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S-adenosyl-L-methionine + 7Me-GpppA-C5
S-adenosyl-L-homocysteine + 7Me-GpppA-2'OMe-C5
S-adenosyl-L-methionine + 7Me-GpppA-Cn
S-adenosyl-L-homocysteine + 7Me-GpppA-2'OMe-Cn
-
exclusive methylation at the 2'O position
-
-
?
S-adenosyl-L-methionine + 7Me-GpppG
S-adenosyl-L-homocysteine + 7Me-Gppp-2'OMe-G
-
-
-
?
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA]
S-adenosyl-L-methionine + ApppGR-RNA
?
S-adenosyl-L-methionine + brome mosaic virus RNA
?
-
-
-
-
r
S-adenosyl-L-methionine + G(5')pppA-poly(A)
S-adenosyl-L-homocysteine + G(5')pppA-2'-OMe-poly(A)
-
-
-
-
r
S-adenosyl-L-methionine + GpppA-Cn
S-adenosyl-L-homocysteine + GpppA-2'OMe-Cn
-
exclusive methylation at the 2'O position
-
-
?
S-adenosyl-L-methionine + GpppACCCCC
S-adenosyl-L-homocysteine + GpppAmCCCCC
-
-
?
S-adenosyl-L-methionine + m7G(5')pppA-poly(A)
S-adenosyl-L-homocysteine + m7G(5')pppA-2'-OMe-poly(A)
-
-
-
-
r
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppAm-RNA
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRA-RNA
S-adenosyl-L-methionine + m7G(5')pppG-RNA
S-adenosyl-L-homocysteine + m7G(5')pppGm-RNA
S-adenosyl-L-methionine + m7G(5')pppN-RNA
S-adenosyl-L-homocysteine + m7G(5')pppNm-RNA
-
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppNmpN-RNA
S-adenosyl-L-homocysteine + m7G(5')pppNmpNm-RNA
-
N: purin and pyrimidine nucleotides are methylated, enzyme: cap II-methyltransferase
i.e. cap II
?
S-adenosyl-L-methionine + m7G(5')pppNpN-RNA
S-adenosyl-L-homocysteine + m7G(5')pppNmpN-RNA
-
i.e. cap O, N: purine and pyrimidine nucleotides are methylated, enzyme: cap I-methyltransferase, substrates are RNAs with a capped terminus with at least 2 additional nucleotides, G(5')pppNpNp
i.e. cap I
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
S-adenosyl-L-methionine + m7G-(5')pppGpApApA
?
-
-
-
?
S-adenosyl-L-methionine + m7GpppACCCCC
S-adenosyl-L-homocysteine + m7GpppAmCCCCC
-
-
?
S-adenosyl-L-methionine + m7GpppApGp
S-adenosyl-L-homocysteine + m7GpppAmpGp
-
i.e. capped dinucleotide, cap I-methyltransferase
-
?
S-adenosyl-L-methionine + m7GpppApGpUp
S-adenosyl-L-homocysteine + m7GpppAmpGpUp
-
i.e. capped trinucleotide, cap I-methyltransferase
-
?
S-adenosyl-L-methionine + m7GpppG
S-adenosyl-L-homocysteine + m7GpppGm
-
-
-
?
S-adenosyl-L-methionine + m7GpppGp
S-adenosyl-L-homocysteine + m7GpppGmp
-
substrate of minimal chain length for the cap-specific enzyme, m7GpppG is no substrate
-
-
?
S-adenosyl-L-methionine + m7GpppGpN
S-adenosyl-L-homocysteine + m7GpppGmpN
-
-
-
-
?
S-adenosyl-L-methionine + m7GpppGpNp
?
-
-
-
-
?
S-adenosyl-L-methionine + m7GpppGpUbiotin-p
?
-
-
-
-
?
S-adenosyl-L-methionine + mononucleotide
?
-
such as m7GpppA or GpppA, poor substrates for cap I-methyltransferase
-
-
?
S-adenosyl-L-methionine + RNA chain length 2-6 nt
?
-
-
-
-
r
S-adenosyl-L-methionine + RNA chain length 20-50 nt
?
-
-
-
-
r
additional information
?
-
S-adenosyl-L-methionine + 7Me-GpppA-C5
S-adenosyl-L-homocysteine + 7Me-GpppA-2'OMe-C5
-
exclusive methylation at the 2'O position
-
-
?
S-adenosyl-L-methionine + 7Me-GpppA-C5
S-adenosyl-L-homocysteine + 7Me-GpppA-2'OMe-C5
-
-
-
-
?
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA]
-
-
-
-
?
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA]
-
-
-
?
S-adenosyl-L-methionine + ApppGR-RNA
?
-
adenine-capped RNA, wild-type and mutants, indicating the redundancy of m7G-contact residues able to confer cap-type specificity
-
-
?
S-adenosyl-L-methionine + ApppGR-RNA
?
-
synthetic substrate with unusual cap structure, 20% activity compared to m7G-terminated substrates
-
-
?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppAm-RNA
-
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppAm-RNA
-
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppAm-RNA
-
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRA-RNA
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRA-RNA
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppG-RNA
S-adenosyl-L-homocysteine + m7G(5')pppGm-RNA
-
m7GTP capped nucleotides 1-110. 2'-O MTase activity is seen only in glycine buffer, at pH 10, with a minimum RNA length of 20 nucleotides needed
-
-
?
S-adenosyl-L-methionine + m7G(5')pppG-RNA
S-adenosyl-L-homocysteine + m7G(5')pppGm-RNA
-
cap1 formation is optimal at 0.005 mM S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
His-tagged N-terminal part of NS5 protein, termed NS5MTaseDV, amino acids 1-296, utilizes methylated and unmethylated capped RNA, but not uncapped RNA
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
satellite tobacco necrosis virus
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
best substrates are poly(A)-nucleosides and poly-(I)-nucleosides with m7G(5')pppN-ends
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
specific, in vitro methyl group acceptors are polyribonucleosides containing 7-methylguanine(5')pppG-terminals
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
brome mosaic virus RNA ending in m7G(5')pppG as substrate
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
adenine-capped RNA, wild-type and mutants, indicating the redundancy of m7G-contact residues able to confer cap-type specificity
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
poor substrates are m7GpppN-dinucleotides
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
much less active with poly(G), poly(U) and poly(C)
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
methylates 2'-O-position of penultimate nucleoside of RNA, no methylation of internal sites
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
methylates 2'-O-position of penultimate nucleoside of RNA, no methylation of internal sites
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
best substrates are poly(A)-nucleosides and poly-(I)-nucleosides with m7G(5')pppN-ends
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
specific, in vitro methyl group acceptors are polyribonucleosides containing 7-methylguanine(5')pppG-terminals
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
specific, in vitro methyl group acceptors are polyribonucleosides containing 7-methylguanine(5')pppG-terminals
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
brome mosaic virus RNA ending in m7G(5')pppG as substrate
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
brome mosaic virus RNA ending in m7G(5')pppG as substrate
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
RNA-polymerase holoenzyme has methyltransferase activity: the same protein acts as methyltransferase and poly(A)-polymerase stimulatory factor VP39
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
final step in formation of 7-methylguanosine(5')pppNm-cap structure of viral RNA
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
final step in formation of 7-methylguanosine(5')pppNm-cap structure of viral RNA
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
methylates 2'-O-position of penultimate nucleoside of RNA, no methylation of internal sites
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
specific, in vitro methyl group acceptors are polyribonucleosides containing 7-methylguanine(5')pppG-terminals
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
brome mosaic virus RNA ending in m7G(5')pppG as substrate
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
poor substrates are m7GpppN-dinucleotides
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
much less active with poly(G), poly(U) and poly(C)
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
methylates 2'-O-position of penultimate nucleoside of RNA, no methylation of internal sites
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
brome mosaic virus RNA ending in m7G(5')pppG as substrate
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
RNA-polymerase holoenzyme has methyltransferase activity: the same protein acts as methyltransferase and poly(A)-polymerase stimulatory factor VP39
-
-
?
additional information
?
-
-
maximum 2'O-MTase activity requires the cap and at least 6 nucleotides
-
-
?
additional information
?
-
-
the enzyme shows highest activity towards 7Me-GpppA-Cn where n equals at least four, and does not methylate GpppAC5 or pppAC5
-
-
?
additional information
?
-
-
the enzyme catalyzes specific methylation of the 2'-O-ribose of the first nucleotide of a capped RNA transcript
-
-
?
additional information
?
-
the enzyme does not methylate m7G(5')pppG-RNA
-
-
?
additional information
?
-
-
the enzyme does not methylate m7G(5')pppG-RNA
-
-
?
additional information
?
-
the enzyme does not methylate m7G(5')pppG-RNA
-
-
?
additional information
?
-
-
no substrates are RNAs with pN-, ppN-, guanine(5')pppN-terminals
-
-
?
additional information
?
-
-
poly(A) and internal nucleotides of RNA
-
-
?
additional information
?
-
-
poly(A) and internal nucleotides of RNA
-
-
?
additional information
?
-
-
no substrates are RNAs with pN-, ppN-, guanine(5')pppN-terminals
-
-
?
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Acquired Immunodeficiency Syndrome
1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10.
Arteritis
Arterivirus nsp12 versus the coronavirus nsp16 2'-O-methyltransferase: comparison of the C-terminal cleavage products of two nidovirus pp1ab polyproteins.
Asthma
CMTR1 is associated with increased asthma exacerbations in patients taking inhaled corticosteroids.
Carcinoma, Ehrlich Tumor
Isolation and characterization of a nucleolar 2'-O-methyltransferase from Ehrlich ascites tumor cells.
Carcinoma, Ehrlich Tumor
Specificity of a nucleolar 2'-O-methyltransferase for RNA substrates.
Coronavirus Infections
Binding of the Methyl Donor
Coronavirus Infections
Middle East Respiratory Syndrome Coronavirus Nonstructural Protein 16 Is Necessary for Interferon Resistance and Viral Pathogenesis.
COVID-19
Identification of promising drug candidates against NSP16 of SARS-CoV-2 through computational drug repurposing study.
COVID-19
In silico identification of novel SARS-COV-2 2'-O-methyltransferase (nsp16) inhibitors: structure-based virtual screening, molecular dynamics simulation and MM-PBSA approaches.
COVID-19
Potential Drugs Targeting Early Innate Immune Evasion of SARS-Coronavirus 2 via 2'-O-Methylation of Viral RNA.
COVID-19
SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses.
COVID-19
Structural insight into the recognition of S-adenosyl-L-homocysteine and sinefungin in SARS-CoV-2 Nsp16/Nsp10 RNA cap 2'-O-Methyltransferase.
COVID-19
Whole Genome Sequencing of SARS-CoV-2 Strains in COVID-19 Patients From Djibouti Shows Novel Mutations and Clades Replacing Over Time.
Dengue
A structural basis for the inhibition of the NS5 dengue virus mRNA 2'-O-methyltransferase domain by ribavirin 5'-triphosphate.
Dengue
Biochemical characterization of the (nucleoside-2'O)-methyltransferase activity of dengue virus protein NS5 using purified capped RNA oligonucleotides 7MeGpppACn and GpppACn.
Dengue
Characterization of a candidate tetravalent vaccine based on 2'-O-methyltransferase mutants.
Dengue
Correction: Rational Design of a Live Attenuated Dengue Vaccine: 2'-O-Methyltransferase Mutants Are Highly Attenuated and Immunogenic in Mice and Macaques.
Dengue
Designing cyclopentapeptide inhibitor as potential antiviral drug for dengue virus ns5 methyltransferase.
Dengue
Evaluation of Adamantane Derivatives as Inhibitors of Dengue Virus mRNA Cap Methyltransferase by Docking and Molecular Dynamics Simulations.
Dengue
High-yield production of short GpppA- and 7MeGpppA-capped RNAs and HPLC-monitoring of methyltransfer reactions at the guanine-N7 and adenosine-2'O positions.
Dengue
Higher catalytic efficiency of N-7-methylation is responsible for processive N-7 and 2'-O methyltransferase activity in dengue virus.
Dengue
Inhibition of dengue viral infection by diasarone-I is associated with 2'O methyltransferase of NS5.
Dengue
Rational design of a live attenuated dengue vaccine: 2'-o-methyltransferase mutants are highly attenuated and immunogenic in mice and macaques.
Encephalitis, Japanese
Ifit1 Inhibits Japanese Encephalitis Virus Replication through Binding to 5' Capped 2'-O Unmethylated RNA.
Hepatitis
Construction and genetic analysis of murine hepatitis virus strain A59 Nsp16 temperature sensitive mutant and the revertant virus.
Hepatitis
Coronavirus nsp10/nsp16 Methyltransferase Can Be Targeted by nsp10-Derived Peptide In Vitro and In Vivo To Reduce Replication and Pathogenesis.
Infections
Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-o-methyltransferase activity.
Infections
Coronavirus non-structural protein 16: evasion, attenuation, and possible treatments.
Infections
Coronavirus nsp10/nsp16 Methyltransferase Can Be Targeted by nsp10-Derived Peptide In Vitro and In Vivo To Reduce Replication and Pathogenesis.
Influenza, Human
Genome-wide CRISPR screen identifies host dependency factors for influenza A virus infection.
Intellectual Disability
Loss of Ftsj1 perturbs codon-specific translation efficiency in the brain and is associated with X-linked intellectual disability.
Neoplasms
Isolation and characterization of a nucleolar 2'-O-methyltransferase from Ehrlich ascites tumor cells.
Neoplasms
Specificity of a nucleolar 2'-O-methyltransferase for RNA substrates.
Severe Acute Respiratory Syndrome
Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-o-methyltransferase activity.
Severe Acute Respiratory Syndrome
Coronavirus nsp10/nsp16 Methyltransferase Can Be Targeted by nsp10-Derived Peptide In Vitro and In Vivo To Reduce Replication and Pathogenesis.
Severe Acute Respiratory Syndrome
Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2'-O-methyltransferase nsp10/nsp16 complex.
Severe Acute Respiratory Syndrome
Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.
Severe Acute Respiratory Syndrome
Molecular mapping of the RNA Cap 2'-O-methyltransferase activation interface between severe acute respiratory syndrome coronavirus nsp10 and nsp16.
Severe Acute Respiratory Syndrome
Potential Drugs Targeting Early Innate Immune Evasion of SARS-Coronavirus 2 via 2'-O-Methylation of Viral RNA.
Vaccinia
A polyadenylylation-specific RNA-contact site on the surface of the bifunctional vaccinia virus RNA modifying protein VP39 that is distinct from the mRNA 5' end-binding "cleft".
Vaccinia
A protein related to the vaccinia virus cap-specific methyltransferase VP39 is involved in cap 4 modification in Trypanosoma brucei.
Vaccinia
Active site in RrmJ, a heat shock-induced methyltransferase.
Vaccinia
Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2'O)-methyltransferase activity.
Vaccinia
Genetic Analysis of Murine Hepatitis Virus Non-Structural Protein 16.
Vaccinia
Insertion of an N7-methylguanine mRNA cap between two coplanar aromatic residues of a cap-binding protein is fast and selective for a positively charged cap.
Vaccinia
Interaction between the J3R subunit of vaccinia virus poly(A) polymerase and the H4L subunit of the viral RNA polymerase.
Vaccinia
Mechanism of RNA 2'-O-methylation: evidence that the catalytic lysine acts to steer rather than deprotonate the target nucleophile.
Vaccinia
Methyltransferase-specific domains within VP-39, a bifunctional protein that participates in the modification of both mRNA ends.
Vaccinia
Mutational analysis of a multifunctional protein, with mRNA 5' cap-specific (nucleoside-2'-O-)-methyltransferase and 3'-adenylyltransferase stimulatory activities, encoded by vaccinia virus.
Vaccinia
pK(a) of the mRNA Cap-Specific 2'-O-Methyltransferase Catalytic Lysine by HSQC NMR Detection of a Two-Carbon Probe.
Vaccinia
Recognition of capped RNA substrates by VP39, the vaccinia virus-encoded mRNA cap-specific 2'-O-methyltransferase.
Vaccinia
Studying vaccinia virus RNA processing in vitro.
Vaccinia
The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends.
Vaccinia
The vaccinia virus bifunctional gene J3 (nucleoside-2'-O-)-methyltransferase and poly(A) polymerase stimulatory factor is implicated as a positive transcription elongation factor by two genetic approaches.
Vaccinia
Transcription elongation activity of the vaccinia virus J3 protein in vivo is independent of poly(A) polymerase stimulation.
Vesicular Stomatitis
Identification of sendai virus L protein amino acid residues affecting viral mRNA cap methylation.
Vesicular Stomatitis
Sequence-function analysis of the Sendai virus L protein domain VI.
Virus Diseases
Emetine, a potent alkaloid for the treatment of SARS-CoV-2 targeting papain-like protease and non-structural proteins: pharmacokinetics, molecular docking and dynamic studies.
Virus Diseases
Inhibition of dengue viral infection by diasarone-I is associated with 2'O methyltransferase of NS5.
Virus Diseases
The human interferon-regulated ISG95 protein interacts with RNA polymerase II and shows methyltransferase activity.
Virus Diseases
The mRNA Cap 2'-O-Methyltransferase CMTR1 Regulates the Expression of Certain Interferon-Stimulated Genes.
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D265E
complete loss of 2'-O-methylation activity, Bluetongue virus replication in cells is abrogated
D265V
complete loss of 2'-O-methylation activity, Bluetongue virus replication in cells is abrogated
N311A
2fold reduction of 2'-O-methylation activity, Bluetongue virus replication in cells is abrogated
N311A/Y334/R367A
2fold reduction of 2'-O-methylation activity, Bluetongue virus replication in cells is abrogated
R367A
mutation does not affect methyl group transfer
Y334A
mutation does not affect methyl group transfer
D113A
-
about 110% substrate binding and activity compared to the wild type enzyme
D129A
-
about 40% substrate binding and activity compared to the wild type enzyme
D221A
-
about 115% substrate binding and activity compared to the wild type enzyme
D247A
-
about 75% substrate binding and activity compared to the wild type enzyme
E202A
-
about 30% substrate binding and activity compared to the wild type enzyme
F173A
-
about 20% substrate binding and activity compared to the wild type enzyme
K169A
-
about 20% substrate binding and activity compared to the wild type enzyme
K45A
-
about 1% substrate binding and activity compared to the wild type enzyme
W4A
-
about 90% substrate binding and activity compared to the wild type enzyme
Y14A
-
about 10% substrate binding and activity compared to the wild type enzyme
Y29A
-
about 15% substrate binding and activity compared to the wild type enzyme
D141A
-
RNA synthesis is severely impaired in this mutant
DELTA2-35
-
RNA synthesis is severely impaired in this mutant
H93A
-
RNA synthesis is severely impaired in this mutant
R100A
-
RNA synthesis is severely impaired in this mutant
W215A
-
the mutant shows reduced RNA synthesis activity compared to the wild type
K239A
-
the mutant shows no activity
D106A
-
the mutant shows 38% of wild type activity
D130A
-
the mutant shows 2% of wild type activity
G73A
-
the mutant shows 18% of wild type activity
G94A
-
the nsp10 mutation binds nsp16 with a slightly reduced affinity (60%) but is still able to stimulate nsp16 2'O-MTase activity
G94D
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
I40A
-
the mutant shows 8% of wild type activity
K46A
-
the mutant shows 1% of wild type activity
K93E
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
K95A
-
the nsp10 mutation binds nsp16 with a slightly reduced affinity (80%) but is still able to stimulate nsp16 2'O-MTase activity
M41A
-
the mutant shows 4% of wild type activity
M44A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
N43A
-
the mutant shows 11% of wild type activity
Q87A
-
the mutant shows 62% of wild type activity
R78A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
R78G
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
S188A
-
the substitution shows 72% loss of activity with no significant effect on the stability of the nsp10/nsp16 complex
S72A
-
the mutant protein binds nsp16 but weakly activates 2'O-MTase activity
T48A
-
the mutant shows 20% of wild type activity
T54E
-
the substitution shows 72% loss of activity with no significant effect on the stability of the nsp10/nsp16 complex
T58A
-
the substitution shows 43% loss of activity with no significant effect on the stability of the nsp10/nsp16 complex
T58E
-
the substitution shows 99% loss of activity with 54% association of the Nsp10/nsp16 complex compared to the wild type
T58N
-
the substitution shows 70% loss of activity with no significant effect on the stability of the nsp10/nsp16 complex
V104G
-
the mutant shows 4% of wild type activity
V42A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
V44A
-
the mutant shows 1% of wild type activity
Y132A
-
the mutant shows 5% of wild type activity
Y132F
-
the mutant shows 9% of wild type activity
Y132T
-
the mutant shows 5% of wild type activity
Y30A
-
the mutant shows 1% of wild type activity
Y30F
-
the mutant shows 6% of wild type activity
Y96I
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
Y96V
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
G70A
-
the mutant shows reduced activity compared to the wild type
-
K93A
-
the mutant shows reduced activity compared to the wild type
-
Y76A/C77A/R78A
-
inactive
-
K266A
proteins similar to that of the wild-type TbMT57-HA protein, defective in the biogenesis of the SL cap 4 structure
C178S
-
point mutations, glutathione-S-transferase-tagged, exchange shows no effect
C272S
-
point mutations, glutathione-S-transferase-tagged, exchange shows no effect
C272S/K175C/R209K
2-bromoethylamine reveals 64% target site modification in a overnight reaction at 37°C, unmodified mutant has no detectable methyltransferase activity, whereas the modified protein is active, exhibiting 20-30% of the specific catalytic rate of wild-type
D182A
-
m7G binding pocket mutant, mutagenesis, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
D182A/E233A
-
m7G binding pocket double mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
E233A
-
m7G binding pocket mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
F180A
-
m7G binding pocket mutant, mutagenesis, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
F180W
-
no apparent defects in catalytic activity
K175C
aziridine reveals 66.7% target site modification in a 4 h, room temperature reaction, equivalent modification level achieved in an overnight incubation using 2-bromoethylamine at 37°C, but protein losses due to aggregation during the modification reaction are, notably, negligible in the lower temperature/shorter duration reactions employed for aziridine
Y22A
-
m7G binding pocket mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
D1762A
-
with pinpoint plaque morphologies and replication defects in single-step growth assays, viral RNA and protein synthesis is diminished
E1674A
-
the mutation in the V1 region of L protein abolishes 2'-O methylation activity
E1674D
-
the mutation in the V1 region of L protein shows severely reduced 2'-O methylation activity (about 20%) compared to the wild type
E1674K
-
the mutation in the V1 region of L protein shows severely reduced 2'-O methylation activity (about 15%) compared to the wild type
E1674Q
-
the mutation in the V1 region of L protein shows severely reduced 2'-O methylation activity (about 15%) compared to the wild type
E1833A
-
with pinpoint plaque morphologies and most significant replication defects in single-step growth assays, viral RNA and protein synthesis is diminished
E1833Q
-
delay in replication
F1691A
-
the mutation in the V1 region of L protein abolishes 2'-O methylation activity
F1691W
-
the mutation in the V1 region of L protein shows slightly reduced 2'-O methylation activity (about 78%) compared to the wild type
F1691Y
-
the mutation in the V1 region of L protein shows slightly reduced 2'-O methylation activity (about 80%) compared to the wild type
G1674A
-
does not significantly perturb viral growth and gene expression, replicates with almost indistinguishable kinetics to recombinant vesicular stomatitis virus
K1651A
-
with pinpoint plaque morphologies and most significant replication defects in single-step growth assays, viral RNA and protein synthesis is diminished
Y1650A
-
the mutation in the V1 region of L protein abolishes 2'-O methylation activity
Y1650F
-
the mutation in the V1 region of L protein shows slightly reduced 2'-O methylation activity (about 85%) compared to the wild type
Y1650W
-
the mutation in the V1 region of L protein shows slightly reduced 2'-O methylation activity (about 90%) compared to the wild type
E218A
-
the mutation abolishes 2'-O-methyltransferase activity and enhances replication but not virulence in Ifit1-deficient mice after peripheral infection
G70A
the mutant shows reduced activity compared to the wild type
G70A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
K93A
the mutant shows reduced activity compared to the wild type
K93A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
Y96A
-
the mutation abrogates nsp10/nsp16 interaction with enzyme activity
Y96A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
Y96F
-
the mutation increases both nsp10/nsp16 interaction with MTase activity and enzyme activity
Y96F
-
the nsp10 mutation overstimulates nsp16 enzyme activity
G96D
-
mutation in J3 protein with nucleoside-2-O'-methyltransferase activity evokes a phenotype with abnormally long RNA transcripts analogously to A18 gene-mutation Cts23
G96D
-
double mutant G96D plus Cts23 mutation in gene A18 shows that the J3-mutants serves as an extragenic suppressor of A18-Cts23 mutant
K1795A
-
most significant defect in replication
K1795A
-
with pinpoint plaque morphologies and replication defects in single-step growth assays, viral RNA and protein synthesis is diminished
additional information
trans-splicing utilization of the SL RNA is not detectably affected in mt57-/- cells, SS1 proteins similar to that of the wild-type TbMT57-HA protein, defective in the biogenesis of the SL cap 4 structure
additional information
trans-splicing utilization of the SL RNA is not detectably affected in mt57-/- cells, SS1 proteins similar to that of the wild-type TbMT57-HA protein, defective in the biogenesis of the SL cap 4 structure
additional information
-
trans-splicing utilization of the SL RNA is not detectably affected in mt57-/- cells, SS1 proteins similar to that of the wild-type TbMT57-HA protein, defective in the biogenesis of the SL cap 4 structure
additional information
-
333-codon open-reading frame is cut out and expressed in Escherichia coli, reduced methyltransferase and RNA binding activity
additional information
-
charged amino acids Asp, Glu, His, Lys, Arg are exchanged for Ala by oligonucleotide-directed mutagenesis, glutathione-S-transferase-tagged, 11 of 21 Ala-mutants show reduced activity, 4 show increased activity
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Cap-specific mRNA (nucleoside-O2-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein
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Biochemistry
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Vaccinia virus
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An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization
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Mutational analysis of a multifunctional protein, with mRNA 5' cap-specific (nucleoside-2'-O-)-methyltransferase and 3'-adenylyltransferase stimulatory activities, encoded by vaccinia virus
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Preliminary characterization of (nucleoside-2-O-)-methyltransferase crystals from Meaban and Yokose flaviviruses
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Meaban virus, Yokose virus
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pKa of the mRNA cap-specific 2-O-methyltransferase catalytic lysine by HSQC NMR detection of a two-carbon probe
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Vaccinia virus (P07617)
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A protein related to the vaccinia virus cap-specific methyltransferase VP39 is involved in cap 4 modification in Trypanosoma brucei
RNA
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Trypanosoma brucei (Q385S9), Trypanosoma brucei (Q38DJ3), Trypanosoma brucei
brenda
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Biochemical characterization of the (nucleoside-2'O)-methyltransferase activity of dengue virus protein NS5 using purified capped RNA oligonucleotides (7Me)GpppAC(n) and GpppAC(n)
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Characterization of hMTr1, a human Cap1 2-O-ribose methyltransferase
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Molecular mapping of the RNA cap 2'-O-methyltransferase activation interface between severe acute respiratory syndrome coronavirus nsp10 and nsp16
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Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2-O-methyltransferase nsp10/nsp16 complex
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Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2-O-methylation by nsp16/nsp10 protein complex
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Severe acute respiratory syndrome-related coronavirus (G8H306), Severe acute respiratory syndrome-related coronavirus, Severe acute respiratory syndrome-related coronavirus WHU (G8H306)
brenda
Szretter, K.J.; Daniels, B.P.; Cho, H.; Gainey, M.D.; Yokoyama, W.M.; Gale, M.; Virgin, H.W.; Klein, R.S.; Sen, G.C.; Diamond, M.S.
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Identification of aromatic amino acid residues in conserved region VI of the large polymerase of vesicular stomatitis virus is essential for both guanine-N-7 and ribose 2-O methyltransferases
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Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2'-O-methyltransferase activity of nsp10/nsp16 complex
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Structure-based identification of functional residues in the nucleoside-2-O-methylase domain of Bluetongue virus VP4 capping enzyme
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brenda
Simabuco, F.M.; Pavan, I.C.B.; Pestana, N.F.; Carvalho, P.C.; Basei, F.L.; Campos Granato, D.; Paes Leme, A.F.; Zanchin, N.I.T.
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