ID G0TUD8_TRYVY Unreviewed; 478 AA.
AC G0TUD8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=TVY486_0402380 {ECO:0000313|EMBL:CCC47572.1};
OS Trypanosoma vivax (strain Y486).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Duttonella.
OX NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCC47572.1};
RN [1] {ECO:0000313|EMBL:CCC47572.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y486 {ECO:0000313|EMBL:CCC47572.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE573020; CCC47572.1; -; Genomic_DNA.
DR AlphaFoldDB; G0TUD8; -.
DR VEuPathDB; TriTrypDB:TvY486_0402380; -.
DR OrthoDB; 118473at2759; -.
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: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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..478
FT /note="DNA-(apurinic or apyrimidinic site) lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003409815"
FT DOMAIN 217..392
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 478 AA; 53560 MW; 456AADF866021970 CRC64;
MHCWHVLAPA SAVHLPMTLC GGQCFRWRRT PRGTYVGVVR RIAYELANFS SCHTLPFQKD
CHDSTPGFVV PAGVGSVKDE GDVPSGCLWF RCLNCELRDS SEVESQAVFL RHYLAVDVDL
EKMWEQWTAE NPMCGHPLVR YLTLHSSLKL PVKIRHLRQE LHETLFAFLC SQNNNVQRIT
SLIERLSLKY GDHLCDYNLE TGDVRCFDHV CKLHRKRAAR CGQEAAEERN QWIALHVLPT
VEQLSAATED ELRSLGFGYR SNYIIGCTNV IRQSGVVGRE VLSEHCRGAT KFSESTVVPS
YRWYEELLSP NCTLEERRAK LLTLPGVGRK VADCVLLFGL GHHELVPVDT HMAQVAAEYL
ASSGGAGSYG RREGGRLKGG KRARVNDSRS RLRGVNDIEE NQRGDSTWEA VVAGWRMGNG
EGKNKLPPLL PKHHDAIQVG FRSLFGEYCG WAHSILFYAR MRTGAAAMNR LAEGAVSV
//
