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P29347

- MTS1_STRSA

UniProt

P29347 - MTS1_STRSA

Protein

Modification methylase StsI

Gene

stsIM

Organism
Streptococcus sanguinis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence 5'-GGATG-3' in one strand and 3'-CATCC-5' in the other, causes specific methylation on the A of both strands, and protects the DNA from cleavage by the StsI endonuclease. The 2 domains of the protein participates in modification of the two strands.

    Catalytic activityi

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

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro
    2. 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

    REBASEi3512. M.StsI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase StsI (EC:2.1.1.72)
    Short name:
    M.StsI
    Alternative name(s):
    Adenine-specific methyltransferase StsI
    Gene namesi
    Name:stsIM
    OrganismiStreptococcus sanguinis
    Taxonomic identifieri1305 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 653653Modification methylase StsIPRO_0000087962Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP29347.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di1.10.1020.10. 1 hit.
    3.40.50.150. 4 hits.
    InterProiIPR012186. Ade-mod_methylase_MStsI.
    IPR023095. Ade_MeTrfase_dom_2.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR012327. MeTrfase_D12.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF02086. MethyltransfD12. 2 hits.
    [Graphical view]
    PIRSFiPIRSF036638. M_m6A_StsI. 1 hit.
    PRINTSiPR00505. D12N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 3 hits.
    TIGRFAMsiTIGR00571. dam. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P29347-1 [UniParc]FASTAAdd to Basket

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    MRYIGSKKLL LPEIKKMVDK HTDGSEEVFL DLFAGTNVVA NYFKQFYTVY    50
    SNDMLFFSYV NAKATIENNS KPSFSKLIQA GISSPMTYLQ NLEVNDETIG 100
    YYEVAYSPTG EANYLSVHNA KKLDIIRSQI ESWKNQNLLT EHEYYYLLSS 150
    LIEALPFISN TTGTYGAFLK HWDKRSLNDL ELQDFTIFDN SKQNKAFNED 200
    ANELVQKIKA DIVYIDTPYN SRQYASNYHL LENVARNEHP TLKGITKIFD 250
    WKNLKSDYAT KGKALVAMRD LIQNINSTHI ILSYNNEGII SEEDLTNILK 300
    EFSVDGIVDI KKIPYRKYQS KNVSKNKEIY ELLFYIQRKP FSKNKTLNKP 350
    LNNVRVSSTK KYIKSPLNYI GGKYKLLNQI LPLFPKNINT FVDIFSGGAN 400
    VGINVKAKKY IFNDMNTRIN EMFRYFQTQP PVKLVQQIEE KIDEWGLSKT 450
    NEDAFLAFRK HYNTNPNPLD LYVLSSFSYN YQFRFNNSME FNNPFGRNRS 500
    HFSENMRNNL LNFVTKLQTL DATFTDNYFN EFDFSNLTSN DFIYLDPPYL 550
    ITTGSYNDGK RGFSDWNNTS EMKLLNFMDY LNQHGIRFAL SNVTEHKGKT 600
    NQLLKDWAYS RNLNVNYLDH NYNNSSHNSK SKGSQEVLIT NYETKTFNLL 650
    NTK 653
    Length:653
    Mass (Da):76,068
    Last modified:December 1, 1992 - v1
    Checksum:iC4D42B76E5665E91
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11101 Genomic DNA. Translation: BAA01876.1.
    PIRiS35493.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11101 Genomic DNA. Translation: BAA01876.1 .
    PIRi S35493.

    3D structure databases

    ProteinModelPortali P29347.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3512. M.StsI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.1020.10. 1 hit.
    3.40.50.150. 4 hits.
    InterProi IPR012186. Ade-mod_methylase_MStsI.
    IPR023095. Ade_MeTrfase_dom_2.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR012327. MeTrfase_D12.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF02086. MethyltransfD12. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF036638. M_m6A_StsI. 1 hit.
    PRINTSi PR00505. D12N6MTFRASE.
    SUPFAMi SSF53335. SSF53335. 3 hits.
    TIGRFAMsi TIGR00571. dam. 1 hit.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of the StsI restriction-modification gene: presence of homology to FokI restriction-modification enzymes."
      Kita K., Suisha M., Kotani H., Yanase H., Kato N.
      Nucleic Acids Res. 20:4167-4172(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 54.

    Entry informationi

    Entry nameiMTS1_STRSA
    AccessioniPrimary (citable) accession number: P29347
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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