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P14385

- MTTA_THEAQ

UniProt

P14385 - MTTA_THEAQ

Protein

Modification methylase TaqI

Gene

taqIM

Organism
Thermus aquaticus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    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

    1. nucleic acid binding Source: InterPro
    2. 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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    IPR002296. N12N6_MeTrfase.
    IPR021188. N6_DNA_MeTrfase_TaqI.
    IPR023135. N6_DNA_MeTrfase_TaqI_C.
    IPR029063. SAM-dependent_MTases-like.
    IPR025931. TaqI_C.
    [Graphical view]
    PfamiPF12950. TaqI_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037236. Ade-sp_methyltransferase_TaqI. 1 hit.
    PRINTSiPR00507. N12N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14385-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLPPLLSLP SNSAPRSLGR VETPPEVVDF MVSLAEAPRG GRVLEPACAH    50
    GPFLRAFREA HGTAYRFVGV EIDPKALDLP PWAEGILADF LLWEPGEAFD 100
    LILGNPPYGI VGEASKYPIH VFKAVKDLYK KAFSTWKGKY NLYGAFLEKA 150
    VRLLKPGGVL VFVVPATWLV LEDFALLREF LAREGKTSVY YLGEVFPQKK 200
    VSAVVIRFQK SGKGLSLWDT QESESGFTPI LWAEYPHWEG EIIRFETEET 250
    RKLEISGMPL GDLFHIRFAA RSPEFKKHPA VRKEPGPGLV PVLTGRNLKP 300
    GWVDYEKNHS GLWMPKERAK ELRDFYATPH LVVAHTKGTR VVAAWDERAY 350
    PWREEFHLLP KEGVRLDPSS LVQWLNSEAM QKHVRTLYRD FVPHLTLRML 400
    ERLPVRREYG FHTSPESARN F 421
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00499 Genomic DNA. Translation: CAA68551.1 . Sequence problems.
    M76681 Genomic DNA. Translation: AAA27506.1 .
    PIRi JN0257.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AQI X-ray 2.60 A/B 1-421 [» ]
    1AQJ X-ray 2.60 A/B 1-421 [» ]
    1G38 X-ray 2.00 A/D 21-413 [» ]
    2ADM X-ray 2.60 A/B 1-421 [» ]
    2IBS X-ray 2.40 A/D 1-421 [» ]
    2IBT X-ray 1.70 A/D 1-421 [» ]
    2IH2 X-ray 1.61 A/D 1-421 [» ]
    2IH4 X-ray 2.10 A/D 1-421 [» ]
    2IH5 X-ray 1.80 A 1-421 [» ]
    2JG3 X-ray 1.90 A/D 1-421 [» ]
    2NP6 X-ray 2.10 A/D 1-421 [» ]
    2NP7 X-ray 1.90 A 1-421 [» ]
    ProteinModelPortali P14385.
    SMRi P14385. Positions 20-413.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3520. M.TaqI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P14385.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    3.90.220.10. 1 hit.
    InterProi IPR002052. DNA_methylase_N6_adenine_CS.
    IPR002296. N12N6_MeTrfase.
    IPR021188. N6_DNA_MeTrfase_TaqI.
    IPR023135. N6_DNA_MeTrfase_TaqI_C.
    IPR029063. SAM-dependent_MTases-like.
    IPR025931. TaqI_C.
    [Graphical view ]
    Pfami PF12950. TaqI_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037236. Ade-sp_methyltransferase_TaqI. 1 hit.
    PRINTSi PR00507. N12N6MTFRASE.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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 AND A COFACTOR ANALOG, 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: October 1, 2014
    This is version 96 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