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Database: UniProt
Entry: A0A1G2TFQ6_9BACT
LinkDB: A0A1G2TFQ6_9BACT
Original site: A0A1G2TFQ6_9BACT 
ID   A0A1G2TFQ6_9BACT        Unreviewed;       196 AA.
AC   A0A1G2TFQ6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00019403};
DE            EC=3.2.2.27 {ECO:0000256|ARBA:ARBA00012030};
GN   ORFNames=A3C70_02770 {ECO:0000313|EMBL:OHA96116.1};
OS   Candidatus Zambryskibacteria bacterium RIFCSPHIGHO2_02_FULL_43_14.
OC   Bacteria; Candidatus Zambryskibacteria.
OX   NCBI_TaxID=1802748 {ECO:0000313|EMBL:OHA96116.1, ECO:0000313|Proteomes:UP000178175};
RN   [1] {ECO:0000313|EMBL:OHA96116.1, ECO:0000313|Proteomes:UP000178175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHA96116.1}.
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DR   EMBL; MHVR01000011; OHA96116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2TFQ6; -.
DR   Proteomes; UP000178175; 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          36..188
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
SQ   SEQUENCE   196 AA;  22140 MW;  484DAAEF749CA3BC CRC64;
     MNYQDEALKK IKDEVVELSA SPLYAERVKN KYFPVIGEGS HSAQILFVGE APGENEAKTG
     RPFCGRAGKV LDDLLVSVGI VRSDVYVTNI VKDRPPGNRD PFPDEIEIYA PFLDRQIKII
     KPKMVATLGR FSMQYIMSRY GLEWELDSIS KLHGKVFDTA DFKFVPLYHP AAAIYNQHLL
     DTLKEDFKIL KTCGIV
//
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