UNG_SINMW
ID UNG_SINMW Reviewed; 241 AA.
AC A6UDC0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Smed_2820;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) 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: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; CP000738; ABR61650.1; -; Genomic_DNA.
DR RefSeq; WP_012067035.1; NC_009636.1.
DR RefSeq; YP_001328485.1; NC_009636.1.
DR AlphaFoldDB; A6UDC0; -.
DR SMR; A6UDC0; -.
DR STRING; 366394.Smed_2820; -.
DR EnsemblBacteria; ABR61650; ABR61650; Smed_2820.
DR GeneID; 61611648; -.
DR KEGG; smd:Smed_2820; -.
DR PATRIC; fig|366394.8.peg.6028; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_3_1_5; -.
DR OMA; PDNGYLM; -.
DR OrthoDB; 1260295at2; -.
DR Proteomes; UP000001108; 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; -; 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 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; Hydrolase.
FT CHAIN 1..241
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_1000009941"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ SEQUENCE 241 AA; 27138 MW; 18B29FFD11FF90DE CRC64;
MDSTIRLEES WKAALGPEFR NGYMTELKRF LLDEKQQGRQ VFPRGGEYFR ALDLTPLDRV
RVVILGQDPY HGDGQAHGLC FSVRPGVRTP PSLVNIYKEL KEDLGIDPAR HGFLESWARQ
GVLLLNSVLT VERGRAASHQ GRGWERFTDA VIRAVNEQAQ PVVFMLWGSY AQRKAAFVDR
SRHLVLTAPH PSPLSAHSGF FGCRHFSKAN AFLTSKGLDP IDWRLPEDPP LAVERPTPPN
C