ID   UNG_PSHV1               Reviewed;         362 AA.
AC   Q6UDG6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-JUN-2021, entry version 60.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000250|UniProtKB:P10186};
DE            Short=UDG {ECO:0000250|UniProtKB:P10186};
DE            EC=3.2.2.27 {ECO:0000250|UniProtKB:P10186};
DE   AltName: Full=UNG {ECO:0000250|UniProtKB:P10186};
GN   Name=UL2;
OS   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(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.
CC       {ECO:0000250|UniProtKB:P10186}.
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:0000250|UniProtKB:P10186};
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P10186}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000250|UniProtKB:P10186}.
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DR   EMBL; AY372243; AAQ73744.1; -; Genomic_DNA.
DR   RefSeq; NP_944438.1; NC_005264.1.
DR   SMR; Q6UDG6; -.
DR   GeneID; 2656983; -.
DR   KEGG; vg:2656983; -.
DR   Proteomes; UP000006840; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   Gene3D; 3.40.470.10; -; 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..362
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000406809"
FT   REGION          28..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..71
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10186"
SQ   SEQUENCE   362 AA;  39874 MW;  DEAEFE0C4259A5A3 CRC64;
     MANDERVATG EDRAWGRLGV AELRIDAASV APNDPTEDRE VVLPIPGPAV SPIPRLTQPP
     RSSPPRPDAP SDLPRAQREP TKRSPATAGP TEDPNFADKI FKQAAPARKK PRFMPPPKLI
     CGGVTDVTAE LPAPSWDRVA EEFGIPDSWK NILAPLVETQ RFAKTLQSYN GAKKSGNVLP
     SQDQIFAWAR YCAPHEVKVI IVGQDPYPTE GDAHGLAFSV PVGRRVPPSL RRVFAALKDC
     YGDGFPTPSS GSLIAWAKQG VLLLNRHLTV ERGLPRSHVS MGWDKLTFGV IKTLANDNPR
     MAVMLWGYDA KTFVPKLPSK HLRLEYSHPS TSTRRPFDCR HFIEANKFLE EGGLQAVVWR
     LP