42909E7B38CEDC6B CRC64;
     MDVSGEPTVC SNAYANEMKL SDSKDIYVLA HPVTKKTRKR PRGPPLGVKL DPPTFKLNNM
     SHHYDTETFT PVSSQLDSVE VFSKFNISPE WYDLLSDELK EPYAKGIFLE YNRLLNSGEE
     ILPSTGDIFA WTRFCGPQSI RVVIIGQDPY PTAGHAHGLA FSVKRGITPP SSLKNIFAAL
     MESYPNMTPP THGCLESWAR QGVLLLNTTL TVRRGTPGSH VYLGWGRLVQ RVLQRLCENR
     TGLVFMLWGA HAQKTTQPNS RCHLVLTHAH PSPLSRVPFR NCRHFVQANE YFTRKGEPEI
     DWSVI