(data stored in SCRATCH zone)

SWISSPROT: Q6BMM3_DEBHA

ID   Q6BMM3_DEBHA            Unreviewed;       375 AA.
AC   Q6BMM3;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=Endonuclease III homolog {ECO:0000256|HAMAP-Rule:MF_03183};
DE            EC=3.2.2.- {ECO:0000256|HAMAP-Rule:MF_03183};
DE            EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_03183};
DE   AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_03183};
DE            Short=DNA glycosylase/AP lyase {ECO:0000256|HAMAP-Rule:MF_03183};
GN   Name=NTG1 {ECO:0000256|HAMAP-Rule:MF_03183};
GN   OrderedLocusNames=DEHA2F04180g {ECO:0000313|EMBL:CAG88864.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88864.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88864.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Bifunctional DNA N-glycosylase with associated
CC       apurinic/apyrimidinic (AP) lyase function that catalyzes the first
CC       step in base excision repair (BER), the primary repair pathway for
CC       the repair of oxidative DNA damage. The DNA N-glycosylase activity
CC       releases the damaged DNA base from DNA by cleaving the N-
CC       glycosidic bond, leaving an AP site. The AP lyase activity cleaves
CC       the phosphodiester bond 3' to the AP site by a beta-elimination.
CC       Primarily recognizes and repairs oxidative base damage of
CC       pyrimidines. {ECO:0000256|HAMAP-Rule:MF_03183}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in
CC         DNA is broken by a beta-elimination reaction, leaving a 3'-
CC         terminal unsaturated sugar and a product with a terminal 5'-
CC         phosphate.; EC=4.2.99.18; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03183};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03183}.
CC       Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03183}.
CC   -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000256|HAMAP-
CC       Rule:MF_03183}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03183}.
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DR   EMBL; CR382138; CAG88864.2; -; Genomic_DNA.
DR   RefSeq; XP_460548.2; XM_460548.1.
DR   STRING; 4959.XP_460548.2; -.
DR   EnsemblFungi; CAG88864; CAG88864; DEHA2F04180g.
DR   GeneID; 2903199; -.
DR   KEGG; dha:DEHA2F04180g; -.
DR   HOGENOM; HOG000252209; -.
DR   InParanoid; Q6BMM3; -.
DR   KO; K10773; -.
DR   OMA; RGKRCDL; -.
DR   OrthoDB; 1322642at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProtKB-UniRule.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; -; 1.
DR   HAMAP; MF_03183; Endonuclease_III_Nth; 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR004036; Endonuclease-III-like_CS2.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HTH_base_excis_C.
DR   InterPro; IPR030841; NTH1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; SSF48150; 1.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMM3.
DR   SWISS-2DPAGE; Q6BMM3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_03183};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_03183};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_03183};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03183};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_03183};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03183};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN      160    317       ENDO3c. {ECO:0000259|SMART:SM00478}.
FT   ACT_SITE    250    250       Nucleophile; for N-glycosylase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03183}.
FT   SITE        269    269       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03183}.
SQ   SEQUENCE   375 AA;  41646 MW;  CD9C1CFA793716EA CRC64;
     MTVAKSKRLR EVNGTDVLNK RVKTEETLSF ESITIPNIKH ESDLIITPSI KPESDSVIPS
     NKLEPDSISN TKKYLTVEIE DKKPNVFAKV TSDDVDSIPS TCKAPPKWSE LYNEVVAMRS
     KFLSPVDTMG CERIPEGISP NVAKTNPRVF RFQLLISLML SSQTKDEVNF QAMRNLHSGL
     MALGHKDGLS LESIVTLSEG EIDAFISKVG FHRKKAAYIK KACAILQSNF DSDIPKNITD
     IVTLPGVGPK MGFLLLQRGW NINDGIGVDV HIHRLAQMWG WVAKSEKPES TRTELESWLP
     KKFWGDINPL LVGFGQVICV PKASNCDICT LGINKLCKSS NKKLLNASMT DARRAKLLKG
     RGNLTELITE IEDLV
//

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