ID UNG_EBVB9 Reviewed; 255 AA.
AC P12888; Q777D9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 24-JAN-2024, entry version 114.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_04046};
DE Short=UDG {ECO:0000255|HAMAP-Rule:MF_04046};
DE EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_04046};
DE AltName: Full=UNG {ECO:0000255|HAMAP-Rule:MF_04046};
GN Name=UNG; ORFNames=BKRF3;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Lymphocryptovirus;
OC Lymphocryptovirus humangamma4; Epstein-Barr virus (strain GD1).
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=12771413; DOI=10.1099/vir.0.19054-0;
RA de Jesus O., Smith P.R., Spender L.C., Elgueta Karstegl C., Niller H.H.,
RA Huang D., Farrell P.J.;
RT "Updated Epstein-Barr virus (EBV) DNA sequence and analysis of a promoter
RT for the BART (CST, BARF0) RNAs of EBV.";
RL Virology 84:1443-1450(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 25-255.
RX PubMed=17157317; DOI=10.1016/j.jmb.2006.11.007;
RA Geoui T., Buisson M., Tarbouriech N., Burmeister W.P.;
RT "New insights on the role of the gamma-herpesvirus uracil-DNA glycosylase
RT leucine loop revealed by the structure of the Epstein-Barr virus enzyme in
RT complex with an inhibitor protein.";
RL J. Mol. Biol. 366:117-131(2007).
CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC result of misincorporation of dUMP residues by DNA polymerase or
CC deamination of cytosines. Therefore may reduce deleterious uracil
CC incorporation into the viral genome, particularly in terminally
CC differentiated cells which lack DNA repair enzymes. {ECO:0000255|HAMAP-
CC Rule:MF_04046}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_04046};
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04046}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000255|HAMAP-Rule:MF_04046}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24818.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; V01555; CAA24818.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ507799; CAD53429.1; -; Genomic_DNA.
DR RefSeq; YP_401679.1; NC_007605.1.
DR PDB; 2J8X; X-ray; 2.30 A; A/C=25-255.
DR PDB; 6LYJ; X-ray; 2.10 A; A/B=1-255.
DR PDBsum; 2J8X; -.
DR PDBsum; 6LYJ; -.
DR SMR; P12888; -.
DR IntAct; P12888; 2.
DR MINT; P12888; -.
DR DNASU; 3783711; -.
DR GeneID; 3783711; -.
DR KEGG; vg:3783711; -.
DR EvolutionaryTrace; P12888; -.
DR Proteomes; UP000153037; Segment.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR CDD; cd10027; UDG-F1-like; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR NCBIfam; TIGR00628; ung; 1.
DR PANTHER; PTHR11264; URACIL-DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR11264:SF0; URACIL-DNA GLYCOSYLASE; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Host nucleus; Hydrolase;
KW Reference proteome.
FT CHAIN 1..255
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176183"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 42..59
FT /evidence="ECO:0007829|PDB:6LYJ"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6LYJ"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6LYJ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:6LYJ"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6LYJ"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:6LYJ"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6LYJ"
FT TURN 159..164
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:6LYJ"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:6LYJ"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:6LYJ"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6LYJ"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:6LYJ"
SQ SEQUENCE 255 AA; 28605 MW; F7A26FB6F674E689 CRC64;
MASRGLDLWL DEHVWKRKQE IGVKGENLLL PDLWLDFLQL SPIFQRKLAA VIACVRRLRT
QATVYPEEDM CMAWARFCDP SDIKVVILGQ DPYHGGQANG LAFSVAYGFP VPPSLRNIYA
ELHRSLPEFS PPDHGCLDAW ASQGVLLLNT ILTVQKGKPG SHADIGWAWF TDHVISLLSE
RLKACVFMLW GAKAGDKASL INSKKHLVLT SQHPSPLAQN STRKSAQQKF LGNNHFVLAN
NFLREKGLGE IDWRL
//
