NFI_PYRHO
ID NFI_PYRHO Reviewed; 211 AA.
AC O58394;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=PH0661;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29752.1; -; Genomic_DNA.
DR PIR; F71111; F71111.
DR RefSeq; WP_010884755.1; NC_000961.1.
DR AlphaFoldDB; O58394; -.
DR SMR; O58394; -.
DR STRING; 70601.3257069; -.
DR EnsemblBacteria; BAA29752; BAA29752; BAA29752.
DR GeneID; 1442990; -.
DR KEGG; pho:PH0661; -.
DR eggNOG; arCOG00929; Archaea.
DR OMA; VKVGKYY; -.
DR OrthoDB; 80668at2157; -.
DR Proteomes; UP000000752; 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; 2.
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..211
FT /note="Endonuclease V"
FT /id="PRO_0000159692"
FT REGION 182..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT SITE 67
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ SEQUENCE 211 AA; 23540 MW; 552B8BDCB488A81B CRC64;
MLERIANIQK KLSKSIVERK INEVRKVAAV DVSYKEEKAR AALVITTFPE GEVLKTKVIE
TTVSFPYIPT FFFLRETKPI LIATKGETFD VLIVEGHGKA HPRGYGLASH IGVVLRKPTI
GVAKRLLKNT PKDTYKKVGK VYVSVGNLIT LEDATKIIRA ILDESGYPKP LKLADKLSKG
RIYEVKNTPS PNRSRKKRGN RGKDNNNSQG N