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P25240

- MT57_ECOLX

UniProt

P25240 - MT57_ECOLX

Protein

Modification methylase Eco57IB

Gene

eco57IBM

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence 5'-CTGAAG-3' in one strand and 5'-CTTCAG-3' in the other, causes specific methylation on A-5 on one strand, and protects the DNA from cleavage by the Eco57I endonuclease.

    Catalytic activityi

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

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. N-methyltransferase activity Source: InterPro
    3. 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

    REBASEi5234. M.Eco57I.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase Eco57IB (EC:2.1.1.72)
    Short name:
    M.Eco57IB
    Alternative name(s):
    Adenine-specific methyltransferase Eco57IB
    Gene namesi
    Name:eco57IBM
    Synonyms:eco57IM
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 544544Modification methylase Eco57IBPRO_0000087940Add
    BLAST

    Proteomic databases

    PRIDEiP25240.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP25240.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR003356. DNA_methylase_A-5.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR002296. N12N6_MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF02384. N6_Mtase. 1 hit.
    [Graphical view]
    PRINTSiPR00507. N12N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25240-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFKADQTSQ KLRGGYYTPQ NLADYVTKWV LSKNPKTILE PSCGDGVFIQ    50
    AIANNGYNSN IELFCFELFD TEASKALERC KLNNFSNATI TEGDFLVWAN 100
    ECLKKNKQIF DGALGNPPFI RYQFLERNFQ EQAQLVFEHL DLKFTKHTNA 150
    WVPFLLSSLA LLKQGGRIGM VIPSEISHVM HAQSLRSYLG HVCSKIVIID 200
    PKEIWFEDTL QGAVILLAEK KQYPDEASQG VGIVSVSGFE FLQEDPNVLF 250
    NDTAGINGET VEGKWTKATL SIDELQLIKR VIAHPDVRKF KDIAKVDVGR 300
    YCDGANNYFL VDNETVKLYK LERFAHPMFG RSQHCPGIIY DEKQHIENQE 350
    KGLPTNFLYI DEEFEYLSKS VKNYIKLGEV EEYHKRYKCR IRKPWFKVPS 400
    VYSTEIGMLK RCHDAPRLIH NRVRAYTTDT AYRVSSTVTS TENLVCSFLN 450
    PITVITAELE GLFYGGGVLE LVPSEIEKLY ILIVEGLEHN VEELNLLIKD 500
    GQIERVIRQQ GSLILGTLGF TQEENEKLVE IGRSLEIEGY VSRV 544
    Length:544
    Mass (Da):62,013
    Last modified:May 1, 1992 - v1
    Checksum:i53A1D5D7337AB4FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74821 Genomic DNA. Translation: AAA23388.1.
    X61122 Genomic DNA. Translation: CAA43433.1.
    PIRiS26425.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74821 Genomic DNA. Translation: AAA23388.1 .
    X61122 Genomic DNA. Translation: CAA43433.1 .
    PIRi S26425.

    3D structure databases

    ProteinModelPortali P25240.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 5234. M.Eco57I.

    Proteomic databases

    PRIDEi P25240.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR003356. DNA_methylase_A-5.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR002296. N12N6_MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF02384. N6_Mtase. 1 hit.
    [Graphical view ]
    PRINTSi PR00507. N12N6MTFRASE.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of the genes coding for Eco57I type IV restriction-modification enzymes."
      Janulaitis A., Vaisvila R., Timinskas A., Klimasauskas S., Butkus V.
      Nucleic Acids Res. 20:6051-6056(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: RFL57.
    2. "Purification and properties of the Eco57I restriction endonuclease and methylase -- prototypes of a new class (type IV)."
      Janulaitis A., Petrusyte M., Maneliene Z., Klimasauskas S., Butkus V.
      Nucleic Acids Res. 20:6043-6049(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiMT57_ECOLX
    AccessioniPrimary (citable) accession number: P25240
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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