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Database: UniProt
Entry: R7RUS8_9CLOT
LinkDB: R7RUS8_9CLOT
Original site: R7RUS8_9CLOT 
ID   R7RUS8_9CLOT            Unreviewed;       190 AA.
AC   R7RUS8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00019403};
DE            EC=3.2.2.27 {ECO:0000256|ARBA:ARBA00012030};
GN   ORFNames=TCEL_02379 {ECO:0000313|EMBL:CDF59311.1};
OS   Thermobrachium celere DSM 8682.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Thermobrachium.
OX   NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF59311.1, ECO:0000313|Proteomes:UP000014923};
RN   [1] {ECO:0000313|EMBL:CDF59311.1, ECO:0000313|Proteomes:UP000014923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF59311.1,
RC   ECO:0000313|Proteomes:UP000014923};
RA   Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT   "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT   alkalithermophilic Caloramator celere.";
RL   Submitted (MAR-2013) 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:CDF59311.1}.
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DR   EMBL; CAVN010000162; CDF59311.1; -; Genomic_DNA.
DR   RefSeq; WP_018666968.1; NZ_HF952041.1.
DR   AlphaFoldDB; R7RUS8; -.
DR   eggNOG; COG1573; Bacteria.
DR   HOGENOM; CLU_044815_1_3_9; -.
DR   OrthoDB; 5290748at2; -.
DR   Proteomes; UP000014923; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014923}.
FT   DOMAIN          26..180
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
SQ   SEQUENCE   190 AA;  21771 MW;  3FA30AEC181DCCB6 CRC64;
     MDLTTIYKEY SDKIKEVFGE DRKIVYGDGN TNADIMLIGE APGRFEEEQG KPFVGQAGKN
     LDEFIDILEI KREDLFITNV VKVRPYKINE KTGRKVNRAP NKKEIELSLD TLLKEIEIVS
     PKIIVTLGNT PLKALLGDVK IGDVHGKLIE YNGRFIYPLY HPASIIYNRS LYDVYIEDLK
     NLKKYIKSNC
//
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