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P14385 (MTTA_THEAQ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Modification methylase TaqI
Short name=M.TaqI
EC=2.1.1.72
Alternative name(s):
Adenine-specific methyltransferase TaqI
Gene names
Name:taqIM
OrganismThermus aquaticus
Taxonomic identifier271 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

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

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.6 µM for DNA Ref.3

KM=3.7 µM for S-adenosylmethionine

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Modification methylase TaqI
PRO_0000087980

Experimental info

Mutagenesis1081Y → A or G: Drastically reduces enzymatic activity; KM for both DNA and s-adenosylmethionine is not significantly changed. Ref.3
Mutagenesis1081Y → F or W: Essentially wild-type activity. Ref.3
Mutagenesis1961F → A: Drastically reduces enzymatic activity; KM for both DNA and s-adenosylmethionine is not significantly changed. Ref.3
Mutagenesis1961F → W: Essentially wild-type activity. Ref.3
Sequence conflict131S → A in CAA68551. Ref.1
Sequence conflict641A → G in AAA27506. Ref.1

Secondary structure

1 ................................................................................ 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14385 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 21C62B53C43DB7FF

FASTA42147,862
        10         20         30         40         50         60 
MGLPPLLSLP SNSAPRSLGR VETPPEVVDF MVSLAEAPRG GRVLEPACAH GPFLRAFREA 

        70         80         90        100        110        120 
HGTAYRFVGV EIDPKALDLP PWAEGILADF LLWEPGEAFD LILGNPPYGI VGEASKYPIH 

       130        140        150        160        170        180 
VFKAVKDLYK KAFSTWKGKY NLYGAFLEKA VRLLKPGGVL VFVVPATWLV LEDFALLREF 

       190        200        210        220        230        240 
LAREGKTSVY YLGEVFPQKK VSAVVIRFQK SGKGLSLWDT QESESGFTPI LWAEYPHWEG 

       250        260        270        280        290        300 
EIIRFETEET RKLEISGMPL GDLFHIRFAA RSPEFKKHPA VRKEPGPGLV PVLTGRNLKP 

       310        320        330        340        350        360 
GWVDYEKNHS GLWMPKERAK ELRDFYATPH LVVAHTKGTR VVAAWDERAY PWREEFHLLP 

       370        380        390        400        410        420 
KEGVRLDPSS LVQWLNSEAM QKHVRTLYRD FVPHLTLRML ERLPVRREYG FHTSPESARN 


F

« Hide

References

[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 PROPERTIES.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y00499 Genomic DNA. Translation: CAA68551.1. Sequence problems.
M76681 Genomic DNA. Translation: AAA27506.1.
PIRJN0257.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP14385.
SMRP14385. Positions 20-413.
ModBaseSearch...

Protein family/group databases

REBASE3520. M.TaqI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.220.10. 1 hit.
InterProIPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR021188. N6_DNA_MeTrfase_TaqI.
IPR023135. N6_DNA_MeTrfase_TaqI_C.
IPR025931. TaqI_C.
[Graphical view]
PfamPF12950. TaqI_C. 1 hit.
[Graphical view]
PIRSFPIRSF037236. Ade-sp_methyltransferase_TaqI. 1 hit.
PRINTSPR00507. N12N6MTFRASE.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14385.

Entry information

Entry nameMTTA_THEAQ
AccessionPrimary (citable) accession number: P14385
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 17, 2006
Last modified: April 3, 2013
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents