(data stored in ACNUC7421 zone)

SWISSPROT: Q13E70_RHOPS

ID   Q13E70_RHOPS            Unreviewed;       258 AA.
AC   Q13E70;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
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=RPD_0381 {ECO:0000313|EMBL:ABE37619.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37619.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37619.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37619.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE37619.1; -; Genomic_DNA.
DR   STRING; 316057.RPD_0381; -.
DR   EnsemblBacteria; ABE37619; ABE37619; RPD_0381.
DR   KEGG; rpd:RPD_0381; -.
DR   eggNOG; ENOG4105CSM; Bacteria.
DR   eggNOG; COG0177; LUCA.
DR   HOGENOM; HOG000252206; -.
DR   KO; K10773; -.
DR   OMA; KAKNPLC; -.
DR   Proteomes; UP000001818; 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; 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.
PE   3: Inferred from homology;
DR   PRODOM; Q13E70.
DR   SWISS-2DPAGE; Q13E70.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
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:ABE37619.1};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942,
KW   ECO:0000313|EMBL:ABE37619.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942,
KW   ECO:0000313|EMBL:ABE37619.1}; 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:ABE37619.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Nuclease {ECO:0000313|EMBL:ABE37619.1}.
FT   DOMAIN       85    232       ENDO3c. {ECO:0000259|SMART:SM00478}.
FT   METAL       234    234       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       241    241       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       244    244       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       250    250       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
SQ   SEQUENCE   258 AA;  28409 MW;  FBC86B41FFB482B0 CRC64;
     MQKITRRAPA PAVAKSAKIP ASSVAAKPRP QRQKSGKAAT KPKRLRRWSP DEVREAFTRF
     ARANPEPKGE LEHLNPFTLL VAVVLSAQAT DSGVNKATRA LFAVADTPQK MLALGEERVR
     DYIKTIGLFR TKAKNVIALS QKLITDFGGE VPSTRAELET LPGAGRKTAN VVLNMAFGQP
     TMAVDTHVFR VGNRTGLAPG DTPLAVELAL ERMIPPEFMQ HAHHWLILHG RYTCLARKPR
     CEVCPINDLC RWPEKTVA
//

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