NFI_STRAW
ID NFI_STRAW Reviewed; 229 AA.
AC Q82MH6;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=SAV_1684;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND
RP COFACTOR.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the endonuclease V (SAV1684) from Streptomyces
RT avermitilis. Northeast structural genomics consortium target SVR196.";
RL Submitted (MAR-2009) to the PDB data bank.
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, ECO:0000269|Ref.3};
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}.
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; BA000030; BAC69395.1; -; Genomic_DNA.
DR RefSeq; WP_010983123.1; NZ_JZJK01000086.1.
DR PDB; 3GOC; X-ray; 1.60 A; A/B=1-229.
DR PDBsum; 3GOC; -.
DR AlphaFoldDB; Q82MH6; -.
DR SMR; Q82MH6; -.
DR STRING; 227882.SAV_1684; -.
DR EnsemblBacteria; BAC69395; BAC69395; SAVERM_1684.
DR KEGG; sma:SAVERM_1684; -.
DR eggNOG; COG1515; Bacteria.
DR HOGENOM; CLU_047631_1_1_11; -.
DR OMA; RIHFRQA; -.
DR OrthoDB; 1681607at2; -.
DR EvolutionaryTrace; Q82MH6; -.
DR Proteomes; UP000000428; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..229
FT /note="Endonuclease V"
FT /id="PRO_0000159672"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT SITE 84
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:3GOC"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 39..49
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 51..64
FT /evidence="ECO:0007829|PDB:3GOC"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:3GOC"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:3GOC"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:3GOC"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:3GOC"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:3GOC"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:3GOC"
FT HELIX 211..228
FT /evidence="ECO:0007829|PDB:3GOC"
SQ SEQUENCE 229 AA; 23988 MW; 0172D8C2A1DBA1A0 CRC64;
MTTVRIPAGW PATEEEARAV QDELRGRVIL DEPGPPPGTG RVTGVDVAYD DERDVVVAAA
VVLDAATLDV VAEATAVGEV SFPYVPGLLA FREIPTVLAA LDALPCPPGL IVCDGYGVAH
PRRFGLASHL GVLTGLPTIG VAKNPFTFSY EDPGAPRGSA APLLAGADEV GRALRTQSGV
KPVFVSVGHR VDLDHACAHT LALTPKYRIP ETTRRADSLC RRALKEATA
