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P10484

- T1M1_ECOLX

UniProt

P10484 - T1M1_ECOLX

Protein

Type I restriction enzyme EcoR124II 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 93 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Methylation of specific adenine residues; required for both restriction and modification activities By similarity. The EcoR124/3 I enzyme recognizes 5'-GAAN7RTCG-3'.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei254 – 2541S-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

    Enzyme and pathway databases

    BRENDAi2.1.1.72. 2026.

    Protein family/group databases

    REBASEi3392. M.EcoR124I.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type I restriction enzyme EcoR124II M protein (EC:2.1.1.72)
    Short name:
    M.EcoR124II
    Gene namesi
    Name:hsdM
    Synonyms:hsm
    Encoded oniPlasmid IncFIV R124/30 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 520520Type I restriction enzyme EcoR124II M proteinPRO_0000088023Add
    BLAST

    Proteomic databases

    PRIDEiP10484.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-17004N.

    Structurei

    3D structure databases

    ProteinModelPortaliP10484.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni198 – 2036S-adenosyl-L-methionine bindingBy similarity
    Regioni230 – 2323S-adenosyl-L-methionine bindingBy similarity

    Sequence similaritiesi

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

    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.
    IPR004546. Restrct_endonuc_typeI_HsdM.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF12161. HsdM_N. 1 hit.
    PF02384. N6_Mtase. 1 hit.
    [Graphical view]
    PRINTSiPR00507. N12N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 2 hits.
    TIGRFAMsiTIGR00497. hsdM. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10484-1 [UniParc]FASTAAdd to Basket

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    MKMTSIQQRA ELHRQIWQIA NDVRGSVDGW DFKQYVLGAL FYRFISENFS    50
    SYIEAGDDSI CYAKLDDSVI TDDIKDDAIK TKGYFIYPSQ LFCNVAAKAN 100
    TNDRLNADLN SIFVAIESSA YGYPSEADIK GLFADFDTTS NRLGNTVKDK 150
    NARLAAVLKG VEGLKLGDFN EHQIDLFGDA YEFLISNYAA NAGKSGGEFF 200
    TPQHVSKLIA QLAMHGQTHV NKIYDPAAGS GSLLLQAKKQ FDNHIIEEGF 250
    FGQEINHTTY NLARMNMFLH NINYDKFDIK LGNTLTEPHF RDEKPFDAIV 300
    SNPPYSVKWI GSDDPTLIND ERFAPAGVLA PKSKADFAFV LHALNYLSAK 350
    GRAAIVCFPG IFYRGGAEQK IRQYLVDNNY VETVISLAPN LFFGTTIAVN 400
    ILVLSKHKTD TNVQFIDASE LFKKETNNNI LTDAHIEQIM QVFASKEDVA 450
    HLAKSVAFET VVANDYNLSV SSYVEAKDNR EIIDIAELNA ELKTTVSKID 500
    QLRKDIDAIV AEIEGCEVQK 520
    Length:520
    Mass (Da):58,013
    Last modified:July 1, 1989 - v1
    Checksum:i8D82E715F41D94C3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13145 Genomic DNA. Translation: CAA31541.1.
    PIRiS02166.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13145 Genomic DNA. Translation: CAA31541.1 .
    PIRi S02166.

    3D structure databases

    ProteinModelPortali P10484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-17004N.

    Protein family/group databases

    REBASEi 3392. M.EcoR124I.

    Proteomic databases

    PRIDEi P10484.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 2.1.1.72. 2026.

    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.
    IPR004546. Restrct_endonuc_typeI_HsdM.
    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. 2 hits.
    TIGRFAMsi TIGR00497. hsdM. 1 hit.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I DNA restriction and modification enzymes."
      Price C., Lingner J., Bickle J., Firman T.A., Glover S.W.
      J. Mol. Biol. 205:115-125(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiT1M1_ECOLX
    AccessioniPrimary (citable) accession number: P10484
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 93 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.

    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