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P05102

- MTH1_HAEPH

UniProt

P05102 - MTH1_HAEPH

Protein

Modification methylase HhaI

Gene

hhaIM

Organism
Haemophilus parahaemolyticus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence GCGC, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease.

    Catalytic activityi

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

    Kineticsi

    1. KM=69 nM for DNA1 Publication
    2. KM=15 nM for S-adenosyl-L-methionine (SAM)1 Publication

    Vmax=87.0 nmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei81 – 811

    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

    REBASEi3421. M.HhaI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase HhaI (EC:2.1.1.37)
    Short name:
    M.HhaI
    Alternative name(s):
    Cytosine-specific methyltransferase HhaI
    Gene namesi
    Name:hhaIM
    OrganismiHaemophilus parahaemolyticus
    Taxonomic identifieri735 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi237 – 2371Q → X: Decrease in enzyme activity due to 98%-99% loss of DNA-binding activity. No change in substrate specificity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 327327Modification methylase HhaIPRO_0000087882Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    327
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 114
    Beta strandi13 – 175
    Turni20 – 223
    Helixi23 – 308
    Beta strandi34 – 396
    Helixi43 – 5311
    Helixi61 – 633
    Helixi66 – 683
    Beta strandi73 – 786
    Turni82 – 843
    Turni86 – 894
    Helixi92 – 943
    Helixi96 – 983
    Helixi100 – 11112
    Beta strandi114 – 1218
    Helixi122 – 1254
    Helixi127 – 1304
    Helixi131 – 14212
    Beta strandi148 – 1536
    Helixi154 – 1574
    Beta strandi164 – 1729
    Helixi173 – 1753
    Helixi192 – 1943
    Helixi199 – 2013
    Helixi203 – 2053
    Beta strandi213 – 2164
    Beta strandi228 – 2325
    Beta strandi240 – 2434
    Beta strandi244 – 2463
    Turni258 – 2625
    Beta strandi264 – 2674
    Beta strandi270 – 2734
    Helixi276 – 2827
    Helixi295 – 30410
    Helixi308 – 32316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    10MHX-ray2.55A1-327[»]
    1FJXX-ray2.26A1-327[»]
    1HMYX-ray2.50A1-327[»]
    1M0EX-ray2.50A1-327[»]
    1MHTX-ray2.60A1-327[»]
    1SKMX-ray2.20A1-327[»]
    1SVUX-ray2.66A/B1-327[»]
    2C7OX-ray1.90A1-327[»]
    2C7PX-ray1.70A1-327[»]
    2C7QX-ray1.85A1-327[»]
    2C7RX-ray1.90A1-327[»]
    2HMYX-ray2.61B1-327[»]
    2HR1X-ray1.96A1-327[»]
    2I9KX-ray2.65A1-327[»]
    2UYCX-ray2.00A1-327[»]
    2UYHX-ray2.63A1-327[»]
    2UZ4X-ray2.10A1-327[»]
    2Z6AX-ray2.88A1-327[»]
    2Z6QX-ray2.79A1-327[»]
    2Z6UX-ray2.72A1-327[»]
    2ZCJX-ray2.75A1-327[»]
    3EEOX-ray1.94A1-327[»]
    3MHTX-ray2.70A1-327[»]
    4MHTX-ray2.70A1-327[»]
    5MHTX-ray2.70A1-327[»]
    6MHTX-ray2.05A1-327[»]
    7MHTX-ray2.87A1-327[»]
    8MHTX-ray2.76A1-327[»]
    9MHTX-ray2.39A1-327[»]
    ProteinModelPortaliP05102.
    SMRiP05102. Positions 1-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05102.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 325314SAM-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.
    PS00095. C5_MTASE_2. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P05102-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIEIKDKQLT GLRFIDLFAG LGGFRLALES CGAECVYSNE WDKYAQEVYE    50
    MNFGEKPEGD ITQVNEKTIP DHDILCAGFP CQAFSISGKQ KGFEDSRGTL 100
    FFDIARIVRE KKPKVVFMEN VKNFASHDNG NTLEVVKNTM NELDYSFHAK 150
    VLNALDYGIP QKRERIYMIC FRNDLNIQNF QFPKPFELNT FVKDLLLPDS 200
    EVEHLVIDRK DLVMTNQEIE QTTPKTVRLG IVGKGGQGER IYSTRGIAIT 250
    LSAYGGGIFA KTGGYLVNGK TRKLHPRECA RVMGYPDSYK VHPSTSQAYK 300
    QFGNSVVINV LQYIAYNIGS SLNFKPY 327
    Length:327
    Mass (Da):36,996
    Last modified:August 13, 1987 - v1
    Checksum:iEF8A297E1DF819EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02677 Genomic DNA. Translation: AAA24989.1.
    PIRiA26260. XYHIH1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02677 Genomic DNA. Translation: AAA24989.1 .
    PIRi A26260. XYHIH1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    10MH X-ray 2.55 A 1-327 [» ]
    1FJX X-ray 2.26 A 1-327 [» ]
    1HMY X-ray 2.50 A 1-327 [» ]
    1M0E X-ray 2.50 A 1-327 [» ]
    1MHT X-ray 2.60 A 1-327 [» ]
    1SKM X-ray 2.20 A 1-327 [» ]
    1SVU X-ray 2.66 A/B 1-327 [» ]
    2C7O X-ray 1.90 A 1-327 [» ]
    2C7P X-ray 1.70 A 1-327 [» ]
    2C7Q X-ray 1.85 A 1-327 [» ]
    2C7R X-ray 1.90 A 1-327 [» ]
    2HMY X-ray 2.61 B 1-327 [» ]
    2HR1 X-ray 1.96 A 1-327 [» ]
    2I9K X-ray 2.65 A 1-327 [» ]
    2UYC X-ray 2.00 A 1-327 [» ]
    2UYH X-ray 2.63 A 1-327 [» ]
    2UZ4 X-ray 2.10 A 1-327 [» ]
    2Z6A X-ray 2.88 A 1-327 [» ]
    2Z6Q X-ray 2.79 A 1-327 [» ]
    2Z6U X-ray 2.72 A 1-327 [» ]
    2ZCJ X-ray 2.75 A 1-327 [» ]
    3EEO X-ray 1.94 A 1-327 [» ]
    3MHT X-ray 2.70 A 1-327 [» ]
    4MHT X-ray 2.70 A 1-327 [» ]
    5MHT X-ray 2.70 A 1-327 [» ]
    6MHT X-ray 2.05 A 1-327 [» ]
    7MHT X-ray 2.87 A 1-327 [» ]
    8MHT X-ray 2.76 A 1-327 [» ]
    9MHT X-ray 2.39 A 1-327 [» ]
    ProteinModelPortali P05102.
    SMRi P05102. Positions 1-327.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3421. M.HhaI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P05102.

    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.
    PS00095. C5_MTASE_2. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, in vivo promoter mapping, and expression in Escherichia coli of the gene for the HhaI methyltransferase."
      Caserta M., Zacharias W., Nwankwo D.O., Wilson G.G., Wells R.D.
      J. Biol. Chem. 262:4770-4777(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 10014 / CCUG 3716 / NCTC 8479.
    2. "The DNA binding affinity of HhaI methylase is increased by a single amino acid substitution in the catalytic center."
      Mi S., Roberts R.J.
      Nucleic Acids Res. 21:2459-2464(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    3. "Functional analysis of Gln-237 mutants of HhaI methyltransferase."
      Mi S., Alonso D., Roberts R.J.
      Nucleic Acids Res. 23:620-627(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-237.
    4. "Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine."
      Cheng X., Kumar S., Posfai J., Pflugrath J.W., Roberts R.J.
      Cell 74:299-307(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    5. "HhaI methyltransferase flips its target base out of the DNA helix."
      Klimasauskas S., Kumar S., Roberts R.J., Cheng X.
      Cell 76:357-369(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    6. "DNA containing 4'-thio-2'-deoxycytidine inhibits methylation by HhaI methyltransferase."
      Kumar S., Horton J.R., Jones G.D., Walker R.T., Roberts R.J., Cheng X.
      Nucleic Acids Res. 25:2773-2783(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
    7. "Structures of HhaI methyltransferase complexed with substrates containing mismatches at the target base."
      O'Gara M., Horton J.R., Roberts R.J., Cheng X.
      Nat. Struct. Biol. 5:872-877(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
    8. "Structure of a binary complex of HhaI methyltransferase with S-adenosyl-L-methionine formed in the presence of a short non-specific DNA oligonucleotide."
      O'Gara M., Zhang X., Roberts R.J., Cheng X.
      J. Mol. Biol. 287:201-209(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).

    Entry informationi

    Entry nameiMTH1_HAEPH
    AccessioniPrimary (citable) accession number: P05102
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Strain ATCC 10014 was originally thought to originate from H.haemolyticus.Curated

    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