UNG_HHV11
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 23-FEB-2022, entry version 127.
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; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PRIDE; P10186; -.
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; -; 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..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
