ID   UNG_VAR67               Reviewed;         218 AA.
AC   P0DSP7; P32988;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   02-DEC-2020, entry version 7.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=UNG; ORFNames=D4R, F4R;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8383392; DOI=10.1016/0168-1702(93)90110-9;
RA   Shchelkunov S.N., Blinov V.M., Totmenin A.V., Marennikova S.S.,
RA   Kolykhalov A.A., Frolov I.V., Chizhikov V.E., Gytorov V.V., Gashikov P.V.,
RA   Belanov E.F., Belavin P.A., Resenchuk S.M., Andzhaparidze O.G.,
RA   Sandakhchiev L.S.;
RT   "Nucleotide sequence analysis of variola virus HindIII M, L, I genome
RT   fragments.";
RL   Virus Res. 27:25-35(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(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; X67119; CAA47593.1; -; Genomic_DNA.
DR   EMBL; X69198; CAA49035.1; -; Genomic_DNA.
DR   PIR; A36847; A36847.
DR   RefSeq; NP_042138.1; NC_001611.1.
DR   SMR; P0DSP7; -.
DR   GeneID; 1486420; -.
DR   KEGG; vg:1486420; -.
DR   Proteomes; UP000002060; 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; Reference proteome.
FT   CHAIN           1..218
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176182"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10072"
SQ   SEQUENCE   218 AA;  25205 MW;  F76338586A5D2BB7 CRC64;
     MNSVTVSHAP YTITYHDDWE PVMNQLVEFY NEVASWLLRD ETSPIPDKFF IQLKQPLRNK
     RVCVCGIDPY PKDGTGVPFE SPNFTKKSIK EIASSISRLT GVIDYKGYNL NIIDGVIPWN
     YYLSCKLGET KSHAIYWDKI SKLLLHHITK HVRFLYCLGK TDFSNIRAKL ESPVTTIVGY
     HPAARDRQFE KDRSFEIINV LLELDNKAPI NWAQGFIY