UNG_VACCA
ID UNG_VACCA Reviewed; 218 AA.
AC Q91UM2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 02-JUN-2021, entry version 82.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=UNG; OrderedLocusNames=MVA101R, ACAM3000_MVA_101;
OS Vaccinia virus (strain Ankara) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=126794;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT "The complete genomic sequence of the modified vaccinia Ankara strain:
RT comparison with other orthopoxviruses.";
RL Virology 244:365-396(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Acambis 3000;
RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA Khristova M., Wohlhueter R.M.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF GLY-179.
RX PubMed=17605817; DOI=10.1186/1472-6807-7-45;
RA Schormann N., Grigorian A., Samal A., Krishnan R., DeLucas L.,
RA Chattopadhyay D.;
RT "Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric
RT assembly.";
RL BMC Struct. Biol. 7:45-45(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DNA-BINDING.
RX PubMed=20861259; DOI=10.1128/jvi.01435-10;
RA Druck Shudofsky A.M., Silverman J.E., Chattopadhyay D., Ricciardi R.P.;
RT "Vaccinia virus D4 mutants defective in processive DNA synthesis retain
RT binding to A20 and DNA.";
RL J. Virol. 84:12325-12335(2010).
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.
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; U94848; AAB96513.1; -; Genomic_DNA.
DR EMBL; AY603355; AAT10499.1; -; Genomic_DNA.
DR PIR; T37377; T37377.
DR RefSeq; YP_232991.1; NC_006998.1.
DR PDB; 2OWQ; X-ray; 2.40 A; A/B=1-218.
DR PDB; 3NT7; X-ray; 2.40 A; A/C=1-218.
DR PDB; 4DOF; X-ray; 2.80 A; A/B/C/D=1-218.
DR PDB; 4DOG; X-ray; 2.30 A; A=1-218.
DR PDB; 4IRB; X-ray; 2.30 A; A/B/C/D=1-218.
DR PDB; 4LZB; X-ray; 2.03 A; A/B/C/D/E/F/G/H/I/J/K/L=1-218.
DR PDB; 4QC9; X-ray; 2.26 A; A/B/C/D=1-218.
DR PDB; 4QCA; X-ray; 1.90 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 PDBsum; 2OWQ; -.
DR PDBsum; 3NT7; -.
DR PDBsum; 4DOF; -.
DR PDBsum; 4DOG; -.
DR PDBsum; 4IRB; -.
DR PDBsum; 4LZB; -.
DR PDBsum; 4QC9; -.
DR PDBsum; 4QCA; -.
DR PDBsum; 5JX3; -.
DR SMR; Q91UM2; -.
DR DNASU; 3707565; -.
DR GeneID; 3707565; -.
DR KEGG; vg:3707565; -.
DR BRENDA; 3.2.2.27; 6591.
DR EvolutionaryTrace; Q91UM2; -.
DR Proteomes; UP000159908; Genome.
DR Proteomes; UP000172909; 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.
FT CHAIN 1..218
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176179"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10072"
FT MUTAGEN 179
FT /note="G->R: Defective DNA replication, reduced ability to
FT interact with A20."
FT /evidence="ECO:0000269|PubMed:17605817"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4LZB"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:4LZB"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:4LZB"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:4LZB"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:4LZB"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4LZB"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:4LZB"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:4LZB"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4LZB"
FT TURN 160..165
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:4LZB"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:4LZB"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:4LZB"
SQ SEQUENCE 218 AA; 25052 MW; 6A419624A912B97F CRC64;
MNSVTVSHAP YTITYHDDWE PVMSQLVEFY NEVASWLLRD ETSPIPDKFF IQLKQPLRNK
RVCVCGIDPY PKDGTGVPFE SPNFTKKSIK EIASSISRLT GVIDYKGYNL NIIDGVIPWN
YYLSCKLGET KSHAIYWDKI SKLLLQHITK HVSVLYCLGK TDFSNIRAKL ESPVTTIVGY
HPAARDRQFE KDRSFEIINV LLELDNKAPI NWAQGFIY
