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P23192

- MTM2_MORBO

UniProt

P23192 - MTM2_MORBO

Protein

Modification methylase MboII

Gene

mboIIM

Organism
Moraxella bovis
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence GAAGA, causes specific methylation on A-5, and protects the DNA from cleavage by the MboII endonuclease. It is not known if the cytosine of the complementary sequence TCTTC is also methylated by this enzyme.

    Catalytic activityi

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

    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

    REBASEi3441. M1.MboII.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase MboII (EC:2.1.1.72)
    Short name:
    M.MboII
    Alternative name(s):
    Adenine-specific methyltransferase MboII
    DNA MTase MboIIA
    Gene namesi
    Name:mboIIM
    OrganismiMoraxella bovis
    Taxonomic identifieri476 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeMoraxella

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 260260Modification methylase MboIIPRO_0000087967Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi12 – 187
    Beta strandi24 – 296
    Helixi39 – 413
    Helixi46 – 6318
    Beta strandi64 – 7411
    Helixi76 – 8813
    Beta strandi92 – 998
    Beta strandi109 – 1113
    Beta strandi117 – 1259
    Helixi132 – 1343
    Helixi141 – 15111
    Beta strandi170 – 1734
    Helixi199 – 20911
    Beta strandi215 – 2206
    Helixi225 – 2328
    Beta strandi236 – 2427
    Helixi244 – 25512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G60X-ray1.74A/B1-260[»]
    ProteinModelPortaliP23192.
    SMRiP23192. Positions 1-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23192.

    Family & Domainsi

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR002941. DNA_methylase_N4/N6.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR001091. RM_Methylase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF01555. N6_N4_Mtase. 1 hit.
    [Graphical view]
    PRINTSiPR00508. S21N4MTFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23192-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLEINKIHQM NCFDFLDQVE NKSVQLAVID PPYNLSKADW DSFDSHNEFL    50
    PFTYRWIDKV LDKLDKDGSL YIFNTPFNCA FICQYLVSKG MIFQNWITWD 100
    KRDGMGSAKR GFSTGQETIL FFSKSKNHTF NYDEVRVPYE STDRIKHASE 150
    KGILKNGKRW FPNPNGRLCG EVWHFSSQRH KEKVNGKTVK LTHITPKPRD 200
    LIERIIRASS NPNDLVLDCF MGSGTTAIVA KKLGRNFIGC DMNAEYVNQA 250
    NFVLNQLEIN 260
    Length:260
    Mass (Da):30,077
    Last modified:November 1, 1991 - v1
    Checksum:iE53354DCA12DBE7C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56977 Genomic DNA. Translation: CAA40297.1.
    PIRiS26835.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56977 Genomic DNA. Translation: CAA40297.1 .
    PIRi S26835.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G60 X-ray 1.74 A/B 1-260 [» ]
    ProteinModelPortali P23192.
    SMRi P23192. Positions 1-256.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3441. M1.MboII.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P23192.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR002941. DNA_methylase_N4/N6.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR001091. RM_Methylase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF01555. N6_N4_Mtase. 1 hit.
    [Graphical view ]
    PRINTSi PR00508. S21N4MTFRASE.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the MboII restriction-modification system."
      Bocklage H., Heeger K., Mueller-Hill B.
      Nucleic Acids Res. 19:1007-1013(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 10900 / DSM 6328 / LMG 986 / NCTC 11013.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS).

    Entry informationi

    Entry nameiMTM2_MORBO
    AccessioniPrimary (citable) accession number: P23192
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Restriction enzymes and methylases
      Classification of restriction enzymes and methylases and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3