ID A0A2G9EFE2_9FUSO Unreviewed; 253 AA. AC A0A2G9EFE2; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 24-JAN-2024, entry version 25. DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:PIM79657.1}; GN Name=xth {ECO:0000313|EMBL:PIM79657.1}; GN ORFNames=CTM71_04235 {ECO:0000313|EMBL:PIM79657.1}, CTM72_06545 GN {ECO:0000313|EMBL:ATV59423.1}, CTM78_09920 GN {ECO:0000313|EMBL:ATV64677.1}; OS Fusobacterium pseudoperiodonticum. OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=2663009 {ECO:0000313|EMBL:PIM79657.1, ECO:0000313|Proteomes:UP000229011}; RN [1] {ECO:0000313|EMBL:PIM79657.1, ECO:0000313|Proteomes:UP000229011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCOM 1259 {ECO:0000313|EMBL:PIM79657.1, RC ECO:0000313|Proteomes:UP000229011}; RA Kook J.-K., Park S.-N., Lim Y.K.; RT "Genome sequencing of Fusobacterium periodonticum KCOM 1259."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ATV59423.1, ECO:0000313|Proteomes:UP000230056} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCOM 1261 {ECO:0000313|EMBL:ATV59423.1, RC ECO:0000313|Proteomes:UP000230056}; RA Kook J.-K., Park S.-N., Lim Y.K.; RT "Genome sequencing of Fusobacterium periodonticum KCOM 1261."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ATV64677.1, ECO:0000313|Proteomes:UP000229295} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCOM 1277 {ECO:0000313|EMBL:ATV64677.1, RC ECO:0000313|Proteomes:UP000229295}; RA Kook J.-K., Park S.-N., Lim Y.K.; RT "Genome sequencing of Fusobacterium periodonticum KCOM 1277."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP024699; ATV59423.1; -; Genomic_DNA. DR EMBL; CP024701; ATV64677.1; -; Genomic_DNA. DR EMBL; PEQY01000001; PIM79657.1; -; Genomic_DNA. DR RefSeq; WP_008794735.1; NZ_PEQY01000001.1. DR GeneID; 56857744; -. DR Proteomes; UP000229011; Unassembled WGS sequence. DR Proteomes; UP000229295; Chromosome. DR Proteomes; UP000230056; Chromosome. 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; cd09087; Ape1-like_AP-endo; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR020847; AP_endonuclease_F1_BS. 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; PS00726; AP_NUCLEASE_F1_1; 1. DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 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..242 FT /note="Endonuclease/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" FT ACT_SITE 105 FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 144 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 242 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 144 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 146 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 241 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 SITE 146 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 216 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 242 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" SQ SEQUENCE 253 AA; 29803 MW; 8A42196A8307BF53 CRC64; MKLISWNVNG IRAAIKKGFL DYFNEQNADI FCLQETKLSA GQLDLELKGY HQYWNYAEKK GYSGTAIFTK EEPLSVSYGL GIEEHDKEGR VITLEFEKFY MITVYTPNSK DELLRLDYRM VWEDEFRKYL KNLEKKKPVV VCGDLNVAHK EIDLKNPKTN RRNAGFTDEE RGKFTELLES GFIDTFRYFY PDLEHAYSWW SYRANARKNN TGWRIDYFVV SKALEKYLVD AEIHAQTEGS DHCPVVLFLD FKK //