UNG_HHV8P
ID UNG_HHV8P Reviewed; 255 AA.
AC F5HFA1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
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=ORF46;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(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. {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; AF148805; ABD28896.1; -; Genomic_DNA.
DR RefSeq; YP_001129398.1; NC_009333.1.
DR PDB; 5NN7; X-ray; 2.50 A; A=21-255.
DR PDB; 5NNH; X-ray; 2.20 A; A=19-255.
DR PDB; 5NNU; X-ray; 2.97 A; A/B/D/E=19-255.
DR PDB; 6LYV; X-ray; 2.70 A; A/C/E/G/I/K/M/O=1-255.
DR PDBsum; 5NN7; -.
DR PDBsum; 5NNH; -.
DR PDBsum; 5NNU; -.
DR PDBsum; 6LYV; -.
DR SMR; F5HFA1; -.
DR BioGRID; 1776975; 3.
DR PRIDE; F5HFA1; -.
DR DNASU; 4961472; -.
DR GeneID; 4961472; -.
DR KEGG; vg:4961472; -.
DR Proteomes; UP000000942; 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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Host nucleus; Hydrolase;
KW Reference proteome.
FT CHAIN 1..255
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000423835"
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04046"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:5NNH"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:5NNH"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5NNH"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:5NNH"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5NNH"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6LYV"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:5NNH"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:5NNH"
FT TURN 156..161
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:5NNH"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:5NNH"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:5NNH"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:5NNH"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6LYV"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5NNU"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:5NNH"
SQ SEQUENCE 255 AA; 29008 MW; 3DF95D552D0C97C5 CRC64;
MDAWLQQTVF RGTLSISQGV DDRDLLLAPK WISFLSLSSF LKQKLLSLLR QIRELRLTTT
VYPPQDKLMW WSHCCDPEDI KVVILGQDPY HKGQATGLAF SVDPQCQVPP SLRSIFRELE
ASVPNFSTPS HGCLDSWARQ GVLLLNTVLT VEKGRAGSHE GLGWDWFTSF IISSISSKLE
HCVFLLWGRK AIDRTPLINA QKHLVLTAQH PSPLASLGGR HSRWPRFQGC NHFNLANDYL
TRHRRETVDW GLLEQ
