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DescriptionRecName: Full=Endonuclease V {ECO:0000256|HAMAP-Rule:MF_00801}; EC=3.1.21.7 {ECO:0000256|HAMAP-Rule:MF_00801}; AltName: Full=Deoxyinosine 3'endonuclease {ECO:0000256|HAMAP-Rule:MF_00801}; AltName: Full=Deoxyribonuclease V {ECO:0000256|HAMAP-Rule:MF_00801}; Short=DNase V {ECO:0000256|HAMAP-Rule:MF_00801};
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MyHits synonymsA2BN25_HYPBU , A2BN25 , B0577599C61FEEDA
match map segment
ihamap:Endonuclease_5 ipfam:Endonuclease_5  
Legends: 1, Magnesium. {ECO:0000256|HAMAP- Rule:MF_00801}; 2, SITE Interaction with target DNA. {ECO:0000256|HAMAP-Rule:MF_00801}.
ID   A2BN25_HYPBU            Unreviewed;       247 AA.
AC   A2BN25;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   10-MAY-2017, entry version 52.
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   OrderedLocusNames=Hbut_1565 {ECO:0000313|EMBL:ABM81386.1};
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Pyrodictiaceae; Hyperthermus.
OX   NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM81386.1, ECO:0000313|Proteomes:UP000002593};
RN   [1] {ECO:0000313|EMBL:ABM81386.1, ECO:0000313|Proteomes:UP000002593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC   {ECO:0000313|Proteomes:UP000002593};
RX   PubMed=17350933;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A.,
RA   Awayez M., She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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: Endonucleolytic cleavage at apurinic or
CC       apyrimidinic sites to products with a 5'-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00801}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-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; CP000493; ABM81386.1; -; Genomic_DNA.
DR   RefSeq; WP_011822704.1; NC_008818.1.
DR   ProteinModelPortal; A2BN25; -.
DR   STRING; 415426.Hbut_1565; -.
DR   EnsemblBacteria; ABM81386; ABM81386; Hbut_1565.
DR   GeneID; 4782943; -.
DR   KEGG; hbu:Hbut_1565; -.
DR   eggNOG; arCOG00929; Archaea.
DR   eggNOG; COG1515; LUCA.
DR   HOGENOM; HOG000229135; -.
DR   KO; K05982; -.
DR   OMA; HIGVVLK; -.
DR   OrthoDB; POG093Z0CUB; -.
DR   BioCyc; HBUT415426:GC56-1565-MONOMER; -.
DR   Proteomes; UP000002593; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043737; F:deoxyribonuclease V activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP.
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   Complete proteome {ECO:0000313|Proteomes:UP000002593};
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:ABM81386.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00801,
KW   ECO:0000313|EMBL:ABM81386.1};
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   ECO:0000313|EMBL:ABM81386.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002593}.
FT   METAL        39     39       Magnesium. {ECO:0000256|HAMAP-
FT                                Rule:MF_00801}.
FT   METAL       105    105       Magnesium. {ECO:0000256|HAMAP-
FT                                Rule:MF_00801}.
FT   SITE         75     75       Interaction with target DNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00801}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         5    226       ihamap:Endonuclease_5 [T]
FT   MYHIT        16    217       ipfam:Endonuclease_5 [T]
SQ   SEQUENCE   247 AA;  27040 MW;  B0577599C61FEEDA CRC64;
     MTYSSVAKLI ELQKRLSRRI VSSLKPMDTA SIRRIVGLDA AYSKRYGGVA IAALTTRDGQ
     LLTYSVALGE PPLQYIPGLL AFREAPLFYT ALRLLDSNYD LVVVDGHGIS HPRRAGIASH
     IGIAIAKPSI GVAKKKLYGH EQIVSEDCKP PCIAGYVVDE DTGEKLAAIV RTGRSKKSRL
     YVSPGAYTDL DSATTIVLEL LEARKTPLPA PTYHADRISK TIARQLDSGE LSPRSLKKRH
     RTLLDYI
//