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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 + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.

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.

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi108Y → A or G: Drastically reduces enzymatic activity; KM for both DNA and s-adenosylmethionine is not significantly changed. 1 Publication1
    Mutagenesisi108Y → F or W: Essentially wild-type activity. 1 Publication1
    Mutagenesisi196F → A: Drastically reduces enzymatic activity; KM for both DNA and s-adenosylmethionine is not significantly changed. 1 Publication1
    Mutagenesisi196F → W: Essentially wild-type activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000879801 – 421Modification methylase TaqIAdd BLAST421

    Interactioni

    Protein-protein interaction databases

    STRINGi498848.TaqDRAFT_3765.

    Structurei

    Secondary structure

    1421
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi25 – 34Combined sources10
    Beta strandi42 – 46Combined sources5
    Helixi52 – 61Combined sources10
    Beta strandi65 – 72Combined sources8
    Turni74 – 76Combined sources3
    Beta strandi83 – 88Combined sources6
    Helixi90 – 92Combined sources3
    Beta strandi99 – 104Combined sources6
    Turni114 – 116Combined sources3
    Helixi123 – 132Combined sources10
    Helixi142 – 153Combined sources12
    Beta strandi154 – 165Combined sources12
    Helixi166 – 169Combined sources4
    Helixi172 – 174Combined sources3
    Helixi175 – 184Combined sources10
    Beta strandi185 – 194Combined sources10
    Beta strandi196 – 198Combined sources3
    Beta strandi203 – 212Combined sources10
    Beta strandi215 – 223Combined sources9
    Beta strandi226 – 235Combined sources10
    Helixi248 – 255Combined sources8
    Beta strandi257 – 259Combined sources3
    Helixi260 – 263Combined sources4
    Beta strandi264 – 268Combined sources5
    Helixi272 – 277Combined sources6
    Beta strandi282 – 284Combined sources3
    Beta strandi289 – 291Combined sources3
    Helixi295 – 297Combined sources3
    Beta strandi309 – 311Combined sources3
    Beta strandi313 – 315Combined sources3
    Helixi316 – 321Combined sources6
    Helixi324 – 327Combined sources4
    Beta strandi330 – 333Combined sources4
    Beta strandi335 – 340Combined sources6
    Beta strandi343 – 348Combined sources6
    Beta strandi352 – 360Combined sources9
    Beta strandi364 – 366Combined sources3
    Helixi368 – 375Combined sources8
    Helixi378 – 388Combined sources11
    Beta strandi391 – 394Combined sources4
    Helixi397 – 400Combined sources4
    Beta strandi404 – 406Combined sources3
    Turni407 – 409Combined sources3
    Beta strandi410 – 412Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14385.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4105XEZ. Bacteria.
    COG0827. LUCA.

    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.
    IPR011639. RM_methylase_Eco57I.
    IPR029063. SAM-dependent_MTases.
    IPR025931. TaqI_C.
    [Graphical view]
    PfamiPF07669. Eco57I. 1 hit.
    PF12950. 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)DescriptionActionsGraphical viewLength
    Sequence conflicti13S → A in CAA68551 (PubMed:2827113).Curated1
    Sequence conflicti64A → G in AAA27506 (PubMed:2827113).Curated1

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi498848.TaqDRAFT_3765.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG4105XEZ. Bacteria.
    COG0827. LUCA.

    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.
    IPR011639. RM_methylase_Eco57I.
    IPR029063. SAM-dependent_MTases.
    IPR025931. TaqI_C.
    [Graphical view]
    PfamiPF07669. Eco57I. 1 hit.
    PF12950. 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...

    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: November 2, 2016
    This is version 109 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

    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 one 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.