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Database: UniProt
Entry: A7TNQ1_VANPO
LinkDB: A7TNQ1_VANPO
Original site: A7TNQ1_VANPO 
ID   A7TNQ1_VANPO            Unreviewed;       373 AA.
AC   A7TNQ1;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 69.
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=Kpol_1001p14 {ECO:0000313|EMBL:EDO16102.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO16102.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480433; EDO16102.1; -; Genomic_DNA.
DR   RefSeq; XP_001643960.1; XM_001643910.1.
DR   AlphaFoldDB; A7TNQ1; -.
DR   STRING; 436907.A7TNQ1; -.
DR   GeneID; 5544245; -.
DR   KEGG; vpo:Kpol_1001p14; -.
DR   eggNOG; KOG2875; Eukaryota.
DR   HOGENOM; CLU_027543_3_1_1; -.
DR   InParanoid; A7TNQ1; -.
DR   OMA; ITKMCHS; -.
DR   OrthoDB; 118473at2759; -.
DR   PhylomeDB; A7TNQ1; -.
DR   Proteomes; UP000000267; 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:UP000000267}.
FT   DOMAIN          134..309
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
FT   REGION          351..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  42716 MW;  F2D85F713A0027F8 CRC64;
     MTVSKFGRFL VSKEELCLTN VLQVGQSFRW IFDEKLNQYS SSLKVGNDEK YALVVLRQNS
     SNGEDFVEFG SVGGDCELGT LDSHLRNYFR LDVSVNDLYS TQWLPRDDRF KSHSPSGNRI
     LAQEPWETLV SFICSSNNNI SRITKMCHEL CSKFGNKIGT LGDVDYYSFP SSDDIVERSS
     EEELRKLGFG YRAKYIIDTA KMMVEDKTAN GYTSDTQYLM ELGSKLTYEQ LREHLMRYSG
     VGPKVADCVC LMGFKMDHVV PIDTHVSRIA KRDYNFQAAK NKIKDLSKKY TEYPITRKKI
     NMELDLTRLM FVEKWGEYAG WAQGILFSNE VGNANGATST GKIKKRELEV KPEVKEENTT
     VNSKTKRVKR QSY
//
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