ID A0A2A8CV18_9BACT Unreviewed; 323 AA.
AC A0A2A8CV18;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-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=CRI94_13610 {ECO:0000313|EMBL:PEN12555.1};
OS Longibacter salinarum.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC Longibacter.
OX NCBI_TaxID=1850348 {ECO:0000313|EMBL:PEN12555.1, ECO:0000313|Proteomes:UP000220102};
RN [1] {ECO:0000313|EMBL:PEN12555.1, ECO:0000313|Proteomes:UP000220102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52045 {ECO:0000313|EMBL:PEN12555.1,
RC ECO:0000313|Proteomes:UP000220102};
RA Goh K.M., Shamsir M.S., Lim S.W.;
RT "Draft genome of Longibacter Salinarum.";
RL Submitted (OCT-2017) 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:PEN12555.1}.
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DR EMBL; PDEQ01000007; PEN12555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8CV18; -.
DR OrthoDB; 5290748at2; -.
DR Proteomes; UP000220102; 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:UP000220102}.
FT DOMAIN 164..310
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 35140 MW; 5ED36205FB47EBE0 CRC64;
MRSLLQELRG VIEREASLHG PLVPLDAPPT DTDEDASATE DDAPTVNESS PSNTYSQPGE
AATDDASSVD ADDLPAPSTA SDASAGDALS STSSSNDASM PNQDLFGNEV DPTEDPSRPP
SERIEALIPD DAPYKDIDSL AELEKWVAEN TLVPIDEDRK NPVFGVGDPN ADLLIIGEAP
GANEDEQGEP FVGRAGKLLD KILQAIEFDR QDVYIANILK SRPPNNRDPL AEEVEAHIPI
LYKQIALIQP AIILCVGKVA TNTMLDRRSS LGSLREKEHD FYGIPLYATY HPAALLRNSN
WKRPTWEDVK LVRTRYDELT GTS
//
