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P14385

- MTTA_THEAQ

UniProt

P14385 - MTTA_THEAQ

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Protein

Modification methylase TaqI

Gene

taqIM

Organism
Thermus aquaticus
Status
Reviewed - 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 + 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
Complete GO annotation...

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

        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)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