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Database: UniProt
Entry: A0A095V3E8_9BURK
LinkDB: A0A095V3E8_9BURK
Original site: A0A095V3E8_9BURK 
ID   A0A095V3E8_9BURK        Unreviewed;       310 AA.
AC   A0A095V3E8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00019403};
DE            EC=3.2.2.27 {ECO:0000256|ARBA:ARBA00012030};
GN   ORFNames=JL37_08840 {ECO:0000313|EMBL:KGD95896.1};
OS   Achromobacter sp. RTa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1532557 {ECO:0000313|EMBL:KGD95896.1, ECO:0000313|Proteomes:UP000035841};
RN   [1] {ECO:0000313|EMBL:KGD95896.1, ECO:0000313|Proteomes:UP000035841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RTa {ECO:0000313|EMBL:KGD95896.1,
RC   ECO:0000313|Proteomes:UP000035841};
RA   Prabhakaran M., Cougar B., Weirick T., Fathepure B.Z.;
RT   "Genome sequences of the lignin degrading proteobacteria.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       Type 4 (UDGa) family. {ECO:0000256|ARBA:ARBA00006521}.
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:KGD95896.1}.
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DR   EMBL; JPYO01000027; KGD95896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A095V3E8; -.
DR   eggNOG; COG1573; Bacteria.
DR   Proteomes; UP000035841; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd10030; UDG-F4_TTUDGA_SPO1dp_like; 1.
DR   Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR   InterPro; IPR005273; Ura-DNA_glyco_family4.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   NCBIfam; TIGR00758; UDG_fam4; 1.
DR   PANTHER; PTHR33693:SF1; TYPE-4 URACIL-DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR33693; TYPE-5 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.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          152..304
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
FT   REGION          75..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  33152 MW;  C0E1E45D5B4EB244 CRC64;
     MTPVSTPAPA APRVNPLQRI WLREIGMERL WLRPAPAASR PAAEPQVPVS KPVFPVSAPA
     AEAPAVEVAA RPAAPATPAA EPVPGRPGIP ASILNRKGPP PPPPPKVVAE AEAPAPIPVA
     EAIRNSTLDE MREQVVSCEA CGLCKGRRNA VFGHGGQPTR WLVVGEAPGE QEDRQGQPFV
     GRSGQLLDAM LSAVSMSRER DVFITNVIKC RPPGNRNPKP EEIAACSPYL MRQIALLKPE
     RILVLGRFAA QTLLGTDATI GSLRGRIHQL KTDEGVQIPV VVSYHPAYLL RSPGEKARAW
     QDLKLAARMG
//
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