ID D0LQ83_HALO1 Unreviewed; 301 AA. AC D0LQ83; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAR-2024, entry version 68. DE SubName: Full=Exodeoxyribonuclease III Xth {ECO:0000313|EMBL:ACY18892.1}; DE EC=4.2.99.18 {ECO:0000313|EMBL:ACY18892.1}; GN OrderedLocusNames=Hoch_6423 {ECO:0000313|EMBL:ACY18892.1}; OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2). OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium. OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY18892.1, ECO:0000313|Proteomes:UP000001880}; RN [1] {ECO:0000313|EMBL:ACY18892.1, ECO:0000313|Proteomes:UP000001880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2 RC {ECO:0000313|Proteomes:UP000001880}; RX PubMed=21304682; DOI=10.4056/sigs.69.1277; RG US DOE Joint Genome Institute (JGI-PGF); RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A., RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F., RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A., RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J., RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2)."; RL Stand. Genomic Sci. 2:96-106(2010). 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; CP001804; ACY18892.1; -; Genomic_DNA. DR AlphaFoldDB; D0LQ83; -. DR STRING; 502025.Hoch_6423; -. DR KEGG; hoh:Hoch_6423; -. DR eggNOG; COG0708; Bacteria. DR HOGENOM; CLU_027539_1_3_7; -. DR OrthoDB; 9803914at2; -. DR Proteomes; UP000001880; 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:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. 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 Lyase {ECO:0000313|EMBL:ACY18892.1}; 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:UP000001880}. FT DOMAIN 8..281 FT /note="Endonuclease/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" FT REGION 21..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 26..40 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 141 FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 184 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 281 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT BINDING 11 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 184 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 186 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 280 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 281 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT SITE 186 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 255 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 281 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" SQ SEQUENCE 301 AA; 33324 MW; DC86B4A751392112 CRC64; MLARVRVVSW NVNGLRAVDR TTPRRASAAA SPSPGQVRAS TGARAQRGGG RFRRWIERVD ATIVGVQEVR ARRDALPRRL LQPRGWHAHL VEAERAGYSG VGLYAKLAPD GADTALAGGD FDREGRLQIA HFGRLSVANV YFPNGNGSNR DNSRVPFKLD FYRALFDALG ALRDAGQRVL VMGDFNTAHR DIDLARPKQN RKTSGFLPEE RAELDRWVAA GWVDTFRHFE PGPGHYTWWS QRAGVRARNI GWRIDYVFAC PEAMPFVRSA FLMPQVGGSD HCPHGVVLDP AITRAAPPLP S //