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Protein

Modification methylase TaqI

Gene

taqIM

Organism
Thermus aquaticus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Kineticsi

  1. KM=0.6 µM for DNA1 Publication
  2. KM=3.7 µM for S-adenosylmethionine1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Restriction system

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.72. 6334.

    Protein family/group databases

    REBASEi3520. M.TaqI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase TaqI (EC:2.1.1.72)
    Short name:
    M.TaqI
    Alternative name(s):
    Adenine-specific methyltransferase TaqI
    Gene namesi
    Name:taqIM
    OrganismiThermus aquaticus
    Taxonomic identifieri271 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi108 – 1081Y → A or G: Drastically reduces enzymatic activity; KM for both DNA and s-adenosylmethionine is not significantly changed. 1 Publication
    Mutagenesisi108 – 1081Y → F or W: Essentially wild-type activity. 1 Publication
    Mutagenesisi196 – 1961F → A: Drastically reduces enzymatic activity; KM for both DNA and s-adenosylmethionine is not significantly changed. 1 Publication
    Mutagenesisi196 – 1961F → W: Essentially wild-type activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 421421Modification methylase TaqIPRO_0000087980Add
    BLAST

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 3410Combined sources
    Beta strandi42 – 465Combined sources
    Helixi52 – 6110Combined sources
    Beta strandi65 – 728Combined sources
    Turni74 – 763Combined sources
    Beta strandi83 – 886Combined sources
    Helixi90 – 923Combined sources
    Beta strandi99 – 1046Combined sources
    Turni114 – 1163Combined sources
    Helixi123 – 13210Combined sources
    Helixi142 – 15312Combined sources
    Beta strandi154 – 16512Combined sources
    Helixi166 – 1694Combined sources
    Helixi172 – 1743Combined sources
    Helixi175 – 18410Combined sources
    Beta strandi185 – 19410Combined sources
    Beta strandi196 – 1983Combined sources
    Beta strandi203 – 21210Combined sources
    Beta strandi215 – 2239Combined sources
    Beta strandi226 – 23510Combined sources
    Helixi248 – 2558Combined sources
    Beta strandi257 – 2593Combined sources
    Helixi260 – 2634Combined sources
    Beta strandi264 – 2685Combined sources
    Helixi272 – 2776Combined sources
    Beta strandi282 – 2843Combined sources
    Beta strandi289 – 2913Combined sources
    Helixi295 – 2973Combined sources
    Beta strandi309 – 3113Combined sources
    Beta strandi313 – 3153Combined sources
    Helixi316 – 3216Combined sources
    Helixi324 – 3274Combined sources
    Beta strandi330 – 3334Combined sources
    Beta strandi335 – 3406Combined sources
    Beta strandi343 – 3486Combined sources
    Beta strandi352 – 3609Combined sources
    Beta strandi364 – 3663Combined sources
    Helixi368 – 3758Combined sources
    Helixi378 – 38811Combined sources
    Beta strandi391 – 3944Combined sources
    Helixi397 – 4004Combined sources
    Beta strandi404 – 4063Combined sources
    Turni407 – 4093Combined sources
    Beta strandi410 – 4123Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQIX-ray2.60A/B1-421[»]
    1AQJX-ray2.60A/B1-421[»]
    1G38X-ray2.00A/D21-413[»]
    2ADMX-ray2.60A/B1-421[»]
    2IBSX-ray2.40A/D1-421[»]
    2IBTX-ray1.70A/D1-421[»]
    2IH2X-ray1.61A/D1-421[»]
    2IH4X-ray2.10A/D1-421[»]
    2IH5X-ray1.80A1-421[»]
    2JG3X-ray1.90A/D1-421[»]
    2NP6X-ray2.10A/D1-421[»]
    2NP7X-ray1.90A1-421[»]
    ProteinModelPortaliP14385.
    SMRiP14385. Positions 20-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14385.

    Family & Domainsi

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    3.90.220.10. 1 hit.
    InterProiIPR002052. DNA_methylase_N6_adenine_CS.
    IPR021188. N6_DNA_MeTrfase_TaqI.
    IPR023135. N6_DNA_MeTrfase_TaqI_C.
    IPR029063. SAM-dependent_MTases.
    IPR025931. TaqI_C.
    [Graphical view]
    PfamiPF12950. TaqI_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037236. Ade-sp_methyltransferase_TaqI. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14385-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGLPPLLSLP SNSAPRSLGR VETPPEVVDF MVSLAEAPRG GRVLEPACAH
    60 70 80 90 100
    GPFLRAFREA HGTAYRFVGV EIDPKALDLP PWAEGILADF LLWEPGEAFD
    110 120 130 140 150
    LILGNPPYGI VGEASKYPIH VFKAVKDLYK KAFSTWKGKY NLYGAFLEKA
    160 170 180 190 200
    VRLLKPGGVL VFVVPATWLV LEDFALLREF LAREGKTSVY YLGEVFPQKK
    210 220 230 240 250
    VSAVVIRFQK SGKGLSLWDT QESESGFTPI LWAEYPHWEG EIIRFETEET
    260 270 280 290 300
    RKLEISGMPL GDLFHIRFAA RSPEFKKHPA VRKEPGPGLV PVLTGRNLKP
    310 320 330 340 350
    GWVDYEKNHS GLWMPKERAK ELRDFYATPH LVVAHTKGTR VVAAWDERAY
    360 370 380 390 400
    PWREEFHLLP KEGVRLDPSS LVQWLNSEAM QKHVRTLYRD FVPHLTLRML
    410 420
    ERLPVRREYG FHTSPESARN F
    Length:421
    Mass (Da):47,862
    Last modified:October 17, 2006 - v3
    Checksum:i21C62B53C43DB7FF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131S → A in CAA68551 (PubMed:2827113).Curated
    Sequence conflicti64 – 641A → G in AAA27506 (PubMed:2827113).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y00499 Genomic DNA. Translation: CAA68551.1. Sequence problems.
    M76681 Genomic DNA. Translation: AAA27506.1.
    PIRiJN0257.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y00499 Genomic DNA. Translation: CAA68551.1. Sequence problems.
    M76681 Genomic DNA. Translation: AAA27506.1.
    PIRiJN0257.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQIX-ray2.60A/B1-421[»]
    1AQJX-ray2.60A/B1-421[»]
    1G38X-ray2.00A/D21-413[»]
    2ADMX-ray2.60A/B1-421[»]
    2IBSX-ray2.40A/D1-421[»]
    2IBTX-ray1.70A/D1-421[»]
    2IH2X-ray1.61A/D1-421[»]
    2IH4X-ray2.10A/D1-421[»]
    2IH5X-ray1.80A1-421[»]
    2JG3X-ray1.90A/D1-421[»]
    2NP6X-ray2.10A/D1-421[»]
    2NP7X-ray1.90A1-421[»]
    ProteinModelPortaliP14385.
    SMRiP14385. Positions 20-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    REBASEi3520. M.TaqI.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi2.1.1.72. 6334.

    Miscellaneous databases

    EvolutionaryTraceiP14385.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    3.90.220.10. 1 hit.
    InterProiIPR002052. DNA_methylase_N6_adenine_CS.
    IPR021188. N6_DNA_MeTrfase_TaqI.
    IPR023135. N6_DNA_MeTrfase_TaqI_C.
    IPR029063. SAM-dependent_MTases.
    IPR025931. TaqI_C.
    [Graphical view]
    PfamiPF12950. TaqI_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037236. Ade-sp_methyltransferase_TaqI. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Cloning, sequencing and expression of the Taq I restriction-modification system."
      Slatko B.E., Benner J.S., Moran L.S., Jager-Quinton T., Simcox T.G., van Cott E.M., Wilson G.G.
      Nucleic Acids Res. 15:9781-9796(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: YT1.
    2. "The corrected nucleotide sequences of the TaqI restriction and modification enzymes reveal a thirteen-codon overlap."
      Barany F., Slatko B., Danzitz M., Cowburn D., Schildkraut I., Wilson G.G.
      Gene 112:91-95(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
      Strain: YT1.
    3. "Functional roles of the conserved aromatic amino acid residues at position 108 (motif IV) and position 196 (motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus."
      Pues H., Bleimling N., Holz B., Wolcke J., Weinhold E.
      Biochemistry 38:1426-1434(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-108 AND PHE-196, KINETIC PARAMETERS.
    4. "Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine."
      Labahn J., Granzin J., Schluckebier G., Robinson D.P., Jack W.E., Schildkraut I., Saenger W.
      Proc. Natl. Acad. Sci. U.S.A. 91:10957-10961(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH S-ADENOSYLMETHIONINE.
    5. "Differential binding of S-adenosylmethionine S-adenosylhomocysteine and sinefungin to the adenine-specific DNA methyltransferase M.TaqI."
      Schluckebier G., Kozak M., Bleimling N., Weinhold E., Saenger W.
      J. Mol. Biol. 265:56-67(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH S-ADENOSYLHOMOCYSTEINE AND SINEFUNGIN, A REINTERPRETATION IN COMPLEX WITH S-ADENOSYLMETHIONINE.
    6. "Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog."
      Goedecke K., Pignot M., Goody R.S., Scheidig A.J., Weinhold E.
      Nat. Struct. Biol. 8:121-125(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-413 IN COMPLEX WITH DNA, DISCUSSION OF ENZYME MECHANISM.

    Entry informationi

    Entry nameiMTTA_THEAQ
    AccessioniPrimary (citable) accession number: P14385
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 17, 2006
    Last modified: April 29, 2015
    This is version 101 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

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.