ID   UNG1_STRCO              Reviewed;         225 AA.
AC   Q9EX12;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Uracil-DNA glycosylase 1;
DE            Short=UDG 1;
DE            EC=3.2.2.27;
GN   Name=ung1; OrderedLocusNames=SCO1114; ORFNames=2SCG38.07;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000305}.
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DR   EMBL; AL939107; CAC13066.1; -; Genomic_DNA.
DR   RefSeq; NP_625407.1; NC_003888.3.
DR   RefSeq; WP_011027583.1; NZ_VNID01000006.1.
DR   AlphaFoldDB; Q9EX12; -.
DR   SMR; Q9EX12; -.
DR   STRING; 100226.SCO1114; -.
DR   GeneID; 1096537; -.
DR   KEGG; sco:SCO1114; -.
DR   PATRIC; fig|100226.15.peg.1111; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_1_11; -.
DR   InParanoid; Q9EX12; -.
DR   OMA; WEAVTEQ; -.
DR   PhylomeDB; Q9EX12; -.
DR   Proteomes; UP000001973; Chromosome.
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   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT   CHAIN           1..225
FT                   /note="Uracil-DNA glycosylase 1"
FT                   /id="PRO_0000176149"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   225 AA;  24456 MW;  B370AE819B12D144 CRC64;
     MAPRPLNEIV EAGWAKALEP VAGQITSMGE FLRAEIAAGR TYLPAGANVL RAFQQPFDDV
     RVLIVGQDPY PTPGHAVGLS FSVAPEVRPL PGSLVNIFRE LNTDLNLPQP ANGDLTPWTR
     QGVLLLNRAL TTAPRKPAAH RGKGWEEVTE QAIRALAARG KPMVSILWGR DARNLRPLLG
     DLPALESAHP SPMSADRGFF GSRPFSRAND LLMRLGGQPV DWRLP