(data stored in ACNUC7421 zone)

SWISSPROT: Q47TQ8_THEFY

ID   Q47TQ8_THEFY            Unreviewed;       258 AA.
AC   Q47TQ8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 99.
DE   RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942};
DE            EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942};
GN   Name=nth {ECO:0000256|HAMAP-Rule:MF_00942};
GN   OrderedLocusNames=Tfu_0118 {ECO:0000313|EMBL:AAZ54156.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54156.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase
CC       activity and AP-lyase activity. The DNA N-glycosylase activity
CC       releases various damaged pyrimidines from DNA by cleaving the N-
CC       glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The
CC       AP-lyase activity cleaves the phosphodiester bond 3' to the AP
CC       site by a beta-elimination, leaving a 3'-terminal unsaturated
CC       sugar and a product with a terminal 5'-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00942}.
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_00942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00942};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942};
CC   -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000256|HAMAP-
CC       Rule:MF_00942}.
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DR   EMBL; CP000088; AAZ54156.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0118; -.
DR   EnsemblBacteria; AAZ54156; AAZ54156; Tfu_0118.
DR   KEGG; tfu:Tfu_0118; -.
DR   eggNOG; ENOG4105CSM; Bacteria.
DR   eggNOG; COG0177; LUCA.
DR   HOGENOM; HOG000252208; -.
DR   KO; K10773; -.
DR   OMA; KAKNPLC; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; -; 1.
DR   HAMAP; MF_00942; Nth; 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR004036; Endonuclease-III-like_CS2.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR023170; HTH_base_excis_C.
DR   InterPro; IPR005759; Nth.
DR   Pfam; PF10576; EndIII_4Fe-2S; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; SSF48150; 1.
DR   TIGRFAMs; TIGR01083; nth; 1.
DR   PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TQ8.
DR   SWISS-2DPAGE; Q47TQ8.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00942};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00942};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Endonuclease {ECO:0000313|EMBL:AAZ54156.1};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942,
KW   ECO:0000313|EMBL:AAZ54156.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942,
KW   ECO:0000313|EMBL:AAZ54156.1}; Iron {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:AAZ54156.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Nuclease {ECO:0000313|EMBL:AAZ54156.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN       70    217       ENDO3c. {ECO:0000259|SMART:SM00478}.
FT   METAL       219    219       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       226    226       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       229    229       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       235    235       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
SQ   SEQUENCE   258 AA;  28719 MW;  86BDEDB5C4145408 CRC64;
     MSRNVYTASS SPGASGDASA AERDTPTGET RLALMRRSRQ INRELARMYP DAHCELDFTT
     PLELLVATIL SAQCTDRRVN KVTPVLFARY RSAADYASAN QEELENIIRS TGFYRTKARN
     IIALGQRLCD EHGGEVPDRL EDLVKLPGVG RKTANVVLGN AFGVPGLTVD THFGRLVRRF
     GMTRQTDPVK VEQEIAALFP PEEWTMLSHR LIWHGRRVCH ARRPACGACE LQHLCPSYGE
     GPVDEETARR LVRTGPFS
//

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