ID   UNG_EHV1V               Reviewed;         312 AA.
AC   P69859; Q6S6U3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   02-JUN-2021, entry version 57.
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   Name=61;
OS   Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=310273;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Davis-Poynter N.J., Nugent J., Birch-Machin I., Allen G.P.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45945.1; -; Genomic_DNA.
DR   RefSeq; YP_053105.1; NC_001491.2.
DR   SMR; P69859; -.
DR   GeneID; 2948563; -.
DR   KEGG; vg:2948563; -.
DR   Proteomes; UP000008296; 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..312
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176194"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
SQ   SEQUENCE   312 AA;  34778 MW;  6C70A454FCD16E8E CRC64;
     MSSACDHETE ASHVNIPETT PEENGSNSST PTSEIGPACV VSPAPGETGA PPPKRRRPCG
     LPQGVALINT SVSTHPLFTT SCQSSWEDVE REFNIAPSWR PILEREMQQP YVRLLLNEYK
     LRCASEEVFP PKEDIFAWTR FSPPEKVRVV IVGQDPYHAP GQAHGLAFSV RKGVPVPPSL
     RNIYSAVQKS YPSFRHPMHG FLERWAEQGV LLINTTLTVA RGKPGSHATL GWHRLVRAVI
     DRLCTTSQGL VFMLWGAHAQ KSCSPNRQHH LVLTYGHPSP LSRVNFRDCP HFLEANAYLT
     KTGRKPVDWQ IE