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Database: UniProt
Entry: B0T7V6_CAUSK
LinkDB: B0T7V6_CAUSK
Original site: B0T7V6_CAUSK 
ID   B0T7V6_CAUSK            Unreviewed;       272 AA.
AC   B0T7V6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00019403};
DE            EC=3.2.2.27 {ECO:0000256|ARBA:ARBA00012030};
GN   OrderedLocusNames=Caul_2166 {ECO:0000313|EMBL:ABZ71294.1};
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ71294.1};
RN   [1] {ECO:0000313|EMBL:ABZ71294.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31 {ECO:0000313|EMBL:ABZ71294.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) 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}.
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DR   EMBL; CP000927; ABZ71294.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0T7V6; -.
DR   STRING; 366602.Caul_2166; -.
DR   KEGG; cak:Caul_2166; -.
DR   eggNOG; COG1573; Bacteria.
DR   HOGENOM; CLU_044815_1_0_5; -.
DR   OrthoDB; 5290748at2; -.
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          108..259
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
SQ   SEQUENCE   272 AA;  28806 MW;  C9790B0DF326C143 CRC64;
     MNLAVDPRAV ESLLAFWADA GVEASYADDP IDRLAQGAAM LRARKEPAPV AVAPVVTPVL
     GRGPDLGAAI AEAKALAAAC ADLPALAAAI AAFDGCPLKT QGARQAVVSR GPADAPLMII
     GEAPGADEDL QGAPFVGRAG QLLDRMLKAA GLLDRAFVTN TVFWRPPGNR TPTPQEQAVC
     APFLERAIAL VQPKILLLVG GASAKSLLRR DEGILSLRGR WFEWTSSDGQ NELPALPTLH
     PAFLLRQPAA KKKAWTDMLM LSERLDRPER PH
//
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