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P08763

- T3MO_BPP1

UniProt

P08763 - T3MO_BPP1

Protein

Type III restriction-modification system EcoPI enzyme mod

Gene

MOD

Organism
Enterobacteria phage P1 (Bacteriophage P1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    Binds the system-specific DNA recognition site 5'-AGACC-3'. Necessary for restriction and for methylation of A-3.

    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

    REBASEi3390. M.EcoPI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type III restriction-modification system EcoPI enzyme mod (EC:2.1.1.72)
    Short name:
    M.EcoPI
    Alternative name(s):
    EcoPI methyltransferase
    Gene namesi
    Name:MOD
    OrganismiEnterobacteria phage P1 (Bacteriophage P1)
    Taxonomic identifieri10678 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaePunalikevirus
    Virus hostiEnterobacteriaceae [TaxID: 543]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 646646Type III restriction-modification system EcoPI enzyme modPRO_0000088030Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP08763.
    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.

    P08763-1 [UniParc]FASTAAdd to Basket

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    MKKETIFSEV ETANSKQLAV LKANFPQCFD KNGAFIQEKL LEIIRASEVE    50
    LSKESYSLNW LGKSYARLLA NLPPKTLLAE DKTHNQQEEN KNSQNLLIKG 100
    DNLEVLKHMV NAYAEKVNMI YIDPPYNTGK DGFVYNDDRK FTPEQLSELA 150
    GIELDEANRI LEFTTKGSSS HSAWLTFIYP RLYIARELLK EDGVIFISID 200
    DNEDKQLGLL CDEVFGQGNF VAKLPTIMNL KGNHDNFGFS DTHEYIYVYA 250
    KNKDVCSLGQ FDIDESEVEK EWDEDEYGLF KRADTLKRTG QDASRKSRPK 300
    GWFPVFINSE NKVYVTDDDK PLNEDDYVLY PVSPTGEELS WSWGKKKIND 350
    EFYNLIVIDI KDGKNIYKKQ RPALGELPTK KPKSIWYKPE YSTSTATTEL 400
    KNLLGAKLFE GPKPVPLITD LVKIGTKKDS LVLDFFAGSG TTAEAVAYLN 450
    EKDSGCRNFI CIQKDEVINK TKNAYSLGYR SIFEITKKRI QEVFKKSTTT 500
    SDNAAKIGFK VIHTIDDFRA KVESELTLTN HTFFDDAVLT PEQYDALLTT 550
    WCVYDGSLLT TPIEDVDLSG YTAHFCNGRL YLIAPNFTSE ALKALLQKLD 600
    SDEDFAPNKV VFYGCNFESA KQRELNEALK SYANKKSIEL DLVVRN 646
    Length:646
    Mass (Da):73,486
    Last modified:November 1, 1988 - v1
    Checksum:iDB2D8724777A5412
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06287 Genomic DNA. Translation: CAA29614.1.
    PIRiS01351.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06287 Genomic DNA. Translation: CAA29614.1 .
    PIRi S01351.

    3D structure databases

    ProteinModelPortali P08763.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3390. M.EcoPI.

    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], PROTEIN SEQUENCE OF 1-5.

    Entry informationi

    Entry nameiT3MO_BPP1
    AccessioniPrimary (citable) accession number: P08763
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral 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