ID   NFI_TRIV2               Reviewed;         221 AA.
AC   Q3MEZ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Endonuclease V {ECO:0000255|HAMAP-Rule:MF_00801};
DE            EC=3.1.21.7 {ECO:0000255|HAMAP-Rule:MF_00801};
DE   AltName: Full=Deoxyinosine 3'endonuclease {ECO:0000255|HAMAP-Rule:MF_00801};
DE   AltName: Full=Deoxyribonuclease V {ECO:0000255|HAMAP-Rule:MF_00801};
DE            Short=DNase V {ECO:0000255|HAMAP-Rule:MF_00801};
GN   Name=nfi {ECO:0000255|HAMAP-Rule:MF_00801}; OrderedLocusNames=Ava_0819;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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:0000255|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:0000255|HAMAP-Rule:MF_00801};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00801};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00801}.
CC   -!- SIMILARITY: Belongs to the endonuclease V family. {ECO:0000255|HAMAP-
CC       Rule:MF_00801}.
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DR   EMBL; CP000117; ABA20443.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MEZ3; -.
DR   SMR; Q3MEZ3; -.
DR   STRING; 240292.Ava_0819; -.
DR   EnsemblBacteria; ABA20443; ABA20443; Ava_0819.
DR   KEGG; ava:Ava_0819; -.
DR   eggNOG; COG1515; Bacteria.
DR   HOGENOM; CLU_047631_1_1_3; -.
DR   OMA; RIHFRQA; -.
DR   Proteomes; UP000002533; Chromosome.
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; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease.
FT   CHAIN           1..221
FT                   /note="Endonuclease V"
FT                   /id="PRO_1000046991"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   SITE            82
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ   SEQUENCE   221 AA;  24435 MW;  919E0B321D580D00 CRC64;
     MQIYQPHPWP LTVEEAITIQ EELRHQVITQ DQFTQPVQYV AGVDMGFEAD GTISRAAVAV
     LSFPDLQVVE TSLAYRPTSF PYIPGFLSFR EIPAVLDALE KIQTKPDIIL CDGQGIAHPR
     RLGIASHLGV LLNIPTIGVA KSLLIGRHEE LADTKGSWQP LIHRGEIIGA VLRTRVGVKP
     VYVSSGHKIS LPTAIDYVLR CTPKYRLPET TRVADKLASN R