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P15446

- MTH2_HAEPA

UniProt

P15446 - MTH2_HAEPA

Protein

Modification methylase HpaII

Gene

hpaIIM

Organism
Haemophilus parainfluenzae
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence CCGG, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the HpaII 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 sitei103 – 1031PROSITE-ProRule annotation

    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

    REBASEi3432. M.HpaII.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase HpaII (EC:2.1.1.37)
    Short name:
    M.HpaII
    Alternative name(s):
    Cytosine-specific methyltransferase HpaII
    Gene namesi
    Name:hpaIIM
    OrganismiHaemophilus parainfluenzae
    Taxonomic identifieri729 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551C → Y in temperature-sensitive mutant.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Modification methylase HpaIIPRO_0000087883Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP15446.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 356325SAM-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. 1 hit.
    [Graphical view]
    PRINTSiPR00105. C5METTRFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    TIGRFAMsiTIGR00675. dcm. 1 hit.
    PROSITEiPS00094. C5_MTASE_1. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P15446-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKDVLDDNLL EEPAAQYSLF EPESNPNLRE KFTFIDLFAG IGGFRIAMQN    50
    LGGKCIFSSE WDEQAQKTYE ANFGDLPYGD ITLEETKAFI PEKFDILCAG 100
    FPCQAFSIAG KRGGFEDTRG TLFFDVAEII RRHQPKAFFL ENVKGLKNHD 150
    KGRTLKTILN VLREDLGYFV PEPAIVNAKN FGVPQNRERI YIVGFHKSTG 200
    VNSFSYPEPL DKIVTFADIR EEKTVPTKYY LSTQYIDTLR KHKERHESKG 250
    NGFGYEIIPD DGIANAIVVG GMGRERNLVI DHRITDFTPT TNIKGEVNRE 300
    GIRKMTPREW ARLQGFPDSY VIPVSDASAY KQFGNSVAVP AIQATGKKIL 350
    EKLGNLYD 358
    Length:358
    Mass (Da):40,400
    Last modified:April 1, 1990 - v1
    Checksum:iACE69BFD511C37EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51322 Genomic DNA. Translation: CAA35705.1.
    L17342 Genomic DNA. Translation: AAA20481.1.
    PIRiS15908.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51322 Genomic DNA. Translation: CAA35705.1 .
    L17342 Genomic DNA. Translation: AAA20481.1 .
    PIRi S15908.

    3D structure databases

    ProteinModelPortali P15446.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3432. M.HpaII.

    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. 1 hit.
    [Graphical view ]
    PRINTSi PR00105. C5METTRFRASE.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    TIGRFAMsi TIGR00675. dcm. 1 hit.
    PROSITEi PS00094. C5_MTASE_1. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49669.
    2. "Organization and sequence of the HpaII restriction-modification system and adjacent genes."
      Kulakauskas S., Barsomian J.M., Lubys A., Roberts R.J., Wilson G.G.
      Gene 142:9-15(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiMTH2_HAEPA
    AccessioniPrimary (citable) accession number: P15446
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 84 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