ID A0A2H5YW48_9BACT Unreviewed; 243 AA. AC A0A2H5YW48; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 11-DEC-2019, entry version 9. DE RecName: Full=Endonuclease V {ECO:0000256|HAMAP-Rule:MF_00801}; DE EC=3.1.21.7 {ECO:0000256|HAMAP-Rule:MF_00801}; DE AltName: Full=Deoxyinosine 3'endonuclease {ECO:0000256|HAMAP-Rule:MF_00801}; DE AltName: Full=Deoxyribonuclease V {ECO:0000256|HAMAP-Rule:MF_00801}; DE Short=DNase V {ECO:0000256|HAMAP-Rule:MF_00801}; GN Name=nfi {ECO:0000256|HAMAP-Rule:MF_00801, GN ECO:0000313|EMBL:GBD17667.1}; GN ORFNames=HRbin27_00151 {ECO:0000313|EMBL:GBD17667.1}; OS bacterium HR27. OC Bacteria. OX NCBI_TaxID=2035422 {ECO:0000313|EMBL:GBD17667.1, ECO:0000313|Proteomes:UP000236295}; RN [1] {ECO:0000313|Proteomes:UP000236295} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Kato S., Suzuki K.; RT "Metaegenomics of thermophilic ammonia-oxidizing enrichment culture."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA repair enzyme involved in the repair of deaminated bases. CC Selectively cleaves double-stranded DNA at the second phosphodiester CC bond 3' to a deoxyinosine leaving behind the intact lesion on the CC nicked DNA. {ECO:0000256|HAMAP-Rule:MF_00801}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage at apurinic or apyrimidinic sites to CC products with a 5'-phosphate.; EC=3.1.21.7; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00801}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00801}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00801}. CC -!- SIMILARITY: Belongs to the endonuclease V family. {ECO:0000256|HAMAP- CC Rule:MF_00801}. 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:GBD17667.1}. 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; BEID01000012; GBD17667.1; -; Genomic_DNA. DR Proteomes; UP000236295; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043737; F:deoxyribonuclease V activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR CDD; cd06559; Endonuclease_V; 1. DR HAMAP; MF_00801; Endonuclease_5; 1. DR InterPro; IPR007581; Endonuclease-V. DR PANTHER; PTHR28511; PTHR28511; 1. DR Pfam; PF04493; Endonuclease_5; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00801}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00801}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00801}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00801, KW ECO:0000313|EMBL:GBD17667.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00801, ECO:0000313|EMBL:GBD17667.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00801}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00801}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00801}. FT METAL 52 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00801" FT METAL 130 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00801" FT SITE 100 FT /note="Interaction with target DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00801" SQ SEQUENCE 243 AA; 27084 MW; D0F39C8A70A81CFC CRC64; MGDRRHRWHR GTVPEGISAE ELERLADLQR ELAAKVIECP LTRPPRFVAG ADVHLRNDIA IAVAVLQETL DQPMDDQDVR PLPLREVERV TVRTQIAFPY IPGFLSFREA PALLEAIRGL SRPPDLLVLD GQGRAHPRGC GLASHVGVLL DLPTIGAAKS RLYGRYQEPP NERGAWSPLI ADGTVIGATL RTRPNTKPLI VSVGHRITLA EAILWTLRLS RYRLPEPTRW AHRYAKEAVA ALR //