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Database: UniProt
Entry: A0A109BJI2_HYPSL
LinkDB: A0A109BJI2_HYPSL
Original site: A0A109BJI2_HYPSL 
ID   A0A109BJI2_HYPSL        Unreviewed;       311 AA.
AC   A0A109BJI2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00019403};
DE            EC=3.2.2.27 {ECO:0000256|ARBA:ARBA00012030};
GN   ORFNames=APY04_1334 {ECO:0000313|EMBL:KWT69834.1};
OS   Hyphomicrobium sulfonivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT69834.1, ECO:0000313|Proteomes:UP000059074};
RN   [1] {ECO:0000313|EMBL:KWT69834.1, ECO:0000313|Proteomes:UP000059074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDL6 {ECO:0000313|EMBL:KWT69834.1,
RC   ECO:0000313|Proteomes:UP000059074};
RA   Albers P.;
RT   "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT   consortium.";
RL   Submitted (OCT-2015) 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:KWT69834.1}.
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DR   EMBL; LMTR01000043; KWT69834.1; -; Genomic_DNA.
DR   RefSeq; WP_068460857.1; NZ_LMTR01000043.1.
DR   AlphaFoldDB; A0A109BJI2; -.
DR   STRING; 121290.APY04_1334; -.
DR   PATRIC; fig|121290.4.peg.2215; -.
DR   OMA; HFHADAG; -.
DR   OrthoDB; 5290748at2; -.
DR   Proteomes; UP000059074; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059074}.
FT   DOMAIN          153..303
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
SQ   SEQUENCE   311 AA;  32774 MW;  E6019370E8F9A418 CRC64;
     MSSDSNRDIE AQRAAGRILA WYAAMGVDAA ISDTAVDWLA RGEQAPGQGF RLLADAGQAP
     QGAQAFSQGN IAARGPGAPA RPLPTGVPQR PPYAGAAAPA QPARQFSVRP AAAPADAAPV
     VDLANINTLA DLGSALAAFD GCGLKATAKN LCFYRGAERA PLMIIGEAPG RDEDLAGKPF
     VGRAGQLLDR MLAAIDVDET NVHITNIVYW RPPGNRTPTP QEAIACRPFL EKQIALVAPR
     IVLALGGAAA KQLFDVADGI MRLRGKWRPF AVNGQEYKSM ATLHPAYLLR TPAAKNMAWR
     DLLNVKAALK S
//
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