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Database: UniProt
Entry: S0NRJ5_9ENTE
LinkDB: S0NRJ5_9ENTE
Original site: S0NRJ5_9ENTE 
ID   S0NRJ5_9ENTE            Unreviewed;       226 AA.
AC   S0NRJ5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00018429, ECO:0000256|HAMAP-Rule:MF_00148};
DE            Short=UDG {ECO:0000256|HAMAP-Rule:MF_00148};
DE            EC=3.2.2.27 {ECO:0000256|ARBA:ARBA00012030, ECO:0000256|HAMAP-Rule:MF_00148};
GN   Name=ung {ECO:0000256|HAMAP-Rule:MF_00148};
GN   ORFNames=OMQ_00651 {ECO:0000313|EMBL:EOT29959.1};
OS   Enterococcus saccharolyticus subsp. saccharolyticus ATCC 43076.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1139996 {ECO:0000313|EMBL:EOT29959.1, ECO:0000313|Proteomes:UP000014136};
RN   [1] {ECO:0000313|EMBL:EOT29959.1, ECO:0000313|Proteomes:UP000014136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43076 {ECO:0000313|EMBL:EOT29959.1,
RC   ECO:0000313|Proteomes:UP000014136};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus saccharolyticus ATCC_43076 (Illumina
RT   only assembly).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002631,
CC       ECO:0000256|HAMAP-Rule:MF_00148, ECO:0000256|RuleBase:RU003780}.
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:0000256|ARBA:ARBA00001400, ECO:0000256|HAMAP-
CC         Rule:MF_00148, ECO:0000256|RuleBase:RU003780};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00148}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000256|ARBA:ARBA00008184, ECO:0000256|HAMAP-
CC       Rule:MF_00148, ECO:0000256|RuleBase:RU003780}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOT29959.1}.
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DR   EMBL; AHYT01000002; EOT29959.1; -; Genomic_DNA.
DR   RefSeq; WP_016174457.1; NZ_KE136523.1.
DR   AlphaFoldDB; S0NRJ5; -.
DR   STRING; 41997.RV16_GL001856; -.
DR   PATRIC; fig|1139996.3.peg.645; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_0_9; -.
DR   OrthoDB; 9804372at2; -.
DR   Proteomes; UP000014136; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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; Uracil-DNA glycosylase-like domain; 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   NCBIfam; TIGR00628; ung; 1.
DR   PANTHER; PTHR11264; URACIL-DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR11264:SF0; URACIL-DNA GLYCOSYLASE; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SMART; SM00987; UreE_C; 1.
DR   SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00148};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00148};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00148};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00148};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014136}.
FT   DOMAIN          50..210
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00148,
FT                   ECO:0000256|PROSITE-ProRule:PRU10072"
SQ   SEQUENCE   226 AA;  25946 MW;  4A2A8E15CC78625A CRC64;
     MKTIIHNSWQ DILQAEFQKP YYLELREFLK QEYSTQRIFP DMYHIFEALE KTPYEKVKVV
     ILGQDPYHGA NQAHGLSFSV QPSVKIPPSL KNIYKELADD LGIAPVTHGY LTSWAEQGVL
     LLNTVLTVRE GQAYSHRGKG WEQLTDAIIQ KLNEREQPIV FILWGKPAQQ KMSMIDTHKH
     IIIRSVHPSP LSAHRGFFGS KPFSKTNDAL MALGETPINW QLPERV
//
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