ID A0AAN0Y0N5_VIBNA Unreviewed; 443 AA. AC A0AAN0Y0N5; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378}; DE EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378}; DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378}; DE Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378}; GN Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378}; GN ORFNames=BA890_02905 {ECO:0000313|EMBL:ANQ11775.1}; OS Vibrio natriegens NBRC 15636 = ATCC 14048 = DSM 759. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=1219067 {ECO:0000313|EMBL:ANQ11775.1, ECO:0000313|Proteomes:UP000092741}; RN [1] {ECO:0000313|EMBL:ANQ11775.1, ECO:0000313|Proteomes:UP000092741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14048 {ECO:0000313|EMBL:ANQ11775.1, RC ECO:0000313|Proteomes:UP000092741}; RA Weinstock M.T., Hesek E.D., Wilson C.M., Gibson D.G.; RT "Developing Vibrio natriegens as a novel, fast-growing host for RT biotechnology."; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid- CC insoluble oligonucleotides, which are then degraded further into small CC acid-soluble oligonucleotides. {ECO:0000256|HAMAP-Rule:MF_00378}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'- CC direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00378, CC ECO:0000256|RuleBase:RU004355}; CC -!- SUBUNIT: Heterooligomer composed of large and small subunits. CC {ECO:0000256|HAMAP-Rule:MF_00378}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378, CC ECO:0000256|RuleBase:RU004355}. CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP- CC Rule:MF_00378, ECO:0000256|RuleBase:RU004355}. 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; CP016345; ANQ11775.1; -; Genomic_DNA. DR RefSeq; WP_024372697.1; NZ_JAWXXM010000001.1. DR GeneID; 70913221; -. DR Proteomes; UP000092741; Chromosome 1. DR CDD; cd04489; ExoVII_LU_OBF; 1. DR HAMAP; MF_00378; Exonuc_7_L; 1. DR InterPro; IPR003753; Exonuc_VII_L. DR InterPro; IPR020579; Exonuc_VII_lsu_C. DR InterPro; IPR025824; OB-fold_nuc-bd_dom. DR NCBIfam; TIGR00237; xseA; 1. DR PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1. DR PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1. DR Pfam; PF02601; Exonuc_VII_L; 1. DR Pfam; PF13742; tRNA_anti_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00378}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP- KW Rule:MF_00378}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378}. FT DOMAIN 10..103 FT /note="OB-fold nucleic acid binding" FT /evidence="ECO:0000259|Pfam:PF13742" FT DOMAIN 126..440 FT /note="Exonuclease VII large subunit C-terminal" FT /evidence="ECO:0000259|Pfam:PF02601" SQ SEQUENCE 443 AA; 49954 MW; 5080E75FA846D168 CRC64; MLSQTNQNIF TVSRLNAEVR LLLENEMGIV WLVGEISNFS APVSGHWYLT LKDSRAQVKC AMFRGNNRRV TFKPANGNQV LVKARLSLYE PRGDYQLIIE SMQPEGDGRL QQEFEELKMK LAAEGLFAQT NKQILPEHPK RVGVITSKTG AALYDILDVL KRRDPSLPVV IYPTMVQGED AAIQIAQAIG RANSRNECDV LIVGRGGGSL EDLWCFNNEI LARTISASQI PIISAVGHEV DVTIADFVAD VRAPTPSAAA ELVSRDNSHK DQALVTRQHK LASAMRYYLA EQKQQAAQLL HRLERQHPSY QLQRQSQQLD ELDVRLRRAM QRFIDTRQQA IERKHHRLQL NSPVRHLAQQ KSRLDRVEQK LLDAMDRKLL TVRHQLAMAA EKLEAVSPLA TLKRGYSITQ TEQGKVITQA EDVKTGDRLV TRLANGEIRS TVN //