NFI_PROMH
ID NFI_PROMH Reviewed; 222 AA.
AC B4EYT7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=PMI2773;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR45474.1; -; Genomic_DNA.
DR RefSeq; WP_012368503.1; NC_010554.1.
DR AlphaFoldDB; B4EYT7; -.
DR SMR; B4EYT7; -.
DR STRING; 529507.PMI2773; -.
DR EnsemblBacteria; CAR45474; CAR45474; PMI2773.
DR GeneID; 6801125; -.
DR KEGG; pmr:PMI2773; -.
DR eggNOG; COG1515; Bacteria.
DR HOGENOM; CLU_047631_1_0_6; -.
DR OMA; IAHPRRM; -.
DR Proteomes; UP000008319; 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; Reference proteome.
FT CHAIN 1..222
FT /note="Endonuclease V"
FT /id="PRO_1000191577"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT SITE 72
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ SEQUENCE 222 AA; 24995 MW; 41E9C43E7C22B14F CRC64;
MINTQQLRQE QTEKAQQIIL TDQFMAPTYI AGADVGFENS GAVTRAAIVV MHYPSFEIVE
YQIARIATLL PYIPGLLSFR ECPALLKAWQ GIKQKPQLVF VDGQGIAHPR RLGVASHFGL
LADIPTIGVA KSRLCGDDKK LDDDVGSTEK LMDKDEQLGW IYRSKKRCKP LYISPGYKVS
MESALAWVKR CINGYRLPEP TRWADGIASN RRLFEQLNKN KL
