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P11409

- MTP2_PROHU

UniProt

P11409 - MTP2_PROHU

Protein

Modification methylase PvuII

Gene

pvuIIM

Organism
Proteus hauseri
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence CAGCTG, causes specific methylation on C-4 on both strands, and protects the DNA from cleavage by the PvuII endonuclease.

    Catalytic activityi

    S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N(4)-methylcytosine.

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. N-methyltransferase activity Source: InterPro
    3. site-specific DNA-methyltransferase (cytosine-N4-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

    BRENDAi2.1.1.113. 5049.

    Protein family/group databases

    REBASEi3485. M.PvuII.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase PvuII (EC:2.1.1.113)
    Short name:
    M.PvuII
    Alternative name(s):
    N-4 cytosine-specific methyltransferase PvuII
    Gene namesi
    Name:pvuIIM
    OrganismiProteus hauseri
    Taxonomic identifieri183417 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 336336Modification methylase PvuIIPRO_0000087931Add
    BLAST

    Structurei

    Secondary structure

    1
    336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 243
    Beta strandi26 – 338
    Helixi35 – 384
    Helixi39 – 413
    Beta strandi47 – 526
    Beta strandi57 – 593
    Helixi68 – 8619
    Beta strandi87 – 9711
    Beta strandi105 – 1084
    Helixi111 – 12111
    Beta strandi126 – 1349
    Helixi144 – 1485
    Beta strandi157 – 16812
    Helixi173 – 1753
    Beta strandi221 – 2244
    Helixi232 – 2409
    Helixi253 – 26210
    Beta strandi268 – 2714
    Helixi278 – 2858
    Beta strandi289 – 2957
    Helixi297 – 3048
    Helixi305 – 3073
    Helixi314 – 32512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BOOX-ray2.80A14-336[»]
    DisProtiDP00060.
    ProteinModelPortaliP11409.
    SMRiP11409. Positions 16-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11409.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati11 – 1131031Add
    BLAST
    Repeati181 – 2931132Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di3.40.50.150. 2 hits.
    InterProiIPR002941. DNA_methylase_N4/N6.
    IPR017985. MeTrfase_CN4_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.
    PROSITEiPS00093. N4_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P11409-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMTLNLQTMS SNDMLNFGKK PAYTTSNGSM YIGDSLELLE SFPDESISLV    50
    MTSPPFALQR KKEYGNLEQH EYVDWFLSFA KVVNKKLKPD GSFVVDFGGA 100
    YMKGVPARSI YNFRVLIRMI DEVGFFLAED FYWFNPSKLP SPIEWVNKRK 150
    IRVKDAVNTV WWFSKTEWPK SDITKVLAPY SDRMKKLIED PDKFYTPKTR 200
    PSGHDIGKSF SKDNGGSIPP NLLQISNSES NGQYLANCKL MGIKAHPARF 250
    PAKLPEFFIR MLTEPDDLVV DIFGGSNTTG LVAERESRKW ISFEMKPEYV 300
    AASAFRFLDN NISEEKITDI YNRILNGESL DLNSII 336
    Length:336
    Mass (Da):38,365
    Last modified:October 1, 1996 - v2
    Checksum:i084371A667F86B91
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441D → E in CAA32026. (PubMed:2662138)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13778 Genomic DNA. Translation: CAA32026.1.
    AF305615 Genomic DNA. Translation: AAA96336.1.
    PIRiS04739.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13778 Genomic DNA. Translation: CAA32026.1 .
    AF305615 Genomic DNA. Translation: AAA96336.1 .
    PIRi S04739.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BOO X-ray 2.80 A 14-336 [» ]
    DisProti DP00060.
    ProteinModelPortali P11409.
    SMRi P11409. Positions 16-335.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3485. M.PvuII.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 2.1.1.113. 5049.

    Miscellaneous databases

    EvolutionaryTracei P11409.

    Family and domain databases

    Gene3Di 3.40.50.150. 2 hits.
    InterProi IPR002941. DNA_methylase_N4/N6.
    IPR017985. MeTrfase_CN4_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 PS00093. N4_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence, internal homology and high-level expression of the gene for a DNA-(cytosine N4)-methyltransferase, M.Pvu II."
      Tao T., Walter J., Brennan K.J., Cotterman M.M., Blumenthal R.M.
      Nucleic Acids Res. 17:4161-4175(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.
    2. "Gene pvuIIW: a possible modulator of PvuII endonuclease subunit association."
      Adams G.M., Blumenthal R.M.
      Gene 157:193-199(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80, SEQUENCE REVISION TO 44.
      Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.
    3. "Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment."
      Gong W., O'Gara M., Blumenthal R.M., Cheng X.
      Nucleic Acids Res. 25:2702-2715(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiMTP2_PROHU
    AccessioniPrimary (citable) accession number: P11409
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 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