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P40813

- T1M_SALTY

UniProt

P40813 - T1M_SALTY

Protein

Type I restriction enzyme StySJI M protein

Gene

hsdM

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (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. The StySJI enzyme recognizes 5'-GAGN6GTRC-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 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

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-4557-MONOMER.

    Protein family/group databases

    REBASEi5596. M.StyLT2ORF4525P.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type I restriction enzyme StySJI M protein (EC:2.1.1.72)
    Short name:
    M.StySJI
    Gene namesi
    Name:hsdM
    Synonyms:hsdT
    Ordered Locus Names:STM4525
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Type I restriction enzyme StySJI M proteinPRO_0000088026Add
    BLAST

    Proteomic databases

    PaxDbiP40813.
    PRIDEiP40813.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi99287.STM4525.

    Structurei

    3D structure databases

    ProteinModelPortaliP40813.
    SMRiP40813. Positions 4-525.
    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

    Phylogenomic databases

    eggNOGiCOG0286.
    HOGENOMiHOG000295041.
    KOiK03427.
    OMAiCDVLRDD.
    OrthoDBiEOG686NCV.
    PhylomeDBiP40813.

    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.

    P40813-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEADYL    50
    PEGYRWDDLK SRIGQDQMQF YRNLLVQLGS DEKKLVQAVF HNVSTTIEQP 100
    KQLTELVSYM DALDWYNGNH GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF 150
    TPRPLIKTII HLLKPQPREV VQDPAAGTAG FLIEADRYVK SQTNDLDDLD 200
    GDTQDFQIHR AFIGLELVPG TRRLALMNCL LHDIEGNLDH GGAIRLGNTL 250
    GSDGENLPKA HIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL 300
    HPGGRAAVVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV 350
    KTNVLFFTKG TVTNPHQDKN CTDDVWVYDL RTNMPSFGKR TPFTEQHLQP 400
    FETVYGEDPH GLSPREEGEW SFNAEESEVA DSEENKNTDQ HQATSRWRKF 450
    SREWIRSAKS DSLDISWLKD KDSIDADSLP EPDVLAAEAM GELVQALGEL 500
    DALMRELGAG DEADAQRQLL NEAFGEVKA 529
    Length:529
    Mass (Da):59,311
    Last modified:February 1, 1995 - v1
    Checksum:iD5EF542069B8A88A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02506 Unassigned DNA. Translation: AAA19429.1.
    AE006468 Genomic DNA. Translation: AAL23343.1.
    RefSeqiNP_463384.1. NC_003197.1.
    WP_001063190.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL23343; AAL23343; STM4525.
    GeneIDi1256051.
    KEGGistm:STM4525.
    PATRICi32388011. VBISalEnt20916_4768.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02506 Unassigned DNA. Translation: AAA19429.1 .
    AE006468 Genomic DNA. Translation: AAL23343.1 .
    RefSeqi NP_463384.1. NC_003197.1.
    WP_001063190.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali P40813.
    SMRi P40813. Positions 4-525.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM4525.

    Protein family/group databases

    REBASEi 5596. M.StyLT2ORF4525P.

    Proteomic databases

    PaxDbi P40813.
    PRIDEi P40813.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL23343 ; AAL23343 ; STM4525 .
    GeneIDi 1256051.
    KEGGi stm:STM4525.
    PATRICi 32388011. VBISalEnt20916_4768.

    Phylogenomic databases

    eggNOGi COG0286.
    HOGENOMi HOG000295041.
    KOi K03427.
    OMAi CDVLRDD.
    OrthoDBi EOG686NCV.
    PhylomeDBi P40813.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-4557-MONOMER.

    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].
      Strain: LT2.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.

    Entry informationi

    Entry nameiT1M_SALTY
    AccessioniPrimary (citable) accession number: P40813
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 96 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

    Complete proteome, Reference proteome

    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