UNG_SUHVF
ID UNG_SUHVF Reviewed; 315 AA.
AC P52506; Q69399;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 02-JUN-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 Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1)
OS (Pseudorabies virus (strain Indiana-Funkhauser / Becker)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31523;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8189524; DOI=10.1128/jvi.68.6.3868-3878.1994;
RA Klupp B.G., Baumeister J., Karger A., Visser N., Mettenleiter T.C.;
RT "Identification and characterization of a novel structural glycoprotein in
RT pseudorabies virus, gL.";
RL J. Virol. 68:3868-3878(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8396663; DOI=10.1128/jvi.67.10.5955-5961.1993;
RA Dean H.J., Cheung A.K.;
RT "A 3' coterminal gene cluster in pseudorabies virus contains herpes simplex
RT virus UL1, UL2, and UL3 gene homologs and a unique UL3.5 open reading
RT frame.";
RL J. Virol. 67:5955-5961(1993).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16422.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U02512; AAA18856.1; -; Unassigned_DNA.
DR EMBL; L13855; AAA16422.1; ALT_INIT; Unassigned_DNA.
DR SMR; P52506; -.
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..315
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176195"
FT REGION 35..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
FT CONFLICT 26
FT /note="A -> AA (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 32911 MW; 08363116D263DDC7 CRC64;
MEGPPPSKRP CGLPPGVRLV VPAAAASASN AATAAAAAAP AGAGAGASKP ARPPAAARPA
KGTPAASAAT TATGADASAP APDPGAPTWD AFAAEFDVAP SWRALLEPEI AKPYARLLLA
EYRGRCLTEE VLPAREDVFA WTRLTAPEDV KVVIIGQDPY HGPGQAHGLA FSVRRGVPIP
PSLANIFAAV RATYPTLPAP AHGCLEAWAR RGVLLLNTTL TVRRGVPGSH APLGWARLVR
AVVQRLCETR PKLVFMLWGA HAQKACAPDP RRHKVLTFSH PSPLARTPFR TCPHFGEANA
YLVQTGRAPV DWSVD