UNG_BHV1C
ID UNG_BHV1C Reviewed; 204 AA.
AC P53764;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 07-APR-2021, entry version 76.
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=UL2;
OS Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10323;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7483276; DOI=10.1006/viro.1995.1543;
RA Khattar S.K., van Drunen Littel-van den Hurk S., Babiuk L.A., Tikoo S.K.;
RT "Identification and transcriptional analysis of a 3'-coterminal gene
RT cluster containing UL1, UL2, UL3, and UL3.5 open reading frames of bovine
RT herpesvirus-1.";
RL Virology 213:28-37(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; U32173; AAC54556.1; -; Genomic_DNA.
DR SMR; P53764; -.
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.
FT CHAIN 1..204
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176191"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
SQ SEQUENCE 204 AA; 22421 MW; F99138177F111B19 CRC64;
MPYTRHALRE YERRSRVEQV LPPKADIFAW TRYAAPEDIK VVILGQDPYH SRGQAHGLAF
SVNRGVPVPP SLQNIYAAVQ KNFPGAPRPS HGCLEDWARR GVLLLNTSLT VRSGAPGSHS
SLGWGRLVHA VLARLSAESG PLVFMLWGAH AQRAFGAAGK RHLVLTYSHP SPLSRAPFVH
CTHFAEANAF LEQHGRGGVD WSIV
