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P00642

- T2E1_ECOLX

UniProt

P00642 - T2E1_ECOLX

Protein

Type-2 restriction enzyme EcoRI

Gene

ecoRIR

Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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. magnesium ion binding Source: InterPro
    3. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC

    GO - Biological processi

    1. DNA restriction-modification system Source: UniProtKB-KW

    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 EcoRIPRO_0000077303Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-16997N.

    Structurei

    Secondary structure

    1
    277
    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.
    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

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    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: October 1, 2014
    This is version 109 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