ID   UNG_VARV                Reviewed;         218 AA.
AC   P0DSP8; P32988;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   29-SEP-2021, entry version 11.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=UNG; ORFNames=D4R, F4R;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC       result of misincorporation of dUMP residues by DNA polymerase or due to
CC       deamination of cytosine. Also part of a heterodimeric processivity
CC       factor which potentiates the DNA polymerase activity. Binds to DNA (By
CC       similarity). {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. Interacts with protein A20. Component of the
CC       Uracil-DNA glycosylase(UDG)-A20-polymerase complex; A20 and UDG form a
CC       heterodimeric processivity factor that associates with E9 to form the
CC       processive polymerase holoenzyme (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000305}.
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DR   EMBL; L22579; AAA60842.1; -; Genomic_DNA.
DR   SMR; P0DSP8; -.
DR   Proteomes; UP000119805; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.470.10; -; 1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA-binding; Hydrolase.
FT   CHAIN           1..218
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000448129"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10072"
SQ   SEQUENCE   218 AA;  25088 MW;  EC7989F370EC9BB7 CRC64;
     MNSVTVSHAP YTITYHDDWE PVMNQLVEFY NEVASWLLRD ETSPIPDKFF IQLKQPLRNK
     RVCVCGIDPY PKDGTGVPFE SPNFTKKSIK EIASSISRLT GVIDYKGYNL NIIDGVIPWN
     YYLSCKLGET KSHAIYWDKI SKLLLHHITK HVSVLYCLGK TDFSNIRAKL ESPVTTIVGY
     HPAARDRQFE KDRSFEIINV LLELDNKAPI NWAQGFIY