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
- Functionsnucleic acid binding / site-specific DNA-methyltransferase (adenine-specific) activityProcessesDNA 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
- TaqI_C (PF12950)
- 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
Resource Link UniProtKB ID P14385 UniProtKB Entry Name MTTA_THEAQ GenBank Gene ID M76681 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]