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Database: UniProt
Entry: A0A1W2BHP8_9FLAO
LinkDB: A0A1W2BHP8_9FLAO
Original site: A0A1W2BHP8_9FLAO 
ID   A0A1W2BHP8_9FLAO        Unreviewed;       221 AA.
AC   A0A1W2BHP8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN05660703_2401 {ECO:0000313|EMBL:SMC72290.1};
OS   Cellulophaga tyrosinoxydans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=504486 {ECO:0000313|EMBL:SMC72290.1, ECO:0000313|Proteomes:UP000192360};
RN   [1] {ECO:0000313|EMBL:SMC72290.1, ECO:0000313|Proteomes:UP000192360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21164 {ECO:0000313|EMBL:SMC72290.1,
RC   ECO:0000313|Proteomes:UP000192360};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FWXO01000004; SMC72290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2BHP8; -.
DR   STRING; 504486.SAMN05660703_2401; -.
DR   OrthoDB; 9804372at2; -.
DR   Proteomes; UP000192360; 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:UP000192360}.
FT   DOMAIN          50..211
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   221 AA;  25234 MW;  B9F5713D93DE2149 CRC64;
     MELTIQESWK NTLKEEFEKP YFLDLMDFVE KEYAMHTCYP EMSSVFAAFN ACSFQDTRVV
     ILGQDPYHGP NQANGLCFSV KNTVPHPPSL QNIFKEISLD LGTNYPESGD LERWAQQGVL
     LLNATLTVRA HEAGSHQKKG WEQFTDAVIK KISSEKNAVI FMLWGGYAKK KIKLIDTEKH
     HILSSGHPSP LSANRGYWFG NKHFSRANYL LEKTGNSKIM W
//
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