ID D8PSM5_SCHCM Unreviewed; 332 AA.
AC D8PSM5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
DE Flags: Fragment;
GN ORFNames=SCHCODRAFT_66004 {ECO:0000313|EMBL:EFJ00361.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ00361.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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}.
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DR EMBL; GL377303; EFJ00361.1; -; Genomic_DNA.
DR RefSeq; XP_003035263.1; XM_003035217.1.
DR AlphaFoldDB; D8PSM5; -.
DR STRING; 578458.D8PSM5; -.
DR GeneID; 9596091; -.
DR KEGG; scm:SCHCO_02661242; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02661242; -.
DR eggNOG; KOG2875; Eukaryota.
DR HOGENOM; CLU_027543_3_2_1; -.
DR InParanoid; D8PSM5; -.
DR OMA; GYAQEYL; -.
DR OrthoDB; 118473at2759; -.
DR Proteomes; UP000007431; 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; 3.30.310.40; -; 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:UP000007431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..332
FT /note="DNA-(apurinic or apyrimidinic site) lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003120233"
FT DOMAIN 148..325
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT NON_TER 332
FT /evidence="ECO:0000313|EMBL:EFJ00361.1"
SQ SEQUENCE 332 AA; 37260 MW; FCF7AAC2CA978643 CRC64;
MAASIPAGFQ ALPLPIIQLS LAAVLKCGQS FRWSILELPS DSAASACHLP HEYRLCLKDR
VVCLRQSTDH LFYCSVFPQA TPTDTASKLK DAETLLWLRD YFQLDVDLVK LYREWAERDP
VFLKIQDRFA GIRMLRQDPW ENLVSFICSS NNNISRITKM VQNLCREYSP PLLSLPNALG
ELETYHPFPP PSALAEPEVA TRLRALGFGY RADFIHKTAK MLVDAHGEDP AAADRWLGGL
RTRSTNEARE ELLKFMGVGR KVADCVLLMS LDKREVIPVD THVHQIAAKH YGLKVGGKST
NGKVPMTPKI YDEVNTKLVG IWGEYAGWAH SV
//
