UNG_DEIRA
ID UNG_DEIRA Reviewed; 247 AA.
AC Q9RWH9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00148};
DE Short=UDG {ECO:0000255|HAMAP-Rule:MF_00148};
DE EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN Name=ung {ECO:0000255|HAMAP-Rule:MF_00148}; OrderedLocusNames=DR_0689;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC result of misincorporation of dUMP residues by DNA polymerase or due to
CC deamination of cytosine. {ECO:0000255|HAMAP-Rule:MF_00148}.
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_00148};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000255|HAMAP-Rule:MF_00148}.
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DR EMBL; AE000513; AAF10269.1; -; Genomic_DNA.
DR PIR; F75486; F75486.
DR RefSeq; NP_294412.1; NC_001263.1.
DR RefSeq; WP_010887334.1; NZ_CP015081.1.
DR PDB; 2BOO; X-ray; 1.80 A; A=1-247.
DR PDB; 3UFM; X-ray; 1.95 A; A=1-247.
DR PDB; 4UQM; X-ray; 1.35 A; A=1-247.
DR PDBsum; 2BOO; -.
DR PDBsum; 3UFM; -.
DR PDBsum; 4UQM; -.
DR AlphaFoldDB; Q9RWH9; -.
DR SMR; Q9RWH9; -.
DR STRING; 243230.DR_0689; -.
DR EnsemblBacteria; AAF10269; AAF10269; DR_0689.
DR KEGG; dra:DR_0689; -.
DR PATRIC; fig|243230.17.peg.867; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_3_1_0; -.
DR InParanoid; Q9RWH9; -.
DR OMA; PDNGYLM; -.
DR OrthoDB; 1260295at2; -.
DR BRENDA; 3.2.2.27; 1856.
DR EvolutionaryTrace; Q9RWH9; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
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; Cytoplasm; DNA damage; DNA repair; Hydrolase;
KW Reference proteome.
FT CHAIN 1..247
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176090"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:4UQM"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4UQM"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:4UQM"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4UQM"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:4UQM"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:4UQM"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:4UQM"
FT TURN 152..157
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:4UQM"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:4UQM"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:4UQM"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4UQM"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:4UQM"
SQ SEQUENCE 247 AA; 27746 MW; B92EB3319AFF4736 CRC64;
MTDQPDLFGL APDAPRPIIP ANLPEDWQEA LLPEFSAPYF HELTDFLRQE RKEYTIYPPA
PDVFNALRYT PLGEVKVLIL GQDPYHGPNQ AHGLSFSVRP GVRVPPSLRN IYKELTEDIP
GFVAPKHGYL RSWAEQGVLL LNAVLTVRAG QANSHQGKGW EHFTDAVIKA VNAKEERVVF
ILWGSYARKK KKLITGKNHV VIESGHPSPL SEQYFFGTRP FSKTNEALEK AGRGPVEWQL
PATVTEE
