ID A0A1F5X027_9BACT Unreviewed; 197 AA.
AC A0A1F5X027;
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=A2930_02165 {ECO:0000313|EMBL:OGF81244.1};
OS Candidatus Giovannonibacteria bacterium RIFCSPLOWO2_01_FULL_45_34.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1798351 {ECO:0000313|EMBL:OGF81244.1, ECO:0000313|Proteomes:UP000178114};
RN [1] {ECO:0000313|EMBL:OGF81244.1, ECO:0000313|Proteomes:UP000178114}
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:OGF81244.1}.
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DR EMBL; MFID01000014; OGF81244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5X027; -.
DR STRING; 1798351.A2930_02165; -.
DR Proteomes; UP000178114; 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 30..186
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
SQ SEQUENCE 197 AA; 22205 MW; F08227F8F78D0C81 CRC64;
MDKRFELEKL KNEIEADKSL PTYGAANLVF GEGNPEAEVM FIGEAPGFHE NKLGRPFVGR
AGQLLNKLLA DIGWPRESVY ITNIIKRRPP KNRDPLPKEI KAYEPYLKKQ IKIINPKIIA
PLGRFAMNYF LPSAKISQNH GLPSEVLTEE GQRLIICPLY HPAAALRSTA VLNCLEHDFR
KLPKLLKANI NAKIKGK
//