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P00642 (T2E1_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. 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 EcoRI

Short name=R.EcoRI
EC=3.1.21.4
Alternative name(s):
Endonuclease EcoRI
Type II restriction enzyme EcoRI
Gene names
Name:ecoRIR
Encoded onPlasmid pMB1 Ref.1
Plasmid pMB4 Ref.2
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length277 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 GAATTC and cleaves after G-1.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 277276Type-2 restriction enzyme EcoRI
PRO_0000077303

Sites

Active site911
Active site1111
Active site1131
Metal binding911Magnesium 1
Metal binding911Magnesium 2
Metal binding1111Magnesium 1

Experimental info

Mutagenesis1441E → D: Only nicks double strand DNA. Ref.7
Mutagenesis1441E → Q: Inactivates the enzyme. Ref.7

Secondary structure

....................................................... 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00642 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 83EDC82868261B4B

FASTA27731,059
        10         20         30         40         50         60 
MSNKKQSNRL TEQHKLSQGV IGIFGDYAKA HDLAVGEVSK LVKKALSNEY PQLSFRYRDS 

        70         80         90        100        110        120 
IKKTEINEAL KKIDPDLGGT LFVSNSSIKP DGGIVEVKDD YGEWRVVLVA EAKHQGKDII 

       130        140        150        160        170        180 
NIRNGLLVGK RGDQDLMAAG NAIERSHKNI SEIANFMLSE SHFPYVLFLE GSNFLTENIS 

       190        200        210        220        230        240 
ITRPDGRVVN LEYNSGILNR LDRLTAANYG MPINSNLCIN KFVNHKDKSI MLQAASIYTQ 

       250        260        270 
GDGREWDSKI MFEIMFDIST TSLRVLGRDL FEQLTSK 

« Hide

References

[1]"Sequence analysis of the DNA encoding the Eco RI endonuclease and methylase."
Greene P.J., Gupta M., Boyer H.W., Brown W.E., Rosenberg J.M.
J. Biol. Chem. 256:2143-2153(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequences of structural genes for Eco RI DNA restriction and modification enzymes."
Newman A.K., Rubin R.A., Kim S.-H., Modrich P.
J. Biol. Chem. 256:2131-2139(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C.
[3]"Partial NH2- and COOH-terminal sequence analyses of Eco RI DNA restriction and modification enzymes."
Rubin R.A., Modrich P., Vanaman T.C.
J. Biol. Chem. 256:2140-2142(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN SEQUENCE OF C-TERMINUS.
[4]"Structure of the DNA-Eco RI endonuclease recognition complex at 3-A resolution."
McClarin J.A., Frederick C.A., Wang B.-C., Greene P., Boyer H.W., Grable J., Rosenberg J.M.
Science 234:1526-1541(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[5]"Refinement of Eco RI endonuclease crystal structure: a revised protein chain tracing."
Kim Y., Grable J.C., Love R., Greene P.J., Rosenberg J.M.
Science 249:1307-1309(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[6]"Structure and function of restriction endonucleases."
Rosenberg J.M.
Curr. Opin. Struct. Biol. 1:104-113(1991)
Cited for: REVIEW.
[7]"Probing the role of glutamic acid 144 in the EcoRI endonuclease using aspartic acid and glutamine replacements."
Hager P.W., Reich N.O., Day J.P., Coche T.G., Boyer H.W., Rosenberg J.M., Greene P.J.
J. Biol. Chem. 265:21520-21526(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-144.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01675 Genomic DNA. Translation: AAA26371.1.
PIRNDECP4. B92308.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CKQX-ray1.85A2-277[»]
1CL8X-ray1.80A2-277[»]
1ERIX-ray2.50A2-277[»]
1QC9X-ray3.00A/B/C2-277[»]
1QPSX-ray2.50A17-277[»]
1QRHX-ray2.50A17-277[»]
1QRIX-ray2.60A17-277[»]
2OXVX-ray1.95A1-277[»]
ProteinModelPortalP00642.
SMRP00642. Positions 17-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-16997N.

Chemistry

BindingDBP00642.
ChEMBLCHEMBL5729.

Protein family/group databases

REBASE993. EcoRI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.580.10. 1 hit.
InterProIPR011335. Restrct_endonuc-II-like.
IPR004221. Restrct_endonuc_II_EcoRI.
IPR011336. Restrct_endonuc_II_EcoRI/MunI.
IPR018131. Restrct_endonuc_II_EcoRI_Pbac.
[Graphical view]
PfamPF02963. EcoRI. 1 hit.
[Graphical view]
PIRSFPIRSF001002. Restrict_endonuc_II_EcoRI. 1 hit.
ProDomPD039825. Restrict_endonuc_II_EcoRI. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF52980. SSF52980. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00642.

Entry information

Entry nameT2E1_ECOLX
AccessionPrimary (citable) accession number: P00642
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 108 of the entry and version 2 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