ID A0A498G986_9EURY Unreviewed; 307 AA.
AC A0A498G986;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
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=D3D02_05105 {ECO:0000313|EMBL:RLM90156.1};
OS Halobellus sp. Atlit-38R.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=2282131 {ECO:0000313|EMBL:RLM90156.1, ECO:0000313|Proteomes:UP000277703};
RN [1] {ECO:0000313|EMBL:RLM90156.1, ECO:0000313|Proteomes:UP000277703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Atlit-38R {ECO:0000313|EMBL:RLM90156.1,
RC ECO:0000313|Proteomes:UP000277703};
RA Turgeman-Grott I.;
RT "Pervasive acquisition of CRISPR memory from multiple replicons driven by
RT inter-species mating of archaea.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18;
CC Evidence={ECO:0000256|ARBA:ARBA00024490};
CC -!- SIMILARITY: Belongs to the type-1 OGG1 family.
CC {ECO:0000256|ARBA:ARBA00010679}.
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:RLM90156.1}.
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DR EMBL; QXIJ01000003; RLM90156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498G986; -.
DR OrthoDB; 14922at2157; -.
DR Proteomes; UP000277703; Unassembled WGS sequence.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 3.30.310.260; -; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR012904; OGG_N.
DR PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR10242:SF2; N-GLYCOSYLASE_DNA LYASE; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55945; TATA-box binding protein-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000277703}.
FT DOMAIN 138..302
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 307 AA; 34401 MW; 38AB74E0FA5C0CE3 CRC64;
MTFESGAIPL SSIPGPFDLQ ATLESGQSYL WDRADGRMYE SMDVYGGDAW YETVVPPVDG
VTDEDVVVRV RQRDGDLLWE ATTDPVPLLT HLLRLDDDLD AIYAATPDDD LIERAYDAYR
GMRLVRDPPF PCLVSFICSA QMRVSRIHGM QMALASEFGT HHEVDGETFE AFPTPAQLAA
QSEDDLRDLK LGYRAPYVQR TAAMVADGEA HPREAVGRDY EDAREHLTQF VGVGDKVADC
VLLFSLGYLE AVPLDTWIQS AIAEHFPECD RGNYTETSRA LRERLGGEYA GYAQTYLFYY
LRARGDD
//
