(data stored in ACNUC7421 zone)

SWISSPROT: NFI_SULIK

ID   NFI_SULIK               Reviewed;         198 AA.
AC   C4KKT0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 44.
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};
GN   OrderedLocusNames=M164_0261;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: DNA repair enzyme involved in the repair of deaminated
CC       bases. Selectively cleaves double-stranded DNA at the second
CC       phosphodiester bond 3' to a deoxyinosine leaving behind the intact
CC       lesion on the nicked DNA. {ECO:0000255|HAMAP-Rule:MF_00801}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage at apurinic or apyrimidinic
CC         sites to 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00801}.
DR   EMBL; CP001402; ACR40895.1; -; Genomic_DNA.
DR   SMR; C4KKT0; -.
DR   PRIDE; C4KKT0; -.
DR   EnsemblBacteria; ACR40895; ACR40895; M164_0261.
DR   KEGG; sid:M164_0261; -.
DR   HOGENOM; HOG000229135; -.
DR   KO; K05982; -.
DR   OMA; VKVGKYY; -.
DR   Proteomes; UP000001479; 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;
DR   PRODOM; C4KKT0.
DR   SWISS-2DPAGE; C4KKT0.
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease.
FT   CHAIN         1    198       Endonuclease V.
FT                                /FTId=PRO_1000212978.
FT   METAL        38     38       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00801}.
FT   METAL       101    101       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00801}.
FT   SITE         73     73       Interaction with target DNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00801}.
SQ   SEQUENCE   198 AA;  22051 MW;  DE752959A649398B CRC64;
     MVEKHLLEFL EKLQFLISKN VKISHYGIEN VKKICGVDIA YKGNLGFSVG VSMDINSGDY
     NYKSYVGEVN FPYIPGFLFM REAPLMIKAI EGLDCHLLLV DGHGIAHPRK SGIAAVIGVL
     LDFPTIGVAK SRLTGDLVNE SEITYVYLNG EKVGVKFGRY FYSPGNKVDL QDCIELGKRG
     YPKVLKIADM LTKKIKKE
//

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