NFI_HALMA
ID NFI_HALMA Reviewed; 271 AA.
AC Q5V474;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 3.
DT 03-AUG-2022, entry version 80.
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=rrnAC0676;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; AY596297; AAV45678.1; -; Genomic_DNA.
DR RefSeq; WP_007190476.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V474; -.
DR SMR; Q5V474; -.
DR STRING; 272569.rrnAC0676; -.
DR EnsemblBacteria; AAV45678; AAV45678; rrnAC0676.
DR GeneID; 40151717; -.
DR KEGG; hma:rrnAC0676; -.
DR PATRIC; fig|272569.17.peg.1427; -.
DR eggNOG; arCOG00929; Archaea.
DR HOGENOM; CLU_047631_2_0_2; -.
DR OMA; RIHFRQA; -.
DR Proteomes; UP000001169; Chromosome I.
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..271
FT /note="Endonuclease V"
FT /id="PRO_0000159685"
FT REGION 46..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT BINDING 140
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT SITE 110
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ SEQUENCE 271 AA; 29037 MW; 777230BBC5E3090E CRC64;
MTVHPVRPEF VPDPSLSQTE MEELQRDIAA AARFEDEMDV LPEAITRTGD APDVDQTTLS
TSADDRTEPP FIAGVDQAFV DDKAVSAIVV LQNGEVIERV SAVERTEIPY IPGLLSFREG
GAILAAFAEL ETDPDVVLVD GSGRIHFREA GLATHIGVTL DVPAVGVAKN LLCGTPEQSL
DERYPEGTRI PITADDSVET CPDGTVIGHA LQTRQYDSPN RHINPLIVSP GHRVSASTAA
DIVEATADGY KLPEPTRLAD SYADEAKATV E