ID   UNG_HHV11               Reviewed;         334 AA.
AC   P10186; B9VQC9; Q09ID1;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 133.
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   ORFNames=UL2;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nonneuroinvasive mutant HF10;
RX   PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA   Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT   "Determination and analysis of the DNA sequence of highly attenuated herpes
RT   simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL   Microbes Infect. 9:142-149(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17 syn+;
RA   Cunningham C., Davison A.J.;
RT   "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX   PubMed=8391260; DOI=10.1042/bj2920883;
RA   Focher F., Verri A., Spadari S., Manservigi R., Gambino J., Wright G.E.;
RT   "Herpes simplex virus type 1 uracil-DNA glycosylase: isolation and
RT   selective inhibition by novel uracil derivatives.";
RL   Biochem. J. 292:883-889(1993).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 91-334.
RX   PubMed=7845459; DOI=10.1038/373487a0;
RA   Savva R., McAuley-Hecht K., Brown T., Pearl L.;
RT   "The structural basis of specific base-excision repair by uracil-DNA
RT   glycosylase.";
RL   Nature 373:487-493(1995).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 91-334, AND FUNCTION.
RX   PubMed=7552746; DOI=10.1038/nsb0995-752;
RA   Savva R., Pearl L.H.;
RT   "Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-
RT   uracil glycosylase inhibitor protein complex.";
RL   Nat. Struct. Biol. 2:752-757(1995).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 91-334, AND FUNCTION.
RX   PubMed=16306042; DOI=10.1074/jbc.m509137200;
RA   Krusong K., Carpenter E.P., Bellamy S.R., Savva R., Baldwin G.S.;
RT   "A comparative study of uracil-DNA glycosylases from human and herpes
RT   simplex virus type 1.";
RL   J. Biol. Chem. 281:4983-4992(2006).
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, ECO:0000269|PubMed:16306042, ECO:0000269|PubMed:7552746,
CC       ECO:0000269|PubMed:8391260}.
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         ECO:0000269|PubMed:8391260};
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04046,
CC       ECO:0000269|PubMed:8391260}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000255|HAMAP-Rule:MF_04046}.
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DR   EMBL; X14112; CAA32338.1; -; Genomic_DNA.
DR   EMBL; DQ889502; ABI63464.1; -; Genomic_DNA.
DR   EMBL; FJ593289; ACM62224.1; -; Genomic_DNA.
DR   PIR; B28133; DGBEX2.
DR   RefSeq; YP_009137076.1; NC_001806.2.
DR   PDB; 1LAU; X-ray; 1.80 A; E=91-334.
DR   PDB; 1UDG; X-ray; 1.75 A; A=91-334.
DR   PDB; 1UDH; X-ray; 1.75 A; A=91-334.
DR   PDB; 1UDI; X-ray; 2.70 A; E=91-334.
DR   PDB; 2C53; X-ray; 1.80 A; A=91-334.
DR   PDB; 2C56; X-ray; 2.10 A; A=91-334.
DR   PDB; 4L5N; X-ray; 2.16 A; A/B=96-334.
DR   PDB; 5AYS; X-ray; 2.09 A; A/B=91-334.
DR   PDBsum; 1LAU; -.
DR   PDBsum; 1UDG; -.
DR   PDBsum; 1UDH; -.
DR   PDBsum; 1UDI; -.
DR   PDBsum; 2C53; -.
DR   PDBsum; 2C56; -.
DR   PDBsum; 4L5N; -.
DR   PDBsum; 5AYS; -.
DR   SMR; P10186; -.
DR   MINT; P10186; -.
DR   DrugBank; DB03419; Uracil.
DR   DNASU; 2703370; -.
DR   GeneID; 2703370; -.
DR   KEGG; vg:2703370; -.
DR   BRENDA; 3.2.2.27; 2647.
DR   SABIO-RK; P10186; -.
DR   EvolutionaryTrace; P10186; -.
DR   Proteomes; UP000009294; Genome.
DR   Proteomes; UP000180652; 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; 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..334
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176185"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
FT   VARIANT         38
FT                   /note="T -> I (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         49
FT                   /note="T -> N (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         53
FT                   /note="S -> L (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         67..75
FT                   /note="ALLAALEAG -> GAPRRPRGC (in strain: Nonneuroinvasive
FT                   mutant HF10 and 17 syn+)"
FT   VARIANT         126
FT                   /note="M -> L (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         280
FT                   /note="T -> A (in strain: Nonneuroinvasive mutant HF10)"
FT   HELIX           108..116
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           123..130
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           133..148
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   TURN            155..160
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           161..164
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   TURN            183..185
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   STRAND          187..191
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           201..213
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           226..230
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   STRAND          233..239
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   TURN            247..252
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           255..269
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   STRAND          270..272
FT                   /evidence="ECO:0007829|PDB:1UDH"
FT   STRAND          274..279
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           280..285
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   STRAND          293..298
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           309..311
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   HELIX           314..323
FT                   /evidence="ECO:0007829|PDB:1UDG"
FT   TURN            324..326
FT                   /evidence="ECO:0007829|PDB:1UDG"
SQ   SEQUENCE   334 AA;  36328 MW;  7CD3B74FB43F00CD CRC64;
     MKRACSRSPS PRRRPSSPRR TPPRDGTPPQ KADADDPTPG ASNDASTETR PGSGGEPAAC
     RSSGPAALLA ALEAGPAGVT FSSSAPPDPP MDLTNGGVSP AATSAPLDWT TFRRVFLIDD
     AWRPLMEPEL ANPLTAHLLA EYNRRCQTEE VLPPREDVFS WTRYCTPDEV RVVIIGQDPY
     HHPGQAHGLA FSVRANVPPP PSLRNVLAAV KNCYPEARMS GHGCLEKWAR DGVLLLNTTL
     TVKRGAAASH SRIGWDRFVG GVIRRLAARR PGLVFMLWGT HAQNAIRPDP RVHCVLKFSH
     PSPLSKVPFG TCQHFLVANR YLETRSISPI DWSV
//