ID A0A1R3WRR8_9MICO Unreviewed; 258 AA.
AC A0A1R3WRR8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05880579_0893 {ECO:0000313|EMBL:SIT80701.1};
OS Microbacterium sp. RU1D.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1907411 {ECO:0000313|EMBL:SIT80701.1, ECO:0000313|Proteomes:UP000187105};
RN [1] {ECO:0000313|EMBL:SIT80701.1, ECO:0000313|Proteomes:UP000187105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1D {ECO:0000313|EMBL:SIT80701.1,
RC ECO:0000313|Proteomes:UP000187105};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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DR EMBL; FTPQ01000001; SIT80701.1; -; Genomic_DNA.
DR RefSeq; WP_076673582.1; NZ_FTPQ01000001.1.
DR AlphaFoldDB; A0A1R3WRR8; -.
DR Proteomes; UP000187105; 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 CDD; cd08971; AcNei2_N; 1.
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; IPR044090; Nei2_N.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR PANTHER; PTHR42697; ENDONUCLEASE 8; 1.
DR PANTHER; PTHR42697:SF1; ENDONUCLEASE 8; 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 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.
DR PROSITE; PS51066; ZF_FPG_2; 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:SIT80701.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000313|EMBL:SIT80701.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00391}.
FT DOMAIN 2..158
FT /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51068"
FT DOMAIN 218..257
FT /note="FPG-type"
FT /evidence="ECO:0000259|PROSITE:PS51066"
SQ SEQUENCE 258 AA; 28525 MW; 1AD51A37E7DF1330 CRC64;
MPEGDTVYRA AAKMNAALAG RVVTRFDIRV PGSATADLRG ETVHEVAARG KHLLHRMGGY
TLHSHLKMEG RWDLYRPGQR WRRPAFKARA IVGVEGMDAV GFDLAMVEVL RTTDEHTVIG
HLGPDLLADD WDEAEAVRRV SLDDRAAHVA LLDQRNVAGF GNVYANELLF VRGIAPTTPA
TEIDARATIA LGERMIRANL PRPERTFTGD NRPGRRFWVY GREGAPCRRC GTPIRATTLG
ASDTSERNVF WCPTCQPG
//
