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Q47282

- T1ME_ECOLX

UniProt

Q47282 - T1ME_ECOLX

Protein

Type I restriction enzyme EcoEI M protein

Gene

hsdM

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. The EcoEI enzyme recognizes 5'-GAGN7ATGC-3'.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei226 – 2261S-adenosyl-L-methionineBy similarity

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type I restriction enzyme EcoEI M protein (EC:2.1.1.72)
    Short name:
    M.EcoEI
    Gene namesi
    Name:hsdM
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 490490Type I restriction enzyme EcoEI M proteinPRO_0000088021Add
    BLAST

    Proteomic databases

    PRIDEiQ47282.

    Interactioni

    Subunit structurei

    The type I restriction/modification system is composed of three polypeptides R, M and S.

    Structurei

    3D structure databases

    ProteinModelPortaliQ47282.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni163 – 1686S-adenosyl-L-methionine bindingBy similarity
    Regioni193 – 1953S-adenosyl-L-methionine bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0286.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR022749. D12N6_MeTrfase_N.
    IPR003356. DNA_methylase_A-5.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR002296. N12N6_MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF12161. HsdM_N. 1 hit.
    PF02384. N6_Mtase. 1 hit.
    [Graphical view]
    PRINTSiPR00507. N12N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q47282-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSISSVIKSL QDIMRKDAGV DGDAQRLGQL SWLLFLKIFD TQEEELELEQ    50
    DDYQFPIPQR YLWRSWAANS EGITGDALLE FVNDDLFPTL KNLTAPIDKN 100
    PRGFVVKQAF SDAYNYMKNG TLLRQVINKL NEIDFSSSQE RHLFGDIYEQ 150
    ILRDLQSAGN AGEFYTPRAV TRFMVNRIDP KLGESIMDPA CGTGGFLACA 200
    FDHVKDNYVK TTEDHKTLQQ QIYGVEKKQL PHLLCTTNML LHGIEVPVQI 250
    RHDNTLNKPL SSWDEQVDVI VTNPPFGGTE EDGIEKNFPA EMQTRETADL 300
    FLQLIIEVLA DKGRAAVVLP DGTLFGEGVK TKIKKLLTEE CNLHTIVRLP 350
    NGVFNPYTGI KTNILFFTKG QPTKEVWFYE HPYPDGVKNY SKTKPMKFEE 400
    FQAEIDWWGN EADDFASREE NNQAWKVGID DIIARNFNLD IKNPYQGETI 450
    SHDPDELLAQ YQTQQAEIGE LRNQLRDILG AALAGNKGAN 490
    Length:490
    Mass (Da):55,620
    Last modified:November 1, 1996 - v1
    Checksum:iA8643DEB39981FFB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18759 Genomic DNA. Translation: AAD15049.1.
    PIRiI41293.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18759 Genomic DNA. Translation: AAD15049.1 .
    PIRi I41293.

    3D structure databases

    ProteinModelPortali Q47282.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q47282.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0286.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR022749. D12N6_MeTrfase_N.
    IPR003356. DNA_methylase_A-5.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR002296. N12N6_MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF12161. HsdM_N. 1 hit.
    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. "Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes."
      Murray N.E., Daniel A.S., Cowan G.M., Sharp P.M.
      Mol. Microbiol. 9:133-143(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A58.

    Entry informationi

    Entry nameiT1ME_ECOLX
    AccessioniPrimary (citable) accession number: Q47282
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg2+ as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.

    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