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P12364

- T3MO_ECOLX

UniProt

P12364 - T3MO_ECOLX

Protein

Type III restriction-modification system EcoP15I enzyme mod

Gene

mod

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    Binds the system-specific DNA recognition site 5'-CAGCAC-3'. Necessary for both restriction and methylation (of one of the two A's).

    Catalytic activityi

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

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    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

    DNA-binding, S-adenosyl-L-methionine

    Protein family/group databases

    REBASEi3389. M.EcoP15I.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type III restriction-modification system EcoP15I enzyme mod (EC:2.1.1.72)
    Short name:
    M.EcoP15I
    Alternative name(s):
    EcoP15I methyltransferase
    Gene namesi
    Name:mod
    Encoded oniPlasmid p15B0 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 645645Type III restriction-modification system EcoP15I enzyme modPRO_0000088031Add
    BLAST

    Proteomic databases

    PRIDEiP12364.

    Interactioni

    Subunit structurei

    Contains two different subunits: res and mod. Mod is a homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP12364.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni123 – 1264Binding of S-adenosyl methionineSequence Analysis

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di3.40.50.150. 2 hits.
    InterProiIPR002295. D21N6_MeTrfase.
    IPR002941. DNA_methylase_N4/N6.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF01555. N6_N4_Mtase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015855. TypeIII_Mtase_mKpnI. 1 hit.
    PRINTSiPR00506. D21N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 3 hits.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P12364-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKETIFSEV ETANSKQLAV LKANFPQCFD KNGAFIQEKL LEIIRASEVE    50
    LSKESYSLNW LGKSYARLLA NLPPKTLLAE DKTHNQQEEN KNSQHLLIKG 100
    DNLEVLKHMV NAYAEKVKMI YIDPPYNTGK DGFVYNDDRK FTPEQLSELA 150
    GIDLDQAKRI LEFTTKGSSS HSAWLTFIYP RLYIARELMR EDGTIFISID 200
    HNEFSQLKLV CDEIFGEQNH VGDLVWKNAT DNNPSNIAVE HEYIIVYTKN 250
    KEQLISEWKS NISDVKNLLV NIGEEFASKY TGNELQEKYT QWFREHRSEL 300
    WPLDRYKYID KDGIYTGSQS VHNPGKEGYR YDIIHPKTKK PCKQQPLMGY 350
    RFPLDTMDRL LSEEKIIFGD DENKIIELKV YAKDYKQKLS SVIHLDGRVA 400
    TNELKELFPE MTQPFTNAKT IKLVEDLISF ACDGEGIVLD FFAGSGTTAH 450
    TVFNLNNKNK TSYQFITVQL DEPKKDKSDA MKHGYNTIFD LTKERLIRAS 500
    KKNRDQGFKV YQLMADFRAK DESELTLSNH TFFDDVVLTP EQYDTLLTTW 550
    CLYDGSLLTT PIEDVDLGGY KAHLCDGRLY LIAPNFTSEA LKALLQKVDS 600
    DKDFAPNKVV FYGSNFESAK QMELNEALKS YANKKSIELD LVVRN 645
    Length:645
    Mass (Da):74,222
    Last modified:October 1, 1989 - v1
    Checksum:i0EFE6653BAA3A705
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06288 Genomic DNA. Translation: CAA29616.1.
    PIRiS03208.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06288 Genomic DNA. Translation: CAA29616.1 .
    PIRi S03208.

    3D structure databases

    ProteinModelPortali P12364.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3389. M.EcoP15I.

    Proteomic databases

    PRIDEi P12364.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.150. 2 hits.
    InterProi IPR002295. D21N6_MeTrfase.
    IPR002941. DNA_methylase_N4/N6.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF01555. N6_N4_Mtase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015855. TypeIII_Mtase_mKpnI. 1 hit.
    PRINTSi PR00506. D21N6MTFRASE.
    SUPFAMi SSF53335. SSF53335. 3 hits.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1 mod mutants."
      Huembelin M., Suri B., Rao D.N., Hornby D.P., Eberle H., Pripfl T., Kenel S., Bickle T.A.
      J. Mol. Biol. 200:23-29(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiT3MO_ECOLX
    AccessioniPrimary (citable) accession number: P12364
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 82 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

    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