(data stored in SCRATCH zone)

SWISSPROT: D3VJD7_XENNA

ID   D3VJD7_XENNA            Unreviewed;       225 AA.
AC   D3VJD7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 49.
DE   RecName: Full=Endonuclease V {ECO:0000256|HAMAP-Rule:MF_00801};
DE            EC=3.1.21.7 {ECO:0000256|HAMAP-Rule:MF_00801};
DE   AltName: Full=Deoxyinosine 3'endonuclease {ECO:0000256|HAMAP-Rule:MF_00801};
DE   AltName: Full=Deoxyribonuclease V {ECO:0000256|HAMAP-Rule:MF_00801};
DE            Short=DNase V {ECO:0000256|HAMAP-Rule:MF_00801};
GN   Name=nfi {ECO:0000256|HAMAP-Rule:MF_00801,
GN   ECO:0000313|EMBL:CBJ88693.1};
GN   OrderedLocusNames=XNC1_0619 {ECO:0000313|EMBL:CBJ88693.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88693.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88693.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_00801};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00801};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00801}.
CC   -!- SIMILARITY: Belongs to the endonuclease V family.
CC       {ECO:0000256|HAMAP-Rule:MF_00801}.
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DR   EMBL; FN667742; CBJ88693.1; -; Genomic_DNA.
DR   RefSeq; WP_010848916.1; NC_014228.1.
DR   STRING; 406817.XNC1_0619; -.
DR   EnsemblBacteria; CBJ88693; CBJ88693; XNC1_0619.
DR   KEGG; xne:XNC1_0619; -.
DR   eggNOG; ENOG4105Y7X; Bacteria.
DR   eggNOG; COG1515; LUCA.
DR   HOGENOM; HOG000229135; -.
DR   KO; K05982; -.
DR   OMA; GIATHIG; -.
DR   Proteomes; UP000008075; 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; D3VJD7.
DR   SWISS-2DPAGE; D3VJD7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00801};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00801};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00801};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00801,
KW   ECO:0000313|EMBL:CBJ88693.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00801,
KW   ECO:0000313|EMBL:CBJ88693.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00801};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00801};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   METAL        37     37       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00801}.
FT   METAL       105    105       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00801}.
FT   SITE         75     75       Interaction with target DNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00801}.
SQ   SEQUENCE   225 AA;  25175 MW;  28F7D92A88A9641C CRC64;
     MIDTKALRQE QIEKSRRVIR HDVFATSFTP TFIAGADVGF ENDGTVTRAA IAVLQYPSLE
     LVEYQIARIA TVLPYIPGLL SFREYPALLA AWQKIKQRPD LLMVDGQGIA HPRRFGIASH
     FGLLVDVPTI GVAKSRLCGE HAPVGDTPGS RQPLMDHGEQ IGVVLRSKKR CNPLYISIGH
     QISIHSAIFW VEQCMKGYRL PEPTRWADGI ASNRPFFKQT MQKNL
//

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