ID S7XSF1_SPRLO Unreviewed; 331 AA.
AC S7XSF1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-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=SLOPH_80 {ECO:0000313|EMBL:EPR78843.1};
OS Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC Spraguea.
OX NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR78843.1, ECO:0000313|Proteomes:UP000014978};
RN [1] {ECO:0000313|Proteomes:UP000014978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA Williams B.A.P.;
RT "The genome of Spraguea lophii and the basis of host-microsporidian
RT interactions.";
RL PLoS Genet. 9:E1003676-E1003676(2013).
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:EPR78843.1}.
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DR EMBL; ATCN01000529; EPR78843.1; -; Genomic_DNA.
DR AlphaFoldDB; S7XSF1; -.
DR STRING; 1358809.S7XSF1; -.
DR VEuPathDB; MicrosporidiaDB:SLOPH_80; -.
DR HOGENOM; CLU_027543_3_1_1; -.
DR InParanoid; S7XSF1; -.
DR OMA; GYAQEYL; -.
DR OrthoDB; 118473at2759; -.
DR Proteomes; UP000014978; 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:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProt.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 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:UP000014978}.
FT DOMAIN 137..319
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 331 AA; 39029 MW; 79EBC6124845F6AA CRC64;
MYYKYNISEK VNLDLTLYSG QIFSFKKIGD VHIGVIRGIL FYLRDKITES ELKDITIVNE
TENNSEYKYN LYFKYDCENL TPHSAISILS DFFTLDIDYA KLKEVWSLSN IYNFSNNLNG
LRLLRLDLTE TIFSFICSAN NTVKRITGMV EYLLSKGEFI KEIDGNKFYK FPTVFKLSEI
EEDELRNKKF GYRAKYIVQT AKKLYKVITE KHKENNTSYQ HNDNIKELNF LRKLSYDHAL
KYLISLHGIG RKVADCICLM GLYHYDAVPI DVHIFRKSKE IFKNVSDTEN IKNLNKSNYN
KIVELYNKYF IEKIGIAQLF IFYDSMANNK K
//
