ID A0A1G2CRG7_9BACT Unreviewed; 256 AA.
AC A0A1G2CRG7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:OGZ03984.1};
GN ORFNames=A2648_00050 {ECO:0000313|EMBL:OGZ03984.1};
OS Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_01_FULL_41_20.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798657 {ECO:0000313|EMBL:OGZ03984.1, ECO:0000313|Proteomes:UP000178841};
RN [1] {ECO:0000313|EMBL:OGZ03984.1, ECO:0000313|Proteomes:UP000178841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGZ03984.1}.
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DR EMBL; MHLH01000012; OGZ03984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2CRG7; -.
DR STRING; 1798657.A2648_00050; -.
DR Proteomes; UP000178841; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease 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; cd09085; Mth212-like_AP-endo; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR NCBIfam; TIGR00195; exoDNase_III; 1.
DR NCBIfam; TIGR00633; xth; 1.
DR PANTHER; PTHR22748; AP ENDONUCLEASE; 1.
DR PANTHER; PTHR22748:SF6; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 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}.
FT DOMAIN 4..247
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 151
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 221
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 247
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 256 AA; 29778 MW; FD0017D854E17C0B CRC64;
MRLISWNVNG IRAVHKKGAL DIFLKQKADI FCFQEIKADE TQIPEETRNI SGYFSYFASS
KVKKGYSGVA VYTKEEPEKV IYGLGVKKFD DEGRLLELHF KDFIFFNVYF PNGGGGSERL
AYKLEFYDAF LTHIEKIRKK GKSIIFCGDV NTAHEEIDLA RPKENEENTG FLPEERAWID
ELVYHGYVDT FRHFHPHKKD SYTYWDMKTM ARERNVGWRI DYFFVSGDMI KKIKGAGIIS
DIYGSDHCPI FLDVNL
//
