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E8Y689 (E8Y689_ECOKO) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endonuclease V HAMAP-Rule MF_00801
EC=3.1.21.7 HAMAP-Rule MF_00801
Alternative name(s):
Deoxyinosine 3'endonuclease HAMAP-Rule MF_00801
Deoxyribonuclease V HAMAP-Rule MF_00801
Gene names
Name:nfi HAMAP-Rule MF_00801 EMBL AFH15464.1
Ordered Locus Names:EKO11_4323 EMBL ADX52881.1
ORF Names:KO11_02380 EMBL AFH15464.1
OrganismEscherichia coli (strain ATCC 55124 / KO11) [Complete proteome] [HAMAP] EMBL ADX52881.1
Taxonomic identifier595495 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (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 By similarity. HAMAP-Rule MF_00801

Catalytic activity

Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate. HAMAP-Rule MF_00801

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00801

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00801.

Sequence similarities

Belongs to the endonuclease V family. HAMAP-Rule MF_00801

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding351Magnesium By similarity HAMAP-Rule MF_00801
Metal binding1031Magnesium By similarity HAMAP-Rule MF_00801
Site731Interaction with target DNA By similarity HAMAP-Rule MF_00801

Sequences

Sequence LengthMass (Da)Tools
E8Y689 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 4933CABD4BB9E255

FASTA22324,691
        10         20         30         40         50         60 
MDLASLRAQQ IELASSVIRE DRLDKDPPDL IAGADVGFEQ GGEVTRAAMV LLKYPSLELV 

        70         80         90        100        110        120 
EYKVARIATT MPYIPGFLSF REYPALLAAW EMLSQKPDLV FVDGHGISHP RRLGVASHFG 

       130        140        150        160        170        180 
LMVDVPTIGV AKKRLCGKFE PLSSEPGALA PLMDKGEQLA WVWRSKARCN PLFIATGHRV 

       190        200        210        220 
SVDSALAWVQ RCMKGYRLPE PTRWADAVAS ERPAFVRYTA NQP

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of chromosome of Escherichia coli KO11."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Keating D., Landick R., Woyke T.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55124 / KO11 and KO11 EMBL ADX52881.1.
[2]"Optical mapping and sequencing of the Escherichia coli KO11 genome reveal extensive chromosomal rearrangements, and multiple tandem copies of the Zymomonas mobilis pdc and adhB genes."
Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L., Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O.
J. Ind. Microbiol. Biotechnol. 39:629-639(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: KO11FL EMBL AFH15464.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002516 Genomic DNA. Translation: ADX52881.1.
CP002970 Genomic DNA. Translation: AFH15464.1.
RefSeqYP_005279945.1. NC_016902.1.
YP_006162816.1. NC_017660.1.

3D structure databases

SMRE8Y689. Positions 1-212.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADX52881; ADX52881; EKO11_4323.
AFH15464; AFH15464; KO11_02380.
GeneID11779787.
12759988.
KEGGekf:KO11_02380.
eko:EKO11_4323.
PATRIC48648835. VBIEscCol13896_4395.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK05982.

Enzyme and pathway databases

BioCycECOL595495:GI1Q-4410-MONOMER.

Family and domain databases

HAMAPMF_00801. Endonuclease_5.
InterProIPR007581. Endonuclease-V.
[Graphical view]
PfamPF04493. Endonuclease_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE8Y689_ECOKO
AccessionPrimary (citable) accession number: E8Y689
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: May 29, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info