ID A0A1H1FRG6_9FLAO Unreviewed; 254 AA.
AC A0A1H1FRG6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN ORFNames=SAMN05421664_3210 {ECO:0000313|EMBL:SDR03358.1};
OS Chryseobacterium soldanellicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=311333 {ECO:0000313|EMBL:SDR03358.1, ECO:0000313|Proteomes:UP000199627};
RN [1] {ECO:0000313|EMBL:SDR03358.1, ECO:0000313|Proteomes:UP000199627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17072 {ECO:0000313|EMBL:SDR03358.1,
RC ECO:0000313|Proteomes:UP000199627};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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DR EMBL; FNKL01000004; SDR03358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1FRG6; -.
DR STRING; 311333.SAMN05421664_3210; -.
DR Proteomes; UP000199627; Unassembled WGS sequence.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR Gene3D; 1.10.8.50; -; 1.
DR Gene3D; 3.20.190.10; MutM-like, N-terminal; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR PANTHER; PTHR22993:SF30; DNA GLYCOSYLASE_AP LYASE H2TH DNA-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM00898; Fapy_DNA_glyco; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000313|EMBL:SDR03358.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000313|EMBL:SDR03358.1}.
FT DOMAIN 12..101
FT /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51068"
SQ SEQUENCE 254 AA; 29479 MW; 7B3BB3D4D518D570 CRC64;
MYLIQVYIQH MPEGPSILLM KEDLQKFAGK KVVKADGNAK FEKEPLEGKI LKEIRTFGKQ
TYLVFDEISV RIHLLMFGSY SIDEQTKPDK SLRLSLQFKV GGMYFYTCSV KLIDSKGLEK
IDWEADIMSE EWNPEKAEKK LKSNPEMMVC DALMNQDIFS GVGNIIKNEV LFRIGVQPES
LLGNMPPKKI KELITEARNY SFDFLKWKRD FVLKKHWLAH TKTVCPKCGE KLIKKQTGKG
KRRSFYCVND QTLY
//
