ID   UNG_SUHVK               Reviewed;         316 AA.
AC   P52507;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-JUN-2021, entry version 76.
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=UL2;
OS   Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS   Kaplan)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=33703;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8189524; DOI=10.1128/jvi.68.6.3868-3878.1994;
RA   Klupp B.G., Baumeister J., Karger A., Visser N., Mettenleiter T.C.;
RT   "Identification and characterization of a novel structural glycoprotein in
RT   pseudorabies virus, gL.";
RL   J. Virol. 68:3868-3878(1994).
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; U02513; AAA18859.1; -; Unassigned_DNA.
DR   RefSeq; YP_068375.1; NC_006151.1.
DR   SMR; P52507; -.
DR   GeneID; 2952528; -.
DR   KEGG; vg:2952528; -.
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..316
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176196"
FT   REGION          36..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
SQ   SEQUENCE   316 AA;  32998 MW;  FFDA90DBB8A66B43 CRC64;
     MEGPPPSKRP CGLPPGVRLV VPAAAAASAS NAATAAAAAA PAGAGAGASK PARPSAAARP
     AKGTPAASAA TTATGADASA PPPDPGAPTW DAFAAEFDVA PSWRALLEPE IAKPYARLLL
     AEYRGRCLTE EVLPAREDVF AWTRLTAPED VKVVIIGQDP YHGPGQAHGL AFSVRRGVPI
     PPSLANIFAA VRATYPTLPA PAHGCLEAWA RRGVLLLNTT LTVRRGVPGS HAPLGWARLV
     RAVVQRLCET RPKLVFMLWG AHAQKACAPD PRRHKVLTFS HPSPLARTPF RTCPHFGEAN
     AYLVQTGRAP VDWSVD