ID   UNG_HHV23               Reviewed;         294 AA.
AC   P13158;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   07-APR-2021, entry version 81.
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   Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10313;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2846888; DOI=10.1128/jvi.62.12.4774-4777.1988;
RA   Worrad D.M., Caradonna S.;
RT   "Identification of the coding sequence for herpes simplex virus uracil-DNA
RT   glycosylase.";
RL   J. Virol. 62:4774-4777(1988).
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; M25410; AAA45859.1; ALT_SEQ; mRNA.
DR   PIR; A31885; DGBEH2.
DR   SMR; P13158; -.
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   2: Evidence at transcript level;
KW   DNA damage; DNA repair; Host nucleus; Hydrolase.
FT   CHAIN           1..294
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176186"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
SQ   SEQUENCE   294 AA;  32495 MW;  1AE64C334E6F8075 CRC64;
     MAMKRNPSRV FCAYSKNGTH RSAAPTTHRC IAGGGRGALD AGAENTQGHP ESRCFPGGRP
     PQTGPSWCLG AAFRRAFLID DAWRPLLEPE LANPLTARLL AEYDRRCQTE EVLPPREDVF
     SWTRYCTPDD VRVVIIGQDP YHHPGQAHGL AFSVRADVPV PPSLRNVLAA VKNCYPDARM
     SGRGCLEKWA RDGVLLLNTT LTVKRGAAAS TSKLGWDRFV GGVVRRLAAR RPGLVFMLWG
     AHAQNAIRPD PRQHYVLKFS HPSPLSKVPF GTCQHFLAAN RYLETRDIMP ITVV