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Protein

Type-2 restriction enzyme EcoRI

Gene

ecoRIR

Organism
Escherichia coli
Status
Reviewed-Annotation score: 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

Mg2+Note: Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei911
Metal bindingi91Magnesium 11
Metal bindingi91Magnesium 21
Active sitei1111
Metal bindingi111Magnesium 11
Active sitei1131

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi144E → D: Only nicks double strand DNA. 1 Publication1
Mutagenesisi144E → Q: Inactivates the enzyme. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5729.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000773032 – 277Type-2 restriction enzyme EcoRIAdd BLAST276

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-16997N.

Chemistry databases

BindingDBiP00642.

Structurei

Secondary structure

1277
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 31Combined sources11
Helixi35 – 49Combined sources15
Beta strandi55 – 59Combined sources5
Helixi63 – 73Combined sources11
Beta strandi94 – 98Combined sources5
Beta strandi104 – 114Combined sources11
Helixi118 – 123Combined sources6
Turni129 – 132Combined sources4
Beta strandi134 – 136Combined sources3
Helixi142 – 145Combined sources4
Helixi146 – 156Combined sources11
Turni157 – 159Combined sources3
Beta strandi160 – 162Combined sources3
Beta strandi165 – 171Combined sources7
Helixi172 – 174Combined sources3
Beta strandi179 – 182Combined sources4
Beta strandi184 – 186Combined sources3
Beta strandi188 – 191Combined sources4
Turni196 – 198Combined sources3
Helixi201 – 203Combined sources3
Helixi205 – 208Combined sources4
Beta strandi213 – 215Combined sources3
Beta strandi221 – 223Combined sources3
Beta strandi225 – 227Combined sources3
Beta strandi230 – 232Combined sources3
Beta strandi236 – 239Combined sources4
Helixi248 – 265Combined sources18
Helixi267 – 269Combined sources3
Helixi271 – 275Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MSNKKQSNRL TEQHKLSQGV IGIFGDYAKA HDLAVGEVSK LVKKALSNEY
60 70 80 90 100
PQLSFRYRDS IKKTEINEAL KKIDPDLGGT LFVSNSSIKP DGGIVEVKDD
110 120 130 140 150
YGEWRVVLVA EAKHQGKDII NIRNGLLVGK RGDQDLMAAG NAIERSHKNI
160 170 180 190 200
SEIANFMLSE SHFPYVLFLE GSNFLTENIS ITRPDGRVVN LEYNSGILNR
210 220 230 240 250
LDRLTAANYG MPINSNLCIN KFVNHKDKSI MLQAASIYTQ GDGREWDSKI
260 270
MFEIMFDIST TSLRVLGRDL FEQLTSK
Length:277
Mass (Da):31,059
Last modified:January 23, 2007 - v2
Checksum:i83EDC82868261B4B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01675 Genomic DNA. Translation: AAA26371.1.
PIRiB92308. NDECP4.
RefSeqiWP_001565219.1. NZ_LVSW01000143.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01675 Genomic DNA. Translation: AAA26371.1.
PIRiB92308. NDECP4.
RefSeqiWP_001565219.1. NZ_LVSW01000143.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-16997N.

Chemistry databases

BindingDBiP00642.
ChEMBLiCHEMBL5729.

Protein family/group databases

REBASEi993. EcoRI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00642.

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.
ProtoNetiSearch...

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: November 2, 2016
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.