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Description:
Endonuclease V (EC 3.1.21.7) (Deoxyinosine 3'endonuclease)(Deoxyribonuclease V) (DNase V).
Molecular weight: 24673
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
07-MAR-2006, entry version 15.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein NFI_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U00006 | AAC43096.1 | ALT_INIT |
| EMBL | U00096 | AAC76972.1 | ALT_INIT |
| GenomeReviews | U00096_GR | b3998.1 | |
| EchoBASE | EB1859 | -.1 | |
| EcoGene | EG11915 | nfi. | |
| GO | GO:0005515 | F:protein binding | IPI. |
| HAMAP | MF_00801 | - | 1. |
| InterPro | IPR007581 | Endonuc_V. | |
| Pfam | PF04493 | Endonuclease_5 | 1. |
Keywords:
Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium; Nuclease.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=94089392; PubMed=8265357;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
RA Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT region from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-11, AND IDENTIFICATION.
RX MEDLINE=97144513; PubMed=8990280;
RA Guo G., Ding Y., Weiss B.;
RT "nfi, the gene for endonuclease V in Escherichia coli K-12.";
RL J. Bacteriol. 179:310-316(1997).
RN [3]
RP CHARACTERIZATION.
RX MEDLINE=80187404; PubMed=6246346;
RA Demple B., Gates F.T., Linn S.;
RT "Purification and properties of Escherichia coli endodeoxyribonuclease
RT V.";
RL Methods Enzymol. 65:224-231(1980).
RN [4]
RP CHARACTERIZATION.
RX MEDLINE=94266818; PubMed=8206931;
RA Yao M., Hatahet Z., Melamede R.J., Kow Y.W.;
RT "Purification and characterization of a novel deoxyinosine-specific
RT enzyme, deoxyinosine 3' endonuclease, from Escherichia coli.";
RL J. Biol. Chem. 269:16260-16268(1994).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9388217; DOI=10.1074/jbc.272.49.30774;
RA Yao M., Kow Y.W.;
RT "Further characterization of Escherichia coli endonuclease V.
RT Mechanism of recognition for deoxyinosine, deoxyuridine, and base
RT mismatches in DNA.";
RL J. Biol. Chem. 272:30774-30779(1997).
RN [6]
RP FUNCTION.
RX PubMed=11104906; DOI=10.1016/S0921-8777(00)00062-8;
RA Weiss B.;
RT "Endonuclease V of Escherichia coli prevents mutations from
RT nitrosative deamination during nitrate/nitrite respiration.";
RL Mutat. Res. 461:301-309(2001).
Feature:
CHAIN 1 223 Endonuclease V.
/FTId=PRO_0000159660.
Comments:
-!- FUNCTION: Selectively cleaves double-stranded DNA at the second
phosphodiester bond 3' to a deoxyinosine leaving behind the intact
lesion on the nicked DNA. Has a wide substrate spectrum. In
addition to deoxyinosine-containing DNA, the enzyme cleaves DNA
containing urea residues, AP sites, base mismatches,
insertion/deletion mismatches, flaps, and pseudo-Y structures.
Participates in the excision repair of hypoxanthine and xanthine
(deaminated adenine and guanine) in DNA. It thereby reduces the
mutagenic effects of nitrous acid by attacking lesions caused by
nitrosative deamination.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage at apurinic or
apyrimidinic sites to products with a 5'-phosphate.
-!- COFACTOR: Magnesium.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
P06959:aceF; NbExp=1; IntAct=EBI-551698, EBI-542707;
P0A6F5:groL; NbExp=1; IntAct=EBI-551698, EBI-543750;
P28691:hflB; NbExp=1; IntAct=EBI-551698, EBI-548381;
P0A6X3:hfq; NbExp=1; IntAct=EBI-551698, EBI-547637;
P08936:hns; NbExp=1; IntAct=EBI-551698, EBI-544934;
P10484:hsdM; NbExp=1; IntAct=EBI-551698, EBI-552119;
P02342:hupA; NbExp=1; IntAct=EBI-551698, EBI-547648;
P02341:hupB; NbExp=1; IntAct=EBI-551698, EBI-370411;
P0A6X7:ihfA; NbExp=1; IntAct=EBI-551698, EBI-551753;
P0A6Y1:ihfB; NbExp=1; IntAct=EBI-551698, EBI-551813;
P00391:lpdA; NbExp=1; IntAct=EBI-551698, EBI-542856;
P00490:malP; NbExp=1; IntAct=EBI-551698, EBI-551914;
P50465:nei; NbExp=1; IntAct=EBI-551698, EBI-555110;
P00914:phrB; NbExp=1; IntAct=EBI-551698, EBI-555781;
P36767:rdgC; NbExp=1; IntAct=EBI-551698, EBI-561716;
P60438:rplC; NbExp=1; IntAct=EBI-551698, EBI-542200;
P60723:rplD; NbExp=1; IntAct=EBI-551698, EBI-545597;
P0A7K2:rplL; NbExp=1; IntAct=EBI-551698, EBI-543702;
P0A7K6:rplS; NbExp=1; IntAct=EBI-551698, EBI-543891;
P0A7M2:rpmB; NbExp=1; IntAct=EBI-551698, EBI-543024;
P0A7Z4:rpoA; NbExp=1; IntAct=EBI-551698, EBI-544985;
P0A7W1:rpsE; NbExp=1; IntAct=EBI-551698, EBI-543949;
P02358:rpsF; NbExp=1; IntAct=EBI-551698, EBI-543068;
P02359:rpsG; NbExp=1; IntAct=EBI-551698, EBI-543074;
P0A7S9:rpsM; NbExp=1; IntAct=EBI-551698, EBI-543165;
P02370:rpsN; NbExp=1; IntAct=EBI-551698, EBI-543971;
P02371:rpsO; NbExp=1; IntAct=EBI-551698, EBI-545119;
P0A7T7:rpsR; NbExp=1; IntAct=EBI-551698, EBI-548844;
P0A809:ruvA; NbExp=1; IntAct=EBI-551698, EBI-555119;
P0A8F8:uvrB; NbExp=1; IntAct=EBI-551698, EBI-552176;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the endonuclease V family.
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Sequence length: 223
MDLASLRAQQ IELASSVIRE DRLDKDPPDL IAGADVGFEQ GGEVTRAAMV LLKYPSLELV
EYKVARIATT MPYIPGFLSF REYPALLAAW EMLSQKPDLV FVDGHGISHP RRLGVASHFG
LLVDVPTIGV AKKRLCGKFE PLSSEPGALA PLMDKGEQLA WVWRSKARCN PLFIATGHRV
SVDSALAWVQ RCMKGYRLPE PTRWADAVAS ERPAFVRYTA NQP