(data stored in SCRATCH zone)

SWISSPROT: D5E9N6_METMS

ID   D5E9N6_METMS            Unreviewed;       212 AA.
AC   D5E9N6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 58.
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=Mmah_0355 {ECO:0000313|EMBL:ADE35887.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35887.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35887.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity
CC       and AP-lyase activity. The DNA N-glycosylase activity releases various
CC       damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving
CC       an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the
CC       phosphodiester bond 3' to the AP site by a beta-elimination, leaving a
CC       3'-terminal unsaturated sugar and a product with a terminal 5'-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00942}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA
CC         is broken by a beta-elimination reaction, leaving a 3'-terminal
CC         unsaturated sugar and a product with a terminal 5'-phosphate.;
CC         EC=4.2.99.18; Evidence={ECO:0000256|HAMAP-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; CP001994; ADE35887.1; -; Genomic_DNA.
DR   RefSeq; WP_013036830.1; NC_014002.1.
DR   EnsemblBacteria; ADE35887; ADE35887; Mmah_0355.
DR   GeneID; 8982489; -.
DR   KEGG; mmh:Mmah_0355; -.
DR   eggNOG; arCOG00459; Archaea.
DR   eggNOG; COG0177; LUCA.
DR   HOGENOM; HOG000252208; -.
DR   KO; K10773; -.
DR   OMA; WQQFTHL; -.
DR   OrthoDB; 124734at2157; -.
DR   BioCyc; MMAH547558:G1GHT-351-MONOMER; -.
DR   Proteomes; UP000001059; 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; D5E9N6.
DR   SWISS-2DPAGE; D5E9N6.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942};
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:ADE35887.1};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:ADE35887.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:ADE35887.1};
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:ADE35887.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Nuclease {ECO:0000313|EMBL:ADE35887.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          41..189
FT                   /note="ENDO3c"
FT                   /evidence="ECO:0000259|SMART:SM00478"
FT   METAL           191
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT   METAL           198
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT   METAL           201
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT   METAL           207
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
SQ   SEQUENCE   212 AA;  23916 MW;  EDF0385452C03686 CRC64;
     MTANNLSNFP QIWGLLKKEY PDPQPALHFK TPLQLLVATI LSAQSTDVQI NKVTRELFRK
     YRSVFDYADA DISELEKDIY STGFYRNKAK HLQQSARVII EDFDGEVPST MEDLLKLPGV
     ARKTANIVLA RGFGVKAGIA VDTHVKRLAT RLGFTVNKDP VKIERDLMEL VDRNEWDDFS
     LTLILHGRNI CFARKPACGK CVVNHLCPSS LV
//

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