UNG_VACCW
ID UNG_VACCW Reviewed; 218 AA.
AC P04303;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 02-JUN-2021, entry version 105.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=UNG; Synonyms=TS17; OrderedLocusNames=VACWR109; ORFNames=D4R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3033268; DOI=10.1128/jvi.61.5.1398-1406.1987;
RA Roseman N.A., Hruby D.E.;
RT "Nucleotide sequence and transcript organization of a region of the
RT vaccinia virus genome which encodes a constitutively expressed gene
RT required for DNA replication.";
RL J. Virol. 61:1398-1406(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
RA Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
RT "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D
RT fragment.";
RL Virology 153:96-112(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=8291232; DOI=10.1006/viro.1994.1061;
RA Millns A.K., Carpenter M.S., DeLange A.M.;
RT "The vaccinia virus-encoded uracil DNA glycosylase has an essential role in
RT viral DNA replication.";
RL Virology 198:504-513(1994).
RN [5]
RP INTERACTION WITH PROTEIN A20.
RX PubMed=16326701; DOI=10.1074/jbc.m511239200;
RA Stanitsa E.S., Arps L., Traktman P.;
RT "Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to
RT form a heterodimeric processivity factor for the viral DNA polymerase.";
RL J. Biol. Chem. 281:3439-3451(2006).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH A20 AND THE DNA POLYMERASE.
RX PubMed=21572084; DOI=10.1074/jbc.m111.222216;
RA Boyle K.A., Stanitsa E.S., Greseth M.D., Lindgren J.K., Traktman P.;
RT "Evaluation of the role of the vaccinia virus uracil DNA glycosylase and
RT A20 proteins as intrinsic components of the DNA polymerase holoenzyme.";
RL J. Biol. Chem. 286:24702-24713(2011).
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, ECO:0000269|PubMed:8291232}.
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 (By similarity). Interacts with protein A20.
CC Component of the Uracil-DNA glycosylase(UDG)-A20-polymerase complex;
CC A20 and UDG form a heterodimeric processivity factor that associates
CC with E9 to form the processive polymerase holoenzyme. {ECO:0000250,
CC ECO:0000269|PubMed:16326701, ECO:0000269|PubMed:21572084}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000305}.
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DR EMBL; M15058; AAA48258.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89388.1; -; Genomic_DNA.
DR PIR; A93025; QQVZ6.
DR PDB; 2OWQ; X-ray; 2.40 A; A/B=1-218.
DR PDB; 4QCB; X-ray; 2.89 A; A/B=1-218.
DR PDB; 5JX0; X-ray; 2.40 A; A/B/C/D=1-218.
DR PDB; 5JX3; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-218.
DR PDB; 5JX8; X-ray; 2.00 A; A/B=1-218.
DR PDBsum; 2OWQ; -.
DR PDBsum; 4QCB; -.
DR PDBsum; 5JX0; -.
DR PDBsum; 5JX3; -.
DR PDBsum; 5JX8; -.
DR SMR; P04303; -.
DR DIP; DIP-2182N; -.
DR IntAct; P04303; 1.
DR MINT; P04303; -.
DR BindingDB; P04303; -.
DR ChEMBL; CHEMBL1772931; -.
DR DrugCentral; P04303; -.
DR BRENDA; 3.2.2.27; 6591.
DR Proteomes; UP000000344; 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 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_0000176181"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10072"
FT CONFLICT 163
FT /note="Y -> F (in Ref. 2; AAA48258 and 3; AAO89388)"
FT /evidence="ECO:0000305"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:5JX8"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2OWQ"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:5JX8"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:5JX8"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5JX8"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2OWQ"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:5JX8"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5JX8"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:5JX8"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:5JX8"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:5JX8"
FT TURN 160..165
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:5JX3"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:5JX8"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:5JX8"
SQ SEQUENCE 218 AA; 25068 MW; 6541893BA912B968 CRC64;
MNSVTVSHAP YTITYHDDWE PVMSQLVEFY NEVASWLLRD ETSPIPDKFF IQLKQPLRNK
RVCVCGIDPY PKDGTGVPFE SPNFTKKSIK EIASSISRLT GVIDYKGYNL NIIDGVIPWN
YYLSCKLGET KSHAIYWDKI SKLLLQHITK HVSVLYCLGK TDYSNIRAKL ESPVTTIVGY
HPAARDRQFE KDRSFEIINV LLELDNKAPI NWAQGFIY
