(data stored in ACNUC7421 zone)

SWISSPROT: A8LF47_FRASN

ID   A8LF47_FRASN            Unreviewed;       241 AA.
AC   A8LF47;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   16-JAN-2019, entry version 72.
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=Franean1_0326 {ECO:0000313|EMBL:ABW09792.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09792.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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; CP000820; ABW09792.1; -; Genomic_DNA.
DR   RefSeq; WP_012157769.1; NC_009921.1.
DR   STRING; 298653.Franean1_0326; -.
DR   EnsemblBacteria; ABW09792; ABW09792; Franean1_0326.
DR   KEGG; fre:Franean1_0326; -.
DR   eggNOG; ENOG4105CSM; Bacteria.
DR   eggNOG; COG0177; LUCA.
DR   HOGENOM; HOG000252208; -.
DR   KO; K10773; -.
DR   OMA; KAKNPLC; -.
DR   OrthoDB; 1381897at2; -.
DR   BioCyc; FSP298653:G1G9X-325-MONOMER; -.
DR   Proteomes; UP000001313; 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; 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; A8LF47.
DR   SWISS-2DPAGE; A8LF47.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
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:ABW09792.1};
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:ABW09792.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Nuclease {ECO:0000313|EMBL:ABW09792.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313}.
FT   DOMAIN       51    198       ENDO3c. {ECO:0000259|SMART:SM00478}.
FT   METAL       200    200       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       207    207       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       210    210       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       216    216       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
SQ   SEQUENCE   241 AA;  25908 MW;  53C0C8C91DC9CDA8 CRC64;
     MATTVDARAE TALARTRRAR RIVRALGELH PDARIALHFS SPLELLVATV LSAQCTDKKV
     NEVTPGVFAR YPTAAAYAAA DRDELEAILR PTGFFRAKAN SLMGIGAALV ERFDGEVPGR
     LEALVTLPGV GRKTANVVLG HCFGIPGITV DTHVGRLSRR FGLTTETDPV RAESDLAALI
     ERRDWTIASD RMIFHGRRVC HARRPACGAC AIARMCPSFG TGPTEPAEAA RLVRGDAEAA
     R
//

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