Modification methylase TaqI

Details

Name
Modification methylase TaqI
Synonyms
  • 2.1.1.72
  • Adenine-specific methyltransferase TaqI
  • M.TaqI
Gene Name
taqIM
Organism
Thermus aquaticus
Amino acid sequence
>lcl|BSEQ0016815|Modification methylase TaqI
MGLPPLLSLPSNSAPRSLGRVETPPEVVDFMVSLAEAPRGGRVLEPACAHGPFLRAFREA
HGTAYRFVGVEIDPKALDLPPWAEGILADFLLWEPGEAFDLILGNPPYGIVGEASKYPIH
VFKAVKDLYKKAFSTWKGKYNLYGAFLEKAVRLLKPGGVLVFVVPATWLVLEDFALLREF
LAREGKTSVYYLGEVFPQKKVSAVVIRFQKSGKGLSLWDTQESESGFTPILWAEYPHWEG
EIIRFETEETRKLEISGMPLGDLFHIRFAARSPEFKKHPAVRKEPGPGLVPVLTGRNLKP
GWVDYEKNHSGLWMPKERAKELRDFYATPHLVVAHTKGTRVVAAWDERAYPWREEFHLLP
KEGVRLDPSSLVQWLNSEAMQKHVRTLYRDFVPHLTLRMLERLPVRREYGFHTSPESARN
F
Number of residues
421
Molecular Weight
47861.91
Theoretical pI
9.39
GO Classification
Functions
nucleic acid binding / site-specific DNA-methyltransferase (adenine-specific) activity
Processes
DNA restriction-modification system
General Function
Site-specific dna-methyltransferase (adenine-specific) activity
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0004970|1266 bp
ATGGGCCTGCCACCCCTTCTGTCCTTACCTTCCAACTCCGCCCCCAGGAGCCTGGGCCGG
GTGGAGACCCCCCCGGAGGTGGTGGACTTCATGGTCTCCCTGGCCGAGGCGCCCAGGGGG
GGAAGGGTGCTGGAGCCCGCCTGCGCCCATGGGCCCTTCCTCCGGGCTTTCCGGGAGGCC
CACGGGACGGGCTACCGCTTCGTGGGGGTGGAGATAGACCCAAAAGCCCTGGACCTCCCC
CCCTGGGCCGAGGGCATCCTGGCGGACTTCCTCCTCTGGGAGCCGGGGGAGGCCTTTGAC
CTGATCCTGGGCAATCCGCCTTACGGCATCGTAGGAGAAGCCAGCAAATACCCCATTCAC
GTCTTCAAAGCGGTCAAGGACCTCTACAAGAAGGCCTTTTCCACCTGGAAGGGCAAGTAC
AACTTGTACGGGGCCTTTCTTGAAAAGGCCGTTCGCCTTCTTAAGCCTGGTGGGGTCCTC
GTCTTTGTAGTCCCGGCCACCTGGCTTGTCCTGGAGGATTTTGCCCTCCTTCGCGAGTTC
CTTGCCCGGGAAGGGAAAACATCTGTATACTACCTTGGCGAGGTTTTCCCGCAAAAAAAG
GTTAGCGCTGTAGTGATTCGCTTCCAGAAGAGCGGAAAAGGCCTTTCACTTTGGGATACC
CAAGAAAGCGAAAGCGGGTTCACGCCCATCCTCTGGGCTGAATATCCACATTGGGAAGGA
GAGATTATCCGCTTTGAAACAGAGGAGACGCGGAAGCTGGAAATATCGGGAATGCCACTG
GGAGACCTCTTTCATATCCGCTTCGCCGCAAGAAGCCCTGAATTCAAGAAACATCCAGCA
GTGAGAAAGGAACCGGGGCCAGGTCTTGTGCCTGTGCTCACAGGAAGAAATTTAAAGCCG
GGGTGGGTAGATTACGAGAAAAACCACTCCGGGCTTTGGATGCCCAAGGAAAGGGCCAAG
GAGCTCAGGGACTTCTATGCCACGCCCCACCTGGTGGTAGCCCACACCAAGGGGACTAGA
GTGGTGGCCGCTTGGGACGAAAGGGCCTACCCCTGGCGGGAGGAGTTCCACCTCCTGCCC
AAGGAAGGTGTGAGACTGGACCCCTCGTCCCTGGTGCAGTGGTTAAACTCCGAAGCGATG
CAGAAGCACGTCAGGACGCTTTATCGCGACTTCGTGCCCCACCTGACGCTGAGGATGCTA
GAAAGGCTTCCTGTAAGGAGGGAATATGGCTTCCACACAAGCCCAGAAAGCGCTCGAAAC
TTTTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP14385
UniProtKB Entry NameMTTA_THEAQ
GenBank Gene IDM76681
General References
  1. Slatko BE, Benner JS, Jager-Quinton T, Moran LS, Simcox TG, Van Cott EM, Wilson GG: Cloning, sequencing and expression of the Taq I restriction-modification system. Nucleic Acids Res. 1987 Dec 10;15(23):9781-96. [PubMed:2827113]
  2. Barany F, Slatko B, Danzitz M, Cowburn D, Schildkraut I, Wilson GG: The corrected nucleotide sequences of the TaqI restriction and modification enzymes reveal a thirteen-codon overlap. Gene. 1992 Mar 1;112(1):91-5. [PubMed:1551602]
  3. Pues H, Bleimling N, Holz B, Wolcke J, Weinhold E: 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. Biochemistry. 1999 Feb 2;38(5):1426-34. [PubMed:9931007]
  4. Labahn J, Granzin J, Schluckebier G, Robinson DP, Jack WE, Schildkraut I, Saenger W: Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine. Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10957-61. [PubMed:7971991]
  5. Schluckebier G, Kozak M, Bleimling N, Weinhold E, Saenger W: Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI. J Mol Biol. 1997 Jan 10;265(1):56-67. [PubMed:8995524]
  6. Goedecke K, Pignot M, Goody RS, Scheidig AJ, Weinhold E: Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog. Nat Struct Biol. 2001 Feb;8(2):121-5. [PubMed:11175899]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01752S-adenosyl-L-homocysteineexperimentalunknownDetails
DB01910SinefunginexperimentalunknownDetails