(data stored in SCRATCH zone)

SWISSPROT: A0LEV7_SYNFM

ID   A0LEV7_SYNFM            Unreviewed;       230 AA.
AC   A0LEV7;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 66.
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=Sfum_0258 {ECO:0000313|EMBL:ABK15959.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15959.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15959.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK15959.1; -; Genomic_DNA.
DR   RefSeq; WP_011697132.1; NC_008554.1.
DR   STRING; 335543.Sfum_0258; -.
DR   EnsemblBacteria; ABK15959; ABK15959; Sfum_0258.
DR   KEGG; sfu:Sfum_0258; -.
DR   eggNOG; ENOG4105Y7X; Bacteria.
DR   eggNOG; COG1515; LUCA.
DR   HOGENOM; HOG000229135; -.
DR   KO; K05982; -.
DR   OMA; GIATHIG; -.
DR   OrthoDB; 1681607at2; -.
DR   BioCyc; SFUM335543:G1G7I-261-MONOMER; -.
DR   Proteomes; UP000001784; 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; A0LEV7.
DR   SWISS-2DPAGE; A0LEV7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
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:ABK15959.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00801,
KW   ECO:0000313|EMBL:ABK15959.1};
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:UP000001784}.
FT   METAL        43     43       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00801}.
FT   METAL       111    111       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00801}.
FT   SITE         81     81       Interaction with target DNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00801}.
SQ   SEQUENCE   230 AA;  25399 MW;  88C8CE7DAB66FFE3 CRC64;
     MSDGIRHSWD LTPREAIALQ RELAGRVVLR ALPRNFRILG ASDIGYVKAG ERLAAVMLTF
     SWPDLLPLEA VHAICPVRFP YIPGLLSFRE IPPLIEAFEQ LKKRPDVLLC DGQGIAHPRK
     FGLAAHLGLY LGLPTIGCAK KRLCGIHASP PNKKGCSVPL YLDREAVGSV YCSRDNVKPI
     FVSPGHLCDQ KSAERLVARC LGRYRIPEPL RQAHLLATKL RLEISISSNG
//

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