ID S7PHG9_MYOBR Unreviewed; 333 AA.
AC S7PHG9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=D623_10028344 {ECO:0000313|EMBL:EPQ10113.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ10113.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues.
CC Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-
CC methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase
CC activity that nicks DNA 3' to the lesion.
CC {ECO:0000256|ARBA:ARBA00025652}.
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; KE162937; EPQ10113.1; -; Genomic_DNA.
DR RefSeq; XP_014398256.1; XM_014542770.1.
DR AlphaFoldDB; S7PHG9; -.
DR GeneID; 102241967; -.
DR CTD; 4968; -.
DR eggNOG; KOG2875; Eukaryota.
DR OrthoDB; 118473at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IEA:InterPro.
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:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 3.30.310.40; -; 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; IPR004577; Ogg1.
DR InterPro; IPR012904; OGG_N.
DR NCBIfam; TIGR00588; ogg; 1.
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 Lyase {ECO:0000313|EMBL:EPQ10113.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 136..306
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT REGION 314..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 37465 MW; E0FFABA888043217 CRC64;
MGHRTLSSVP ALWASIPCPR SELRLDLVLA SGQSFRWKEQ NPAHWSGVLA DQVWTLTQTE
EQLYCTVYRG EKGQAGRPTP GELKALRQYF QLDVSLAQLY RHWSSKDPHF QKVAQKFQGV
RLLQQDPIEC LFSFICSSNN NIARITGMVE RLCQAFGPRL IQLDDVTYHG FPSLQALAGP
EVEAKLRKLG LGYRARYVNA SARAILEEQG GLPWLQQLRK APYEEAHKAL CTLPGVGTKV
ADCICLMALD KPQAVPVDVH VWQIAQRDYS WHPTTTQGKG PSPQANKELG NFFRNLWGPY
AGWAQAVLFS ADLRQPHQEP PAKRRKRSTG PEV
//