UNG_EHV1B
ID UNG_EHV1B Reviewed; 312 AA.
AC P28866; Q6S6U3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 02-JUN-2021, entry version 104.
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=61;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Davison A.J.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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; AY665713; AAT67318.1; -; Genomic_DNA.
DR PIR; G36801; DGBEF3.
DR RefSeq; YP_053105.1; NC_001491.2.
DR SMR; P28866; -.
DR GeneID; 2948563; -.
DR KEGG; vg:2948563; -.
DR Proteomes; UP000001189; 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..312
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176193"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
SQ SEQUENCE 312 AA; 34778 MW; 6C70A454FCD16E8E CRC64;
MSSACDHETE ASHVNIPETT PEENGSNSST PTSEIGPACV VSPAPGETGA PPPKRRRPCG
LPQGVALINT SVSTHPLFTT SCQSSWEDVE REFNIAPSWR PILEREMQQP YVRLLLNEYK
LRCASEEVFP PKEDIFAWTR FSPPEKVRVV IVGQDPYHAP GQAHGLAFSV RKGVPVPPSL
RNIYSAVQKS YPSFRHPMHG FLERWAEQGV LLINTTLTVA RGKPGSHATL GWHRLVRAVI
DRLCTTSQGL VFMLWGAHAQ KSCSPNRQHH LVLTYGHPSP LSRVNFRDCP HFLEANAYLT
KTGRKPVDWQ IE