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Database: UniProt
Entry: A0A135W097_9ARCH
LinkDB: A0A135W097_9ARCH
Original site: A0A135W097_9ARCH 
ID   A0A135W097_9ARCH        Unreviewed;       281 AA.
AC   A0A135W097;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=AM324_10780 {ECO:0000313|EMBL:KXH78142.1};
OS   Candidatus Thorarchaeota archaeon SMTZ1-83.
OC   Archaea; Asgard group; Candidatus Thorarchaeota.
OX   NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH78142.1, ECO:0000313|Proteomes:UP000070043};
RN   [1] {ECO:0000313|EMBL:KXH78142.1, ECO:0000313|Proteomes:UP000070043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH78142.1};
RX   PubMed=26824177;
RA   Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT   "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT   phylum with pathways for acetogenesis and sulfur reduction.";
RL   ISME J. 0:0-0(2016).
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:KXH78142.1}.
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DR   EMBL; LRSK01000004; KXH78142.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135W097; -.
DR   Proteomes; UP000070043; 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; 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}.
FT   DOMAIN          108..273
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   281 AA;  32280 MW;  B5E81AFF7B33493C CRC64;
     MRELVIEGFD LVDTLECGQT FSWIREGRGY VNSDIGQVVY VEQRGNTLYY DSSDHDVDLQ
     KMFRLNDPLT EIQRKIARDG IMKESIQFAP GLRVISDEFF PCLVSFLCSI RNNIPNIRKF
     TQSIRREFGP TYSYRGAVYH GFPSPVDLSR ATENQLQALG LDWRANFIVR STKSILEDNI
     DATELSRQGY EEAHARLKEL HGVGDKVADC VCLFSLGFLE AFPIDVWIER VIQKHYGIFT
     TAGKSYGKKS EAAREYFGEY AGYAQEYLYY YTRTGGRKPS R
//
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