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Database: UniProt
Entry: D3RWT3_FERPA
LinkDB: D3RWT3_FERPA
Original site: D3RWT3_FERPA 
ID   D3RWT3_FERPA            Unreviewed;       253 AA.
AC   D3RWT3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:ADC64946.1};
GN   OrderedLocusNames=Ferp_0776 {ECO:0000313|EMBL:ADC64946.1};
OS   Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Ferroglobus.
OX   NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC64946.1, ECO:0000313|Proteomes:UP000002613};
RN   [1] {ECO:0000313|Proteomes:UP000002613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA   Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT   "Complete sequence of Ferroglobus placidus DSM 10642.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADC64946.1, ECO:0000313|Proteomes:UP000002613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX   PubMed=22180810; DOI=10.4056/sigs.2225018;
RA   Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA   Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA   Lovley D., Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL   Stand. Genomic Sci. 5:50-60(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604808-2};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604808-2};
CC       Note=Probably binds two magnesium or manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR604808-2};
CC   -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC       {ECO:0000256|ARBA:ARBA00007092}.
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DR   EMBL; CP001899; ADC64946.1; -; Genomic_DNA.
DR   RefSeq; WP_012965289.1; NC_013849.1.
DR   AlphaFoldDB; D3RWT3; -.
DR   STRING; 589924.Ferp_0776; -.
DR   PaxDb; 589924-Ferp_0776; -.
DR   GeneID; 8778282; -.
DR   KEGG; fpl:Ferp_0776; -.
DR   eggNOG; arCOG02207; Archaea.
DR   HOGENOM; CLU_027539_0_1_2; -.
DR   OrthoDB; 146626at2157; -.
DR   Proteomes; UP000002613; Chromosome.
DR   GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd09086; ExoIII-like_AP-endo; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR004808; AP_endonuc_1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR037493; ExoIII-like.
DR   NCBIfam; TIGR00195; exoDNase_III; 1.
DR   NCBIfam; TIGR00633; xth; 1.
DR   PANTHER; PTHR43250; EXODEOXYRIBONUCLEASE III; 1.
DR   PANTHER; PTHR43250:SF2; EXODEOXYRIBONUCLEASE III; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR604808-2};
KW   Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002613}.
FT   DOMAIN          5..243
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF03372"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT   ACT_SITE        141
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT   ACT_SITE        243
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   SITE            143
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            213
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            243
FT                   /note="Interaction with DNA substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ   SEQUENCE   253 AA;  29716 MW;  546CE2D08262C30F CRC64;
     MLKVCTYNVN SIRKRLHIVF PLMEKVDILC MQETKVEDRK FPEADFHLKG YHVVFSGGKA
     RNGVAIASKF EPDEYFSGIN GEKDRVIAAR FGKLWVINVY APQGQSIESE YYRYKLEFFK
     KLKEFLSEFV DFKGYYLLCG DMNVAPEDID VHSPDKLRNH VCFHEDVKKA FKEIVQLGFV
     DVLRKHHPKE RIYTFYDYRV RDAVKRGLGW RVDHILATEK LAEKSKDCYV LLEYRTTEKP
     SDHVPLVAEF EKV
//
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