GENTAUR Molecular Products.

 F4ATR5_GLAS4            Unreviewed;       210 AA.
 F4ATR5;
 28-JUN-2011, integrated into UniProtKB/TrEMBL.
 28-JUN-2011, sequence version 1.
 20-JUN-2018, entry version 49.
 RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942};
          EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942};
 AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942};
 Name=nth {ECO:0000256|HAMAP-Rule:MF_00942};
 OrderedLocusNames=Glaag_1354 {ECO:0000313|EMBL:AEE22314.1};
 Glaciecola sp. (strain 4H-3-7+YE-5).
 Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
 Alteromonadaceae; Glaciecola.
 NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE22314.1, ECO:0000313|Proteomes:UP000006544};
 [1] {ECO:0000313|EMBL:AEE22314.1, ECO:0000313|Proteomes:UP000006544}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE22314.1,
 ECO:0000313|Proteomes:UP000006544};
 PubMed=21705587; DOI=10.1128/JB.05468-11;
 US DOE Joint Genome Institute;
 Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C.,
 Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
 Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
 Abe F., Horikoshi K., Keller M., Antranikian G.;
 "Complete genome sequence of the marine, cellulose and xylan degrading
 bacterium Glaciecola sp. 4H-3-7+YE-5.";
 J. Bacteriol. 193:4547-4548(2011).
 [2]
 NUCLEOTIDE SEQUENCE.
 STRAIN=4H-3-7+YE-5;
 US DOE Joint Genome Institute;
 Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
 Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
 Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
 Piela B., Lochner A., Antranikian F.I., Woyke T.;
 "Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
 Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
 -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase
     activity and AP-lyase activity. The DNA N-glycosylase activity
     releases various damaged pyrimidines from DNA by cleaving the N-
     glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The
     AP-lyase activity cleaves the phosphodiester bond 3' to the AP
     site by a beta-elimination, leaving a 3'-terminal unsaturated
     sugar and a product with a terminal 5'-phosphate.
     {ECO:0000256|HAMAP-Rule:MF_00942}.
 -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
     apyrimidinic site in DNA is broken by a beta-elimination reaction,
     leaving a 3'-terminal unsaturated sugar and a product with a
     terminal 5'-phosphate. {ECO:0000256|HAMAP-Rule:MF_00942}.
 -!- COFACTOR:
     Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
       Evidence={ECO:0000256|HAMAP-Rule:MF_00942};
     Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942};
 -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000256|HAMAP-
     Rule:MF_00942}.
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 EMBL; CP002526; AEE22314.1; -; Genomic_DNA.
 RefSeq; WP_013753254.1; NC_015497.1.
 STRING; 983545.Glaag_1354; -.
 EnsemblBacteria; AEE22314; AEE22314; Glaag_1354.
 KEGG; gag:Glaag_1354; -.
 eggNOG; ENOG4105CSM; Bacteria.
 eggNOG; COG0177; LUCA.
 KO; K10773; -.
 OrthoDB; POG091H021U; -.
 BioCyc; GSP983545:G1GX6-1402-MONOMER; -.
 Proteomes; UP000006544; Chromosome.
 GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
 GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
 GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
 GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
 GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0006284; P:base-excision repair; IEA:InterPro.
 CDD; cd00056; ENDO3c; 1.
 Gene3D; 1.10.1670.10; -; 2.
 HAMAP; MF_00942; Nth; 1.
 InterPro; IPR011257; DNA_glycosylase.
 InterPro; IPR004036; Endonuclease-III-like_CS2.
 InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
 InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
 InterPro; IPR003265; HhH-GPD_domain.
 InterPro; IPR000445; HhH_motif.
 InterPro; IPR023170; HTH_base_excis_C.
 InterPro; IPR005759; Nth.
 Pfam; PF10576; EndIII_4Fe-2S; 1.
 Pfam; PF00633; HHH; 1.
 Pfam; PF00730; HhH-GPD; 1.
 SMART; SM00478; ENDO3c; 1.
 SMART; SM00525; FES; 1.
 SUPFAM; SSF48150; SSF48150; 1.
 TIGRFAMs; TIGR01083; nth; 1.
 PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
 PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
 3: Inferred from homology;
 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942};
 Complete proteome {ECO:0000313|Proteomes:UP000006544};
 DNA damage {ECO:0000256|HAMAP-Rule:MF_00942};
 DNA repair {ECO:0000256|HAMAP-Rule:MF_00942};
 DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942};
 Endonuclease {ECO:0000313|EMBL:AEE22314.1};
 Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942};
 Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942,
 ECO:0000313|EMBL:AEE22314.1}; Iron {ECO:0000256|HAMAP-Rule:MF_00942};
 Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00942};
 Lyase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:AEE22314.1};
 Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942};
 Nuclease {ECO:0000313|EMBL:AEE22314.1}.
 DOMAIN       38    185       ENDO3c. {ECO:0000259|SMART:SM00478}.
 METAL       187    187       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
                              Rule:MF_00942}.
 METAL       194    194       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
                              Rule:MF_00942}.
 METAL       197    197       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
                              Rule:MF_00942}.
 METAL       203    203       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
                              Rule:MF_00942}.
 SEQUENCE   210 AA;  23474 MW;  5175E0FEA12F29C7 CRC64;
 MNQQKRIEML TRWRAANPHP TTELNFTSPF ELLIAVLLSA QATDVSVNKA MAKMFPVANT
 PETVYALGVD GVKEFIKTIG LFNTKAVNVN KTCKMLIDKH NSVVPEDRAA LEALPGVGRK
 TANVVLNTAF GWPTIAVDTH IDRVSNRTKF AMGKTVEKVE EKLLKVVPAE FKVDVHHWLI
 LHGRYTCIAR KPRCGSCIIE DLCEFKDKTE

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