ID   UNG_HHV7J               Reviewed;         254 AA.
AC   P50639;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-JUN-2021, entry version 94.
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=U81;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(1996).
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; U43400; AAC54743.1; -; Genomic_DNA.
DR   PIR; T41983; T41983.
DR   RefSeq; YP_073819.1; NC_001716.2.
DR   SMR; P50639; -.
DR   PRIDE; P50639; -.
DR   DNASU; 3289537; -.
DR   GeneID; 3289537; -.
DR   KEGG; vg:3289537; -.
DR   Proteomes; UP000009246; 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; Reference proteome.
FT   CHAIN           1..254
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176190"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
SQ   SEQUENCE   254 AA;  29006 MW;  FC8EDA1A96AD37AF CRC64;
     MALLQWMLEN ISDDNSIKMS LEEQHETFQI NVKWLKFLNL SDSDIVQLQN VYKLVQRDRE
     RLIIYPDPQN VHSWSYLCSP EEIKVIIVGQ DPYPDGRGHG LAFSTVRGCS PPNSLKTIFA
     ELERTIENFK APAHGSLKSW CAQGVLLLNT VFTVIRGVPM SHEAIGWQVL SNRIINQLSE
     KMQNLVFMLW GSQARKLVSL IDSKKHLILE CAHPSPRTKG SKTPFIGCGH FLKANKYLQI
     HNKCPIDWNI TNDL