ID A0A3B4X8H6_SERLL Unreviewed; 181 AA. AC A0A3B4X8H6; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 13-SEP-2023, entry version 18. DE RecName: Full=exodeoxyribonuclease III {ECO:0000256|ARBA:ARBA00012115}; DE EC=3.1.11.2 {ECO:0000256|ARBA:ARBA00012115}; OS Seriola lalandi dorsalis. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Carangaria; Carangiformes; Carangidae; Seriola. OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000013979.1, ECO:0000313|Proteomes:UP000261360}; RN [1] {ECO:0000313|Ensembl:ENSSLDP00000013979.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield CC nucleoside 5'-phosphates.; EC=3.1.11.2; CC Evidence={ECO:0000256|ARBA:ARBA00000493}; 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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. 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 AlphaFoldDB; A0A3B4X8H6; -. DR Ensembl; ENSSLDT00000014501.1; ENSSLDP00000013979.1; ENSSLDG00000011153.1. DR GeneTree; ENSGT00940000177796; -. DR Proteomes; UP000261360; Unplaced. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. 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 PANTHER; PTHR22748; AP ENDONUCLEASE; 1. DR PANTHER; PTHR22748:SF4; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE 2; 1. DR Pfam; PF14529; Exo_endo_phos_2; 1. DR SUPFAM; SSF56219; DNase I-like; 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 34..159 FT /note="Endonuclease/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF14529" FT ACT_SITE 39 FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 67 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT BINDING 67 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 155 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 156 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT SITE 69 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 131 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 156 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" SQ SEQUENCE 181 AA; 21477 MW; EB546B903E99E205 CRC64; SPCVFFDDVL FHFFEYAEGR WIKIRFTVDK KQWTIMNVYA PNDEVERTQF IRTITHRGKD CDIIMGDFNL KQSTMDVNEN CKWRQDMSRT VLQNLLSVNN LCDLWRHQHP KGRDYTRVQS HLGLIKRSRI DLVLVKKMMV GMFNTVRFNL NFLSDHAFIW VGVESKGEER GGVYGILMQT Y //