ID A0A0C5VLU6_9GAMM Unreviewed; 209 AA.
AC A0A0C5VLU6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00012030, 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=YC6258_02280 {ECO:0000313|EMBL:AJQ94318.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ94318.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ94318.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ94318.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) 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}.
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DR EMBL; CP007142; AJQ94318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C5VLU6; -.
DR STRING; 1445510.YC6258_02280; -.
DR KEGG; gsn:YC6258_02280; -.
DR PATRIC; fig|1445510.3.peg.2237; -.
DR HOGENOM; CLU_032162_3_1_6; -.
DR Proteomes; UP000032266; Chromosome.
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:UP000032266}.
FT DOMAIN 33..193
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00148,
FT ECO:0000256|PROSITE-ProRule:PRU10072"
SQ SEQUENCE 209 AA; 23877 MW; 20C91133C8B50773 CRC64;
MDYMKSLKHF LKHEKASGKQ IYPRGEEYFR AFDLTPFEQT KVVILGQDPY HGEHQAHGLC
FSVRPEVRVP PSLINIYKEL NRDIGFTIPN HGYLESWAHQ GVLLLNSVLT VEAGRAAAHQ
GKGWEQFTDR VIAVINEQLD NVVFMLWGSY AQRKGQFIDT RRHLVLKTTH PSPLSAHRGF
LGCGHFSQAN AYLQQCGRTP VNWQLPLQV
//
