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P13906

- MTB1_LYSSH

UniProt

P13906 - MTB1_LYSSH

Protein

Modification methylase BspRI

Gene

bspRIM

Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 3 (15 Jun 2010)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the BspRI endonuclease.

    Catalytic activityi

    S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei156 – 1561S-methylcysteine intermediate

    GO - Molecular functioni

    1. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB-EC
    2. DNA binding Source: InterPro

    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

    REBASEi3322. M.BspRI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase BspRI (EC:2.1.1.37)
    Short name:
    M.BspRI
    Alternative name(s):
    Cytosine-specific methyltransferase BspRI
    Gene namesi
    Name:bspRIM
    OrganismiLysinibacillus sphaericus (Bacillus sphaericus)
    Taxonomic identifieri1421 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424Modification methylase BspRIPRO_0000087862Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811S-methylcysteine; by autocatalysis

    Post-translational modificationi

    In the absence of DNA, can self-methylate two cysteine residues.

    Keywords - PTMi

    Methylation

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP13906.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 408351SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
    Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR018117. C5_DNA_meth_AS.
    IPR001525. C5_MeTfrase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR10629. PTHR10629. 1 hit.
    PfamiPF00145. DNA_methylase. 2 hits.
    [Graphical view]
    PRINTSiPR00105. C5METTRFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    TIGRFAMsiTIGR00675. dcm. 1 hit.
    PROSITEiPS00094. C5_MTASE_1. 1 hit.
    PS00095. C5_MTASE_2. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P13906-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIKINEKGR GKFKPAPTYE KEEVRQLLME KINEEMEAVA TATSDISNDE    50
    IQYKSDKFNV LSLFCGAGGL DLGFELAGLE QSLGTDKALE AFKDRDVYNA 100
    IRHESVFHTV YANDIFSEAL QTYEKNMPNH VFIHEKDIRK IKEFPSANLV 150
    IGGFPCPGFS EAGPRLVDDE RNFLYIHFIR CLMQVQPEIF VAENVKGMMT 200
    LGGGEVFRQI VEDFGAAGYR VEARLLNARD YGVPQIRERV IIVGVRNDID 250
    FNYEYPEITH GNEEGLKPYV TLEEAIGDLS LDPGPYFTGS YSTIFMSRNR 300
    KKKWTDQSFT IQASGRQAPI HPGGLPMEKV DKNKWIFPDG EENHRRLSVK 350
    EIKRIQTFPD WYEFSDGGNM KVSVNNRLDK QYKQIGNAVP VFLARAVAKS 400
    IAQFAADYLK DNHPHEAPQM KLFI 424
    Length:424
    Mass (Da):48,212
    Last modified:June 15, 2010 - v3
    Checksum:i1DED6A45DB0A4FCF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15758 Genomic DNA. Translation: CAA33764.2.
    PIRiS07792.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15758 Genomic DNA. Translation: CAA33764.2 .
    PIRi S07792.

    3D structure databases

    ProteinModelPortali P13906.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3322. M.BspRI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR018117. C5_DNA_meth_AS.
    IPR001525. C5_MeTfrase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10629. PTHR10629. 1 hit.
    Pfami PF00145. DNA_methylase. 2 hits.
    [Graphical view ]
    PRINTSi PR00105. C5METTRFRASE.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    TIGRFAMsi TIGR00675. dcm. 1 hit.
    PROSITEi PS00094. C5_MTASE_1. 1 hit.
    PS00095. C5_MTASE_2. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the Bacillus sphaericus R modification methylase gene."
      Posfai G., Kiss A., Erdei S., Posfai J., Venetianer P.
      J. Mol. Biol. 170:597-610(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: SEQUENCE REVISION TO 322, PARTIAL PROTEIN SEQUENCE, AUTOMETHYLATION AT CYS-181.
    3. Rasko T., Der A., Klement E., Posfai E., Medzihradszky K.F., Marshak D.R., Roberts R.J., Kiss A.
      Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 394.

    Entry informationi

    Entry nameiMTB1_LYSSH
    AccessioniPrimary (citable) accession number: P13906
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 87 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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