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P00642

- T2E1_ECOLX

UniProt

P00642 - T2E1_ECOLX

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Protein
Type-2 restriction enzyme EcoRI
Gene
ecoRIR
Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequence GAATTC and cleaves after G-1.

Catalytic activityi

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

Cofactori

Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911
Metal bindingi91 – 911Magnesium 1
Metal bindingi91 – 911Magnesium 2
Active sitei111 – 1111
Metal bindingi111 – 1111Magnesium 1
Active sitei113 – 1131

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC
  3. magnesium ion binding Source: InterPro

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

REBASEi993. EcoRI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme EcoRI (EC:3.1.21.4)
Short name:
R.EcoRI
Alternative name(s):
Endonuclease EcoRI
Type II restriction enzyme EcoRI
Gene namesi
Name:ecoRIR
Encoded oniPlasmid pMB11 Publication
Plasmid pMB41 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441E → D: Only nicks double strand DNA. 1 Publication
Mutagenesisi144 – 1441E → Q: Inactivates the enzyme. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 277276Type-2 restriction enzyme EcoRI
PRO_0000077303Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-16997N.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 3111
Helixi35 – 4915
Beta strandi55 – 595
Helixi63 – 7311
Beta strandi94 – 985
Beta strandi104 – 11411
Helixi118 – 1236
Turni129 – 1324
Beta strandi134 – 1363
Helixi142 – 1454
Helixi146 – 15611
Turni157 – 1593
Beta strandi160 – 1623
Beta strandi165 – 1717
Helixi172 – 1743
Beta strandi179 – 1824
Beta strandi184 – 1863
Beta strandi188 – 1914
Turni196 – 1983
Helixi201 – 2033
Helixi205 – 2084
Beta strandi213 – 2153
Beta strandi221 – 2233
Beta strandi225 – 2273
Beta strandi230 – 2323
Beta strandi236 – 2394
Helixi248 – 26518
Helixi267 – 2693
Helixi271 – 2755

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00642.
SMRiP00642. Positions 17-277.

Miscellaneous databases

EvolutionaryTraceiP00642.

Family & Domainsi

Family and domain databases

Gene3Di3.40.580.10. 1 hit.
InterProiIPR011335. Restrct_endonuc-II-like.
IPR004221. Restrct_endonuc_II_EcoRI.
IPR011336. Restrct_endonuc_II_EcoRI/MunI.
IPR018131. Restrct_endonuc_II_EcoRI_Pbac.
[Graphical view]
PfamiPF02963. EcoRI. 1 hit.
[Graphical view]
PIRSFiPIRSF001002. Restrict_endonuc_II_EcoRI. 1 hit.
ProDomiPD039825. Restrict_endonuc_II_EcoRI. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00642-1 [UniParc]FASTAAdd to Basket

« Hide

MSNKKQSNRL TEQHKLSQGV IGIFGDYAKA HDLAVGEVSK LVKKALSNEY    50
PQLSFRYRDS IKKTEINEAL KKIDPDLGGT LFVSNSSIKP DGGIVEVKDD 100
YGEWRVVLVA EAKHQGKDII NIRNGLLVGK RGDQDLMAAG NAIERSHKNI 150
SEIANFMLSE SHFPYVLFLE GSNFLTENIS ITRPDGRVVN LEYNSGILNR 200
LDRLTAANYG MPINSNLCIN KFVNHKDKSI MLQAASIYTQ GDGREWDSKI 250
MFEIMFDIST TSLRVLGRDL FEQLTSK 277
Length:277
Mass (Da):31,059
Last modified:January 23, 2007 - v2
Checksum:i83EDC82868261B4B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01675 Genomic DNA. Translation: AAA26371.1.
PIRiB92308. NDECP4.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01675 Genomic DNA. Translation: AAA26371.1 .
PIRi B92308. NDECP4.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CKQ X-ray 1.85 A 2-277 [» ]
1CL8 X-ray 1.80 A 2-277 [» ]
1ERI X-ray 2.50 A 2-277 [» ]
1QC9 X-ray 3.00 A/B/C 2-277 [» ]
1QPS X-ray 2.50 A 17-277 [» ]
1QRH X-ray 2.50 A 17-277 [» ]
1QRI X-ray 2.60 A 17-277 [» ]
2OXV X-ray 1.95 A 1-277 [» ]
ProteinModelPortali P00642.
SMRi P00642. Positions 17-277.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-16997N.

Chemistry

BindingDBi P00642.
ChEMBLi CHEMBL5729.

Protein family/group databases

REBASEi 993. EcoRI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P00642.

Family and domain databases

Gene3Di 3.40.580.10. 1 hit.
InterProi IPR011335. Restrct_endonuc-II-like.
IPR004221. Restrct_endonuc_II_EcoRI.
IPR011336. Restrct_endonuc_II_EcoRI/MunI.
IPR018131. Restrct_endonuc_II_EcoRI_Pbac.
[Graphical view ]
Pfami PF02963. EcoRI. 1 hit.
[Graphical view ]
PIRSFi PIRSF001002. Restrict_endonuc_II_EcoRI. 1 hit.
ProDomi PD039825. Restrict_endonuc_II_EcoRI. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF52980. SSF52980. 1 hit.
ProtoNeti Search...

Publicationsi

  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].
    Plasmid: pMB1
  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.
    Plasmid: pMB4
  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.

Entry informationi

Entry nameiT2E1_ECOLX
AccessioniPrimary (citable) accession number: P00642
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

External Data

Dasty 3

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