ID A0A2H5YW48_9BACT Unreviewed; 243 AA. AC A0A2H5YW48; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 16-JAN-2019, entry version 7. 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}; RN [1] {ECO:0000313|EMBL:GBD17667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HRbin27 {ECO:0000313|EMBL:GBD17667.1}; RX PubMed=29459499; DOI=.1264/jsme2.ME17165; RA Kato S., Sakai S., Hirai M., Tasumi E., Nishizawa M., Suzuki K., RA Takai K.; RT "Long-Term Cultivation and Metagenomics Reveal Ecophysiology of RT Previously Uncultivated Thermophiles Involved in Biogeochemical RT Nitrogen Cycle."; RL Microbes Environ. 33:107-110(2018). CC -!- FUNCTION: DNA repair enzyme involved in the repair of deaminated CC bases. Selectively cleaves double-stranded DNA at the second CC phosphodiester bond 3' to a deoxyinosine leaving behind the intact CC lesion on the nicked DNA. {ECO:0000256|HAMAP-Rule:MF_00801}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage at apurinic or apyrimidinic CC sites to 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00801}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00801}. CC -!- SIMILARITY: Belongs to the endonuclease V family. CC {ECO:0000256|HAMAP-Rule:MF_00801}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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, KW 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 52 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00801}. FT METAL 130 130 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00801}. FT SITE 100 100 Interaction with target DNA. FT {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 //