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P00472

- MTE1_ECOLX

UniProt

P00472 - MTE1_ECOLX

Protein

Modification methylase EcoRI

Gene

ecoRIM

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence GAATTC, causes specific methylation on A-3 on both strands, and protects the DNA from cleavage by the EcoRI endonuclease.

    Catalytic activityi

    S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro
    2. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC

    GO - Biological processi

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

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Restriction system

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Protein family/group databases

    REBASEi3395. M.EcoRI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase EcoRI (EC:2.1.1.72)
    Short name:
    M.EcoRI
    Alternative name(s):
    Adenine-specific methyltransferase EcoRI
    Gene namesi
    Name:ecoRIM
    Encoded oniPlasmid pMB11 Publication
    Plasmid pMB41 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 326325Modification methylase EcoRIPRO_0000087959Add
    BLAST

    Proteomic databases

    PRIDEiP00472.

    Interactioni

    Subunit structurei

    Monomer.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the N(4)/N(6)-methyltransferase family.Curated

    Family and domain databases

    InterProiIPR002052. DNA_methylase_N6_adenine_CS.
    IPR025247. EcoRI_methylase.
    [Graphical view]
    PfamiPF13651. EcoRI_methylase. 1 hit.
    [Graphical view]
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00472-1 [UniParc]FASTAAdd to Basket

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    MARNATNKLL HKAKKSKSDE FYTQYCDIEN ELQYYREHFS DKVVYCNCDD    50
    PRVSNFFKYF AVNFDNLGLK KLIASCYVEN KEGFSSSEAA KNGFYYEYHK 100
    ENGKKLVFDD ISVSSFCGDG DFRSSESIDL LKKSDIVVTN PPFSLFREYL 150
    DQLIKYDKKF LIIANVNSIT YKEVFNLIKE NKIWLGVHLG RGVSGFIVPE 200
    HYELYGTEAR IDSNGNRIIS PNNCLWLTNL DVFIRHKDLP LTRKYFGNES 250
    SYPKYDNYDA INVNKTKDIP LDYNGVMGVP ITFLHKFNPE QFELIKFRKG 300
    VDEKDLSING KCPYFRILIK NKRLQK 326
    Length:326
    Mass (Da):38,044
    Last modified:January 23, 2007 - v2
    Checksum:i5F6AFE1DD1CBB1A8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01675 Genomic DNA. Translation: AAA26372.1.
    PIRiA92308. XYECP4.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01675 Genomic DNA. Translation: AAA26372.1 .
    PIRi A92308. XYECP4.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3395. M.EcoRI.

    Proteomic databases

    PRIDEi P00472.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002052. DNA_methylase_N6_adenine_CS.
    IPR025247. EcoRI_methylase.
    [Graphical view ]
    Pfami PF13651. EcoRI_methylase. 1 hit.
    [Graphical view ]
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    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: CONFIRMATION OF AMINO AND CARBOXYL ENDS OF SEQUENCE BY AMINO ACID ANALYSIS.

    Entry informationi

    Entry nameiMTE1_ECOLX
    AccessioniPrimary (citable) accession number: P00472
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 71 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

    Plasmid

    Documents

    1. Restriction enzymes and methylases
      Classification of restriction enzymes and methylases and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3