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P04393

- MTE5_ECOLX

UniProt

P04393 - MTE5_ECOLX

Protein

Modification methylase EcoRV

Gene

ecoRVM

Organism
Escherichia coli
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence GATATC, causes specific methylation on A-2 on both strands, and protects the DNA from cleavage by the EcoRV 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

    REBASEi3397. M.EcoRV.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase EcoRV (EC:2.1.1.72)
    Short name:
    M.EcoRV
    Alternative name(s):
    Adenine-specific methyltransferase EcoRV
    Gene namesi
    Name:ecoRVM
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 298298Modification methylase EcoRVPRO_0000087971Add
    BLAST

    Proteomic databases

    PRIDEiP04393.

    Structurei

    3D structure databases

    ProteinModelPortaliP04393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di1.10.1020.10. 1 hit.
    3.40.50.150. 2 hits.
    InterProiIPR023095. Ade_MeTrfase_dom_2.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR012263. M_m6A_EcoRV.
    IPR012327. MeTrfase_D12.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF02086. MethyltransfD12. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000398. M_m6A_EcoRV. 1 hit.
    PRINTSiPR00505. D12N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    TIGRFAMsiTIGR00571. dam. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04393-1 [UniParc]FASTAAdd to Basket

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    MKDKVFVPPI KSQGIKTKLV PCIKRIVPKN FNGVWVEPFM GTGVVAFNVA    50
    PKDALLCDTN PHLISFYNAL KNKDITGDLV KDFLYREGEK LLLSNGEYYY 100
    EVRERFNNYK EPLDFLFLNR SCFNGMIRFN SKGGFNVPFC KKPNRFAQAY 150
    ITKISNQVDR ISEIISKGNY TFLCQSFEKT IGMVNRDDVV YCDPPYIGRH 200
    VDYFNSWGER DERLLFETLS SLNATFITST WHHNDYRENK YVRDLWSSFR 250
    ILTKEHFYHV GASEKNRSPM VEALITNIAK DIIDHIEKSS GDILVIEE 298
    Length:298
    Mass (Da):34,639
    Last modified:March 20, 1987 - v1
    Checksum:i5FF2263E733574D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00530 Genomic DNA. Translation: CAA25209.1.
    M19941 Genomic DNA. Translation: AAA24614.1.
    PIRiA00557. XYECR5.
    RefSeqiNP_863581.1. NC_005019.1.
    WP_011117660.1. NC_005019.1.

    Genome annotation databases

    GeneIDi1446622.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00530 Genomic DNA. Translation: CAA25209.1 .
    M19941 Genomic DNA. Translation: AAA24614.1 .
    PIRi A00557. XYECR5.
    RefSeqi NP_863581.1. NC_005019.1.
    WP_011117660.1. NC_005019.1.

    3D structure databases

    ProteinModelPortali P04393.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3397. M.EcoRV.

    Proteomic databases

    PRIDEi P04393.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1446622.

    Family and domain databases

    Gene3Di 1.10.1020.10. 1 hit.
    3.40.50.150. 2 hits.
    InterProi IPR023095. Ade_MeTrfase_dom_2.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR012263. M_m6A_EcoRV.
    IPR012327. MeTrfase_D12.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF02086. MethyltransfD12. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000398. M_m6A_EcoRV. 1 hit.
    PRINTSi PR00505. D12N6MTFRASE.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    TIGRFAMsi TIGR00571. dam. 1 hit.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the genes coding for the Eco RV restriction and modification system of Escherichia coli."
      Bougueleret L., Schwarzstein M., Tsugita A., Zabeau M.
      Nucleic Acids Res. 12:3659-3676(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The EcoRV restriction-modification system: genes, enzymes, synthetic substrates."
      Kraev A.S., Kravets A.N., Chernov B.K., Skryabin K.G., Baev A.A.
      Mol. Biol. (Mosk.) 19:236-242(1985)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.

    Entry informationi

    Entry nameiMTE5_ECOLX
    AccessioniPrimary (citable) accession number: P04393
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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