NFI_STRCO
ID NFI_STRCO Reviewed; 233 AA.
AC Q9X7N2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=SCO6726;
GN ORFNames=SC5F2A.09;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939129; CAB40676.1; -; Genomic_DNA.
DR PIR; T35251; T35251.
DR RefSeq; NP_630799.1; NC_003888.3.
DR RefSeq; WP_011031135.1; NZ_VNID01000002.1.
DR AlphaFoldDB; Q9X7N2; -.
DR SMR; Q9X7N2; -.
DR STRING; 100226.SCO6726; -.
DR GeneID; 1102165; -.
DR KEGG; sco:SCO6726; -.
DR PATRIC; fig|100226.15.peg.6833; -.
DR eggNOG; COG1515; Bacteria.
DR HOGENOM; CLU_047631_1_1_11; -.
DR InParanoid; Q9X7N2; -.
DR OMA; RIHFRQA; -.
DR PhylomeDB; Q9X7N2; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043737; F:deoxyribonuclease V activity; IBA:GO_Central.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..233
FT /note="Endonuclease V"
FT /id="PRO_0000159673"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT SITE 86
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ SEQUENCE 233 AA; 24313 MW; F3E8E6F7B5BDCED6 CRC64;
MTTVSVQIPA GWPATEERAR AVQDELRARV VLDEPGPPPG TGRVTGVDVA YDDERDVVAA
AAVVLDAGTL AVVAEATAVG RISFPYVPGL LAFREIPTVL AALEALPCPP GLVVCDGYGL
AHPRRFGLAS HLGVLTGLPT IGVAKNPFTF THDDPDTPRG STSPLLAGAE EVGRAVRTRD
GVKPVFVSVG HRVGLGNACA HTLALTPAYR LPETTRRADA LCRAALRDAA YRA
