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P07989

- T1M_SALPO

UniProt

P07989 - T1M_SALPO

Protein

Type I restriction enzyme StySPI M protein

Gene

hsdM

Organism
Salmonella potsdam
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    • Comment

    Functioni

    Methylation of specific adenine residues; required for both restriction and modification activities.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 sitei216 – 2161S-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

    Protein family/group databases

    REBASEi3518. M.StySPI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type I restriction enzyme StySPI M protein (EC:2.1.1.72)
    Short name:
    M.StySPI
    Gene namesi
    Name:hsdM
    Synonyms:hsdT
    OrganismiSalmonella potsdam
    Taxonomic identifieri597 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Type I restriction enzyme StySPI M proteinPRO_0000088025Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP07989.
    SMRiP07989. Positions 4-527.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni148 – 1536S-adenosyl-L-methionine bindingBy similarity
    Regioni178 – 1803S-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.
    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.

    P07989-1 [UniParc]FASTAAdd to Basket

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    MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEADYL    50
    PEGYRWDDLK SRIGQEQLQF YRNLLVHLGA DEKKLVQAVF QNVNTTITQP 100
    KQLTELVSSM DSLDWYNGDH GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF 150
    TPRPLIKTII HLLKPQPREV VQDPAAGTAG FLIEADRYVK SQTNDLDDLD 200
    GDAQDFQIKK AFVGLELVPG TRRLALMNCL LHDIEGNLDH GGAIRLGNTL 250
    GSDGENLPQA DIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL 300
    PPGGRAAAVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV 350
    KTNVLFFTKG TVANPNQDKN CTDDVWVYDL RTNMPSFGKR TPFTEQHLQP 400
    FETVYGEDPH GLSPRTEGEW SFNAEESEVA DSEENKNADQ HQATSRWRKF 450
    SREWIRTAKS DSLDISWLKD KDSIDADSLP EPDVLAAEAM GELVQALGEL 500
    DALMRELGAG DEADAQRQLL EEAFGGVKA 529
    Length:529
    Mass (Da):58,906
    Last modified:February 1, 1995 - v2
    Checksum:i07895A9ADA4FA249
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02507 Genomic DNA. Translation: AAA27143.1.
    M14984 Genomic DNA. Translation: AAA27144.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02507 Genomic DNA. Translation: AAA27143.1 .
    M14984 Genomic DNA. Translation: AAA27144.1 .

    3D structure databases

    ProteinModelPortali P07989.
    SMRi P07989. Positions 4-527.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3518. M.StySPI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Roles of selection and recombination in the evolution of type I restriction-modification systems in enterobacteria."
      Sharp P.M., Kelleher J.E., Daniel A.S., Cowan G.M., Murray N.E.
      Proc. Natl. Acad. Sci. U.S.A. 89:9836-9840(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Two DNA recognition domains of the specificity polypeptides of a family of type I restriction enzymes."
      Fuller-Pace F.V., Murray N.E.
      Proc. Natl. Acad. Sci. U.S.A. 83:9368-9372(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 455-529.

    Entry informationi

    Entry nameiT1M_SALPO
    AccessioniPrimary (citable) accession number: P07989
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 69 of the entry and version 2 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