ID   UNG_HHV6U               Reviewed;         255 AA.
AC   P52345;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-JUN-2021, entry version 89.
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=U81; Synonyms=EDLF4;
OS   Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7941342; DOI=10.1006/viro.1994.1589;
RA   Nicholas J.;
RT   "Nucleotide sequence analysis of a 21-kbp region of the genome of human
RT   herpesvirus-6 containing homologues of human cytomegalovirus major
RT   immediate-early and replication genes.";
RL   Virology 204:738-750(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(1995).
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}.
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DR   EMBL; U13194; AAA68472.1; -; Genomic_DNA.
DR   EMBL; X83413; CAA58330.1; -; Genomic_DNA.
DR   RefSeq; NP_042974.1; NC_001664.2.
DR   SMR; P52345; -.
DR   PRIDE; P52345; -.
DR   DNASU; 1487961; -.
DR   GeneID; 1487961; -.
DR   KEGG; vg:1487961; -.
DR   Proteomes; UP000009295; 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   3: Inferred from homology;
KW   DNA damage; DNA repair; Host nucleus; Hydrolase; Reference proteome.
FT   CHAIN           1..255
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176188"
FT   ACT_SITE        93
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
SQ   SEQUENCE   255 AA;  29038 MW;  F7DB5959BD9D0A48 CRC64;
     MALLQWMLDH VQDEEKNCEN LSIDDQHSLF GINRDWLSFL QLSKLEITHL KHVYKLVDND
     RAHLMVHPSS DNVHAWSFLC KPDNVKVVIL GQDPYPDGRG CGLAFGTVKE CSIPESLKNI
     FKELERSVPN FSPPDNGCLN SWCSEGVLLL NSIFTVVHGL PMSHEAFGWQ TLSYKIISKL
     SVEMDSLVFL LWGNHARKLS YLIDARKHLV LESAHPSPKV KSARMPFIGC NHFVRANLFL
     TEHGKDPINW NILNE