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UNG_EBVB9
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   03-AUG-2022, entry version 107.
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; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
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   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   PRIDE; P12888; -.
DR   DNASU; 3783711; -.
DR   GeneID; 3783711; -.
DR   KEGG; vg:3783711; -.
DR   EvolutionaryTrace; P12888; -.
DR   Proteomes; UP000153037; Genome.
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; -; 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   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 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
 
 
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