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P04390 (T2E5_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type-2 restriction enzyme EcoRV

Short name=R.EcoRV
EC=3.1.21.4
Alternative name(s):
Endonuclease EcoRV
Type II restriction enzyme EcoRV
Gene names
Name:ecoRVR
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recognizes the double-stranded sequence GATATC and cleaves after T-3.

Catalytic activity

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

Cofactor

Binds 2 magnesium ions per subunit.

Subunit structure

Homodimer.

Ontologies

Keywords
   Biological processRestriction system
   LigandMagnesium
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

Type II site-specific deoxyribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 245244Type-2 restriction enzyme EcoRV
PRO_0000077305

Sites

Active site741
Active site901
Active site921
Metal binding451Magnesium 2
Metal binding741Magnesium 1
Metal binding741Magnesium 2
Metal binding901Magnesium 1

Experimental info

Mutagenesis701N → Q: Decrease in activity.
Mutagenesis731P → A or G: Loss of activity.
Mutagenesis741D → A: Loss of activity.
Mutagenesis741D → E: Decrease in activity.
Mutagenesis901D → A, N, E or T: Loss of activity.
Mutagenesis1831S → A or T: Decrease in activity.
Mutagenesis1831S → I: Loss of activity.
Mutagenesis1851N → D, A or Q: Loss of activity.
Mutagenesis1861T → S or N: Loss of activity.
Mutagenesis1871T → S or N: No loss of activity.
Mutagenesis1881N → A, Q or T: Decrease in activity.
Mutagenesis1881N → D: Loss of activity.
Mutagenesis1901G → A: No loss of activity.

Secondary structure

............................................ 245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04390 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7DB7EC640A746281

FASTA24528,650
        10         20         30         40         50         60 
MSLRSDLINA LYDENQKYDV CGIISAEGKI YPLGSDTKVL STIFELFSRP IINKIAEKHG 

        70         80         90        100        110        120 
YIVEEPKQQN HYPDFTLYKP SEPNKKIAID IKTTYTNKEN EKIKFTLGGY TSFIRNNTKN 

       130        140        150        160        170        180 
IVYPFDQYIA HWIIGYVYTR VATRKSSLKT YNINELNEIP KPYKGVKVFL QDKWVIAGDL 

       190        200        210        220        230        240 
AGSGNTTNIG SIHAHYKDFV EGKGIFDSED EFLDYWRNYE RTSQLRNDKY NNISEYRNWI 


YRGRK 

« Hide

References

[1]"Characterization of the genes coding for the Eco RV restriction and modification system of Escherichia coli."
Bougueleret L., Schwarzstein M., Tsugita A., Zabeau M.
Nucleic Acids Res. 12:3659-3676(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The EcoRV restriction-modification system: genes, enzymes, synthetic substrates."
Kraev A.S., Kravets A.N., Chernov B.K., Skryabin K.G., Baev A.A.
Mol. Biol. (Mosk.) 19:236-242(1985)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis."
Thielking V., Selent U., Koehler E., Wolfes H., Pieper U., Geiger R., Urbanke C., Winkler F.K., Pingoud A.
Biochemistry 30:6416-6422(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[4]"The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments."
Winkler F.K., Banner D.W., Oefner C., Tsernoglou D., Brown R., Heathman S.P., Bryan R.K., Martin P.D., Petratos K., Wilson K.S.
EMBO J. 12:1781-1795(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[5]"Mg2+ binding to the active site of EcoRV endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 A resolution."
Kostrewa D., Winkler F.K.
Biochemistry 34:683-696(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[6]"Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis."
Perona J.J., Martin A.M.
J. Mol. Biol. 273:207-225(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]"Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contacts."
Horton N.C., Perona J.J.
J. Biol. Chem. 273:21721-21729(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]"Role of protein-induced bending in the specificity of DNA recognition: crystal structure of EcoRV endonuclease complexed with d(AAAGAT) + d(ATCTT)."
Horton N.C., Perona J.J.
J. Mol. Biol. 277:779-787(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]"Structural analysis of a mutational hot-spot in the EcoRV restriction endonuclease: a catalytic role for a main chain carbonyl group."
Thomas M.P., Brady R.L., Halford S.E., Sessions R.B., Baldwin G.S.
Nucleic Acids Res. 27:3438-3445(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF GLN-69 MUTANTS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00530 Genomic DNA. Translation: CAA25208.1.
M19941 Genomic DNA. Translation: AAA24615.1.
PIRNDECR5. A00784.
RefSeqNP_863580.1. NC_005019.1.
YP_007316617.1. NC_019982.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZ0X-ray2.00A/B2-245[»]
1AZ3X-ray2.40A/B2-245[»]
1AZ4X-ray2.40A/B2-245[»]
1B94X-ray1.90A/B2-245[»]
1B95X-ray2.05A/B2-245[»]
1B96X-ray2.30A/B2-245[»]
1B97X-ray1.90A/B2-245[»]
1BGBX-ray2.00A/B2-245[»]
1BSSX-ray2.15A/B2-245[»]
1BSUX-ray2.00A/B2-245[»]
1BUAX-ray2.15A/B2-245[»]
1EO3X-ray2.00A/B1-245[»]
1EO4X-ray1.90A/B1-245[»]
1EONX-ray1.60A/B1-245[»]
1EOOX-ray2.16A/B1-245[»]
1EOPX-ray2.60A/B1-245[»]
1RV5X-ray2.10A/B2-245[»]
1RVAX-ray2.00A/B2-245[»]
1RVBX-ray2.10A/B2-245[»]
1RVCX-ray2.10A/B2-245[»]
1RVEX-ray2.50A/B1-245[»]
1STXX-ray2.10A/B2-245[»]
1SUZX-ray1.80A/B2-245[»]
1SX5X-ray1.50A/B2-245[»]
1SX8X-ray2.15A/B2-245[»]
2B0DX-ray2.00A/B1-245[»]
2B0EX-ray1.90A/B1-245[»]
2GE5X-ray2.40A/B2-220[»]
2RVEX-ray3.00A/B2-245[»]
4RVEX-ray3.00A/B/C2-245[»]
ProteinModelPortalP04390.
SMRP04390. Positions 2-245.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE995. EcoRV.

Proteomic databases

PRIDEP04390.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID14401263.
1446621.

Family and domain databases

Gene3D3.40.600.10. 1 hit.
InterProIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
IPR015314. Restrct_endonuc_II_EcoRV.
IPR019755. Restrct_endonuc_II_EcoRV_Pbac.
[Graphical view]
PfamPF09233. Endonuc-EcoRV. 1 hit.
[Graphical view]
PIRSFPIRSF000995. RE_EcoRV. 1 hit.
SUPFAMSSF52980. SSF52980. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP04390.

Entry information

Entry nameT2E5_ECOLX
AccessionPrimary (citable) accession number: P04390
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references