ID   UNG_FOWPN               Reviewed;         218 AA.
AC   P21968; Q9J5E9;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   10-FEB-2021, entry version 100.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=UNG; OrderedLocusNames=FPV062; ORFNames=FPD4;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-1;
RX   PubMed=2165135; DOI=10.1099/0022-1317-71-7-1517;
RA   Tartaglia J., Winslow J., Goebel S.J., Johnson G.P., Taylor J.,
RA   Paoletti E.;
RT   "Nucleotide sequence analysis of a 10.5 kbp HindIII fragment of fowlpox
RT   virus: relatedness to the central portion of the vaccinia virus HindIII D
RT   region.";
RL   J. Gen. Virol. 71:1517-1524(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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; X17202; CAA35064.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44406.1; -; Genomic_DNA.
DR   PIR; A35216; A35216.
DR   RefSeq; NP_039025.1; NC_002188.1.
DR   SMR; P21968; -.
DR   GeneID; 1486610; -.
DR   KEGG; vg:1486610; -.
DR   Proteomes; UP000008597; 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; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   Pfam; PF03167; UDG; 1.
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_0000176177"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10072"
FT   CONFLICT        130
FT                   /note="T -> A (in Ref. 1; CAA35064)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   218 AA;  25593 MW;  2355AE81686CD24F CRC64;
     MKTLKLNNWP YPIEYHEDWE NIINHISDVI EETGPWLLEE NTSPSHENIF KQLKQSLKDK
     RVCIVGIDPY PTDATGVPFE SPDFSKKTIK AIAENISRRY NVRLFKNYNF LFVEGVLAWN
     YYLSCREGET KSHKIFWERL ADVFINHIAA YVSVFYFLGK SDFSNFRSIL NSPTTVVVGY
     HPAARNRQFD TDETFEIVNT LLELKNEPRI NWVQGFEI