(data stored in ACNUC7421 zone)

SWISSPROT: E3J7E8_FRAIE

ID   E3J7E8_FRAIE            Unreviewed;       271 AA.
AC   E3J7E8;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   16-JAN-2019, entry version 53.
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=FraEuI1c_0335 {ECO:0000313|EMBL:ADP78421.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78421.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78421.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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; CP002299; ADP78421.1; -; Genomic_DNA.
DR   RefSeq; WP_013421544.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0335; -.
DR   EnsemblBacteria; ADP78421; ADP78421; FraEuI1c_0335.
DR   KEGG; fri:FraEuI1c_0335; -.
DR   eggNOG; ENOG4105CSM; Bacteria.
DR   eggNOG; COG0177; LUCA.
DR   HOGENOM; HOG000252208; -.
DR   KO; K10773; -.
DR   OMA; KAKNPLC; -.
DR   OrthoDB; 1381897at2; -.
DR   BioCyc; FSP298654:G1GOT-336-MONOMER; -.
DR   Proteomes; UP000002484; 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; 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; E3J7E8.
DR   SWISS-2DPAGE; E3J7E8.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
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:ADP78421.1};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942};
KW   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:ADP78421.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Nuclease {ECO:0000313|EMBL:ADP78421.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   DOMAIN       81    228       ENDO3c. {ECO:0000259|SMART:SM00478}.
FT   METAL       230    230       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       237    237       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       240    240       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       246    246       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
SQ   SEQUENCE   271 AA;  29231 MW;  E1C1F46FD8F85B0A CRC64;
     MPATVDPSPE TPGPPTRQAQ TRQAQTRQAQ TRQAQAQPSE TPLARTRRAR RIVRILGEVH
     PDARIALNFT TPLELIVATV LSAQCTDKKV NEVTPTVFAR YPSAAAYAGA DRAELETILR
     PTGFFRAKAN SVIGLGAALV DRFGGEVPRT LEELVTLPGV GRKTANVVLG HAFDTPGITV
     DTHVGRLSRR FGLTTQDDPV KVEADLAALI ERKDWTIASD RMIFHGRRIC HARRPACGAC
     AVAKLCPSYG TGPTSEIEAA KLVRGDVEAA R
//

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