UNG_VACCC
ID UNG_VACCC Reviewed; 218 AA.
AC P20536;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=UNG; ORFNames=D4R;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
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 -!- INTERACTION:
CC P20536; P20995: A20R; NbExp=6; IntAct=EBI-984584, EBI-984598;
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000305}.
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DR EMBL; M35027; AAA48100.1; -; Genomic_DNA.
DR PIR; C42515; C42515.
DR PDB; 4OD8; X-ray; 1.85 A; A/B=1-218.
DR PDB; 4ODA; X-ray; 2.20 A; A/B=1-218.
DR PDB; 4YGM; X-ray; 1.85 A; A/B=1-218.
DR PDB; 4YIG; X-ray; 2.70 A; A/E/I=1-218.
DR PDB; 5JKR; X-ray; 2.60 A; A/B=1-218.
DR PDB; 5JKS; X-ray; 2.79 A; A/B=1-218.
DR PDB; 5JKT; X-ray; 2.49 A; A/B=1-218.
DR PDBsum; 4OD8; -.
DR PDBsum; 4ODA; -.
DR PDBsum; 4YGM; -.
DR PDBsum; 4YIG; -.
DR PDBsum; 5JKR; -.
DR PDBsum; 5JKS; -.
DR PDBsum; 5JKT; -.
DR SMR; P20536; -.
DR IntAct; P20536; 3.
DR BindingDB; P20536; -.
DR ChEMBL; CHEMBL3988595; -.
DR PRIDE; P20536; -.
DR Proteomes; UP000008269; 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 GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Reference proteome.
FT CHAIN 1..218
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176180"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10072"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:4OD8"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:4OD8"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:4OD8"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:4OD8"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:4OD8"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4OD8"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:4OD8"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:4OD8"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4OD8"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4OD8"
FT TURN 160..165
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:4OD8"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:4OD8"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:4OD8"
SQ SEQUENCE 218 AA; 25080 MW; 6A4184AFA912B97F CRC64;
MNSVTVSHAP YTITYHDDWE PVMSQLVEFY NEVASWLLRD ETSPIPDKFF IQLKQPLRNK
RVCVCGIDPY PKDGTGVPFE SPNFTKKSIK EIASSISRLT GVIDYKGYNL NIIDGVIPWN
YYLSCKLGET KSHAIYWDKI SKLLLQHITK HVSVLYCLGK TDFSNIRAKL ESPVTTIVGY
HPAARDRQFE KDRSFEIINV LLELDNKVPI NWAQGFIY
