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Database: UniProt
Entry: F2S7T4_TRIT1
LinkDB: F2S7T4_TRIT1
Original site: F2S7T4_TRIT1 
ID   F2S7T4_TRIT1            Unreviewed;       360 AA.
AC   F2S7T4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=TESG_06978 {ECO:0000313|EMBL:EGD99633.1};
OS   Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=647933;
RN   [1] {ECO:0000313|EMBL:EGD99633.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112818 {ECO:0000313|EMBL:EGD99633.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA   Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA   Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA   Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA   Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; GG698524; EGD99633.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2S7T4; -.
DR   HOGENOM; CLU_027543_4_0_1; -.
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: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   Lyase {ECO:0000313|EMBL:EGD99633.1}.
FT   DOMAIN          81..269
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
FT   REGION          162..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   360 AA;  40288 MW;  E5D2805ABF337B8C CRC64;
     MSGRARSTTC PILKQDSDSL CTDHLNLQAL IHHYFNLEYN LSDLYEQWAA SDPNFKKKAV
     QFAGIRIMRQ DAWETLVSFI CSSNNNIARI SQMVEKLCIN YGPFIGQLGD QKYYDFPEPS
     ALTGNGVESH LRELGFGYRA KYIYQTANIV ANQREPGWLN SLRNPEKPAF NEKPATPGSG
     AKGDKSGYRE AHEQLLALQG VGPKVADCVC LMGLGWGESV PVDTHVWQIA QRDYKFGKGK
     QKTLNKATYD AVGDHFRELW GKEAGWAQSV LFTANLRSFS DRLNPKSGIH DQTTETLKVE
     SKVEAAQVKE EVEEDGIRVT TRISVKRELS EGENTGPKDN PSASEPAPKK RRTQASRSRK
//
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