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Information on EC 2.1.1.57 - methyltransferase cap1
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2.1.1.57 methyltransferase cap1IUBMB Comments
This enzyme catalyses the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules. This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine .
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Word Map
- 2.1.1.57
- sars-cov-2
- coronaviruses
-
2'-o-methylation
-
non-structural
- flaviviruses
- sinefungin
- coronaviridae
-
2'-o-ribose
-
adomet-dependent
- nsp8
- n7-mtase
- 3clpro
-
replication-transcription
-
guanine-n7
-
guanine-n7-methyltransferase
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA]
=
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Synonyms
nsp16, 2'-o-methyltransferase, 2'-o-mtase, cmtr1, ns5 mtase, 2'-o mtase, (nucleoside-2'-o-)-methyltransferase, nonstructural protein 16, 2'-o methyltransferase, isg95, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(nucleoside-2'-O-)-methyltransferase
2'-O MTase
2'-O-methyltransferase
2'-O-MTase
2'O-MTase
2'OMTases
EC 2.1.1.58
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formerly
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messenger ribonucleate nucleoside 2'-methyltransferase
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-
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messenger RNA (nucleoside-2'-)-methyltransferase
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methyltransferase, messenger ribonucleate nucleoside 2'-
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mRNA (nucleoside-2'-O)-methyltransferase
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-
-
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mRNA cap-specific 2'-O-methyltransferase
Mtr1
NS5MTase
nsp10/nsp16 complex
nsp16
nsp16/nsp10 protein complex
RNA cap 2'-O-methyltransferase
-
-
RNA cap 2'-O-MTase
VP39
(nucleoside-2'-O-)-methyltransferase
-
-
NS5MTase
-
the protein contains mRNA cap (guanine N-7) methyltransferase and (nucleoside-2'O)-methyltransferase activities
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
binding sites of the enzyme for the terminal cap nucleotide, m7G, the cap-proximal RNA, and for RNA, immediately downstream, are characterized
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S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
R may be guanine or adenosine, mechanism
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S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
nucleotide binding analysis based on crystal structure
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
simple one-step reaction mechanism, only the positively charged keto tautomer of the cap is recognized and bound. Binding is achieved almost entirely by the interactions of m7guanosine with two aromatic residues in a cation-pi sandwich
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S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
R may be guanine or adenosine, mechanism
-
-
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:5-(N7-methyl 5-triphosphoguanosine)-(ribonucleotide)-[mRNA] 2-O-methyltransferase
This enzyme catalyses the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules. This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine [6].
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CAS REGISTRY NUMBER
COMMENTARY
61970-02-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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
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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)
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-
-
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r
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
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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
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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 + m7GpppACCCCC
S-adenosyl-L-homocysteine + m7GpppAmCCCCC
-
-
?
S-adenosyl-L-methionine + m7GpppApGp
S-adenosyl-L-homocysteine + m7GpppAmpGp
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i.e. capped dinucleotide, cap I-methyltransferase
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?
S-adenosyl-L-methionine + m7GpppApGpUp
S-adenosyl-L-homocysteine + m7GpppAmpGpUp
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i.e. capped trinucleotide, cap I-methyltransferase
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?
S-adenosyl-L-methionine + m7GpppG
S-adenosyl-L-homocysteine + m7GpppGm
-
-
-
?
S-adenosyl-L-methionine + m7GpppGp
S-adenosyl-L-homocysteine + m7GpppGmp
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substrate of minimal chain length for the cap-specific enzyme, m7GpppG is no substrate
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-
?
S-adenosyl-L-methionine + m7GpppGpN
S-adenosyl-L-homocysteine + m7GpppGmpN
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-
-
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?
S-adenosyl-L-methionine + mononucleotide
?
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such as m7GpppA or GpppA, poor substrates for cap I-methyltransferase
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-
?
S-adenosyl-L-methionine + 7Me-GpppA-C5
S-adenosyl-L-homocysteine + 7Me-GpppA-2'OMe-C5
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exclusive methylation at the 2'O position
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-
?
S-adenosyl-L-methionine + 7Me-GpppA-C5
S-adenosyl-L-homocysteine + 7Me-GpppA-2'OMe-C5
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-
-
-
?
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]
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-
-
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?
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]
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-
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?
S-adenosyl-L-methionine + ApppGR-RNA
?
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adenine-capped RNA, wild-type and mutants, indicating the redundancy of m7G-contact residues able to confer cap-type specificity
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?
S-adenosyl-L-methionine + ApppGR-RNA
?
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synthetic substrate with unusual cap structure, 20% activity compared to m7G-terminated substrates
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?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppAm-RNA
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-
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?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppAm-RNA
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-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppAm-RNA
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-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRA-RNA
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-
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?
S-adenosyl-L-methionine + m7G(5')pppA-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRA-RNA
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-
-
?
S-adenosyl-L-methionine + m7G(5')pppG-RNA
S-adenosyl-L-homocysteine + m7G(5')pppGm-RNA
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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
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-
?
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
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?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
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-
-
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?
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
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?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
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satellite tobacco necrosis virus
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-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
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-
?
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
?
-
-
no substrates are RNAs with pN-, ppN-, guanine(5')pppN-terminals
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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 + GpppA-Cn
S-adenosyl-L-homocysteine + GpppA-2'OMe-Cn
-
exclusive methylation at the 2'O position
-
-
?
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 + 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
-
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
-
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
contains Mg2+, Mg2+ can be substituted by Mn2+ or Ca2+, but not Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-deoxy-ribavirin 5'-triphosphate
binds almost as efficiently as ribavirin 5-triphosphate
5-ethynyl-1-beta-D-ribofuranosylimidazole-4-carboxamide triphosphate
-
about 40% inhibition at 0.1 mM
A9145C
-
i.e. amino acid modified structure analogue of adenosyl-L-homocysteine, competitive
additional information
-
peptides K12 (aa 68-80 of nsp10), and K29 (aa 68-96 of nsp10) decrease the S-adenosyl-L-methionine (SAM) binding by nsp16 in a dose-dependent manner. When 0.4 mM of K29 is used, it almost abolishes the SAM-binding activity of nsp16. In contrast, the peptides K8 (aa 100-107 of nsp10), K10 (aa 91-100 of nsp10) and K20 (aa 40-59 of nsp10), which cannot inhibit the 2'-O-MTase activity of nsp16, have no effect on SAM binding of nsp16, even when the final concentration of 0.5 mM is applied
-
additional information
-
no inhibition by poly(A), poly(U), poly(C) or poly(G)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-deoxy-5'-(methylthio)adenosine
-
about 75% increased activity at 0.1 mM
5'-S-isobutylthio-5'-deoxyadenosine
-
about 60% increased activity at 0.1 mM
ATP-dependent RNA DHX15 helicase
-
the enzyme acts poorly on capped RNA molecules whose 5'-terminal residues are base-paired to form secondary structure. However, the enzyme uses its G-patch domain to form a strong complex with ATP-dependent RNA, which significantly improves the efficiency of cap1 methylation of such RNAs
-
nsp10 protein
-
nsp10 acts as an essential trigger to activate the 2'-O-methyltransferase activity of nsp16. The region of amino acids 42120 in nsp10 is needed for stimulating the nsp16 2'-O-methyltransferase activity
-
nsp10 protein
-
nsp16 carries RNA cap 2'-O-methyltransferase activity only in the presence of its interacting partner nsp10
-
nsp10 protein
nsp16 requires non-structural protein nsp10 as a stimulatory factor to execute its methyltransferase activity by binding both S-adenosyl-L-methionine and RNA substrate
-
nsp10 protein
-
the methyltransferase is only active in the presence of its activating partner nsp10
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
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.
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
Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2'O)-methyltransferase activity.
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
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.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
S-adenosyl-L-methionine
-
apparent value, in glycine buffer (pH 10.0), at 22°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
HeLa S-3 cells infected with vaccinia virus, no activity in uninfected cells
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
viruses lacking 2'-O methyltransferase activity exhibit attenuation in primary macrophages
physiological function
physiological function
-
the RNA capping enzyme domain in protein A is essential for flock house virus replication
Show AA Sequence and Transmembrane Helices (2719 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
35000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1 * 33000, recombinant truncated N-terminal protein, gel filtration, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.5 A resolution. Residues 175 to 377 encode a distinct 2'-O MT domain segregated from the other domains and responsible for methylation of cap0 structure
hanging drop method at room temperature, 0.1 M sodium citrate pH 5.8, 1.2 M lithium sulfate, 0.5 M ammonium sulfate, vapour diffusion for 1 week, structure analysis with and without bound nucleotide, model
by vapour-diffusion, to 2.8 A resolution, in complex with S-adenosyl-l-methionine, crystals belong to the tetragonal space group P43, with unit-cell parameters a = b = 83.0, c = 170.2 A, presence of four MTase molecules per asymmetric unit and a corresponding solvent content of 49.9%, residues Lys62, Asp147, Lys184 and Glu220 specifically characterize the active-site region
-
hanging drop vapor diffusion method, using in 0.1 M MES, pH 5.0, 2 M NaCl, 0.1 M NaH2PO4, 0.1 M KH2PO4 after 24 h at 25°C
by vapour-diffusion, to 2.7 A resolution, in complex with S-adenosyl-l-methionine, crystals belong to the orthorhombic space group P21212, with unit-cell parameters a = 58.7, b = 126.6, c = 156.1 A, presence of three MTase molecules in the asymmetric unit, with a solvent content of 57.7%, residues Lys62, Asp147, Lys184 and Glu220 specifically characterize the active-site region
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
W215A
-
the mutant shows reduced RNA synthesis activity compared to the wild type
D106A
-
the mutant shows 38% of wild type activity
D130A
-
the mutant shows 2% of wild type activity
G70A
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
K93A
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
Y96A
Y96F
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
-
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
G96D
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
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
K1795A
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
additional information
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
additional information
-
binding site of the enzyme for RNA, immediately downstream, is pH-sensitive, above pH 7.5: dramatic increase of Km
639484
10
-
at basic pH, 2'O-MTase activity is practically non-existent and neither Mg2+ nor KCl is able to activate the methyl transfer at pH 10.0
704920
10
-
at basic pH, 2'O-MTase activity is practically non-existent and neither Mg2+ nor KCl is able to activate the methyl transfer at pH 10.0
704920
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
and below, stable in the presence of 10% v/v glycerol and 250 mg/l bovine serum albumin
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration
HisPur cobalt resin column chromatography
-
HiTrap heparin column chromatography and HIS Select nickel affinity gel filtration and HiTrap Q column chromatography
-
Ni-NTA resin column chromatography and Superdex 200 gel filtration
nickel-nitrilotriacetic acid resin column chromatography and heparin-Sepharose 6 column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
as N-terminal His6-tag expressed in a pDEST 14 HN expression vector and transformed into Escherichia coli Rosetta (DE3) pRos
cloning of His-tagged N-terminal part of NS5 protein, termed NS5MTaseDV, amino acids 1-296, overexpression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli C41 (DE3) cells
-
expression of wild-type, exchange mutants and open-reading-frame mutant in Escherichia coli, all glutathione-S-transferase-tagged
-
as N-terminal His6-tag expressed in a pDEST 14 HN expression vector and transformed into Escherichia coli Rosetta (DE3) pRos
-
as N-terminal His6-tag expressed in a pDEST 14 HN expression vector and transformed into Escherichia coli Rosetta (DE3) pRos
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
-
the nsp10-nsp16 interface represents an attractive target for antivirals against human and animal pathogenic coronaviruses
additional information
analysis
characterization of the side chain pKa for a single lysine analogue within a 316-residue protein containing 21 lysines and 1678 carbon atoms at natural isotope abundance, achieved by the single reactive cysteine of a K175C mutant of VP39 modified to S-(beta-aminoethyl)cysteine (gamma-thialysine) using freshly prepared (13C)aziridine at room temperature
additional information
-
domain VI of vesicular stomatitis virus L protein functions as a methyltransferase, active-site residues K1651, D1762, K1795, and E1833 within domain VI are essential for mRNA cap methylation
additional information
related to the vaccinia virus VP39 cap 2'-O-methyltransferase, may has a minor role in the biogenesis of the SL RNA cap 4 structure
additional information
related to the vaccinia virus VP39 cap 2'-O-methyltransferase, may has a minor role in the biogenesis of the SL RNA cap 4 structure
additional information
-
related to the vaccinia virus VP39 cap 2'-O-methyltransferase, may has a minor role in the biogenesis of the SL RNA cap 4 structure
additional information
relatively low overall sequence conservation between vaccinia virus VP39 and TbMT57, has a major role in the biogenesis of the SL RNA cap 4 structure
additional information
relatively low overall sequence conservation between vaccinia virus VP39 and TbMT57, has a major role in the biogenesis of the SL RNA cap 4 structure
additional information
-
relatively low overall sequence conservation between vaccinia virus VP39 and TbMT57, has a major role in the biogenesis of the SL RNA cap 4 structure
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pugh, C.S.G.; Borchardt, R.T.
Effects of S-adenosylhomocysteine analogues on vaccinia viral messenger ribonucleic acid synthesis and methylation
Biochemistry
21
1535-1541
1982
Vaccinia virus, Vaccinia virus WR
brenda
Ensinger, M.J.; Martin, S.A.; Paoletti, E.; Moss, B.
Modification of the 5-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus
Proc. Natl. Acad. Sci. USA
72
2525-2529
1975
Vaccinia virus, Vaccinia virus WR
brenda
Ramadevi, N.; Burroughs, N.J.; Mertens, P.P.C.; Jones, I.M.
Capping and methylation of mRNA by purified recombinant VP4 protein of bluetongue virus
Proc. Natl. Acad. Sci. USA
95
13537-13542
1998
bluetongue virus
brenda
Barbosa, E.; Moss, B.
mRNA(nucleoside-2-)-methyltransferase from vaccinia virus. Purification and physical properties
J. Biol. Chem.
253
7692-7697
1978
Vaccinia virus, Vaccinia virus WR
brenda
Barbosa, E.; Moss, B.
mRNA(nucleoside-2-)-methyltransferase from vaccinia virus. Characteristics and substrate specificity
J. Biol. Chem.
253
7698-7702
1978
Vaccinia virus, Vaccinia virus WR
brenda
Pugh, C.S.G.; Borchardt, R.T.; Stone, H.O.
Sinefungin, a potent inhibitor of virion mRNA(guanine-7-)-methyltransferase, mRNA(nucleoside-2-)-methyltransferase, and viral multiplication
J. Biol. Chem.
253
4075-4077
1978
Vaccinia virus, Vaccinia virus WR
brenda
Langberg, S.R.; Moss, B.
Post-transcriptional modifications of mRNA. Purification and characterization of cap I and cap II RNA (nucleoside-2-)-methyltransferases from HeLa cells
J. Biol. Chem.
256
10054-10060
1981
Homo sapiens
brenda
Schnierle, B.S.; Gershon, P.; Moss, B.
Cap-specific mRNA (nucleoside-O2-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein
Proc. Natl. Acad. Sci. USA
89
2897-2901
1992
Vaccinia virus, Vaccinia virus WR
brenda
Boone, R.F.; Ensinger, M.J.; Moss, B.
Synthesis of mRNA guanylyltransferase and mRNA methyltransferases in cells infected with vaccinia virus
J. Virol.
21
475-483
1977
Homo sapiens
brenda
Lockless, S.W.; Cheng, H.T.; Hodel, A.E.; Quiocho, F.A.; Gershon, P.D.
Recognition of capped RNA substrates by VP39, the vaccinia virus-encoded mRNA cap-specific 2'-O-methyltransferase
Biochemistry
37
8564-8574
1998
Vaccinia virus
brenda
Egloff, M.P.; Benarroch, D.; Selisko, B.; Romette, J.L.; Canard, B.
An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization
EMBO J.
21
2757-2768
2002
Dengue virus (P12823)
brenda
Schnierle, B.S.; Gershon, P.D.; Moss, B.
Mutational analysis of a multifunctional protein, with mRNA 5' cap-specific (nucleoside-2'-O-)-methyltransferase and 3'-adenylyltransferase stimulatory activities, encoded by vaccinia virus
J. Biol. Chem.
269
20700-20706
1994
Vaccinia virus
brenda
Latner, D.R.; Xiang, Y.; Lewis, J.I.; Condit, J.; Condit, R.C.
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
Virology
269
345-355
2000
Vaccinia virus
brenda
Hu, G.; Tsai, A.L.; Quiocho, F.A.
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
J. Biol. Chem.
278
51515-51520
2003
Vaccinia virus
brenda
Benarroch, D.; Egloff, M.P.; Mulard, L.; Guerreiro, C.; Romette, J.L.; Canard, B.
A structural basis for the inhibition of the NS5 Dengue Virus mRNA 2'-O-methyltransferase domain by ribavirin 5'-triphosphate
J. Biol. Chem.
279
35638-35643
2004
Dengue virus (P12823), Dengue virus
brenda
Mastrangelo, E.; Bollati, M.; Milani, M.; de Lamballeire, X.; Brisbare, N.; Dalle, K.; Lantez, V.; Egloff, M.P.; Coutard, B.; Canard, B.; Gould, E.; Forrester, N.; Bolognesi, M.
Preliminary characterization of (nucleoside-2-O-)-methyltransferase crystals from Meaban and Yokose flaviviruses
Acta Crystallogr. Sect. F
F62
768-770
2006
Meaban virus, Yokose virus
brenda
Li, C.; Gershon, P.D.
pKa of the mRNA cap-specific 2-O-methyltransferase catalytic lysine by HSQC NMR detection of a two-carbon probe
Biochemistry
45
907-917
2006
Vaccinia virus (P07617)
brenda
Li, J.; Fontaine-Rodriguez, E.C.; Whelan, S.P.
Amino acid residues within conserved domain VI of the vesicular stomatitis virus large polymerase protein essential for mRNA cap methyltransferase activity
J. Virol.
79
13373-13384
2005
vesicular stomatitis virus
brenda
Arhin, G.K.; Li, H.; Ullu, E.; Tschudi, C.
A protein related to the vaccinia virus cap-specific methyltransferase VP39 is involved in cap 4 modification in Trypanosoma brucei
RNA
12
53-62
2006
Trypanosoma brucei (Q385S9), Trypanosoma brucei (Q38DJ3), Trypanosoma brucei
brenda
Selisko, B.; Peyrane, F.F.; Canard, B.; Alvarez, K.; Decroly, E.
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)
J. Gen. Virol.
91
112-121
2010
Dengue virus, feline coronavirus
brenda
Belanger, F.; Stepinski, J.; Darzynkiewicz, E.; Pelletier, J.
Characterization of hMTr1, a human Cap1 2-O-ribose methyltransferase
J. Biol. Chem.
285
33037-33044
2010
Homo sapiens
brenda
Lugari, A.; Betzi, S.; Decroly, E.; Bonnaud, E.; Hermant, A.; Guillemot, J.C.; Debarnot, C.; Borg, J.P.; Bouvet, M.; Canard, B.; Morelli, X.; Lecine, P.
Molecular mapping of the RNA cap 2'-O-methyltransferase activation interface between severe acute respiratory syndrome coronavirus nsp10 and nsp16
J. Biol. Chem.
285
33230-33241
2010
Severe acute respiratory syndrome-related coronavirus
brenda
Decroly, E.; Debarnot, C.; Ferron, F.; Bouvet, M.; Coutard, B.; Imbert, I.; Gluais, L.; Papageorgiou, N.; Sharff, A.; Bricogne, G.; Ortiz-Lombardia, M.; Lescar, J.; Canard, B.
Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2-O-methyltransferase nsp10/nsp16 complex
PLoS Pathog.
7
e1002059
2011
Severe acute respiratory syndrome-related coronavirus
brenda
Chen, Y.; Su, C.; Ke, M.; Jin, X.; Xu, L.; Zhang, Z.; Wu, A.; Sun, Y.; Yang, Z.; Tien, P.; Ahola, T.; Liang, Y.; Liu, X.; Guo, D.
Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2-O-methylation by nsp16/nsp10 protein complex
PLoS Pathog.
7
e1002294
2011
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.
2-O methylation of the viral mRNA cap by West Nile virus evades Ifit1-dependent and -independent mechanisms of host restriction in vivo
PLoS Pathog.
8
e1002698
2012
West Nile virus
brenda
Chung, K.Y.; Dong, H.; Chao, A.T.; Shi, P.Y.; Lescar, J.; Lim, S.P.
Higher catalytic efficiency of N-7-methylation is responsible for processive N-7 and 2-O methyltransferase activity in dengue virus
Virology
402
52-60
2010
Dengue virus
brenda
Zhang, X.; Wei, Y.; Ma, Y.; Hu, S.; Li, J.
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
Virology
408
241-252
2010
vesicular stomatitis virus
brenda
Ke, M.; Chen, Y.; Wu, A.; Sun, Y.; Su, C.; Wu, H.; Jin, X.; Tao, J.; Wang, Y.; Ma, X.; Pan, J.A.; Guo, D.
Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2'-O-methyltransferase activity of nsp10/nsp16 complex
Virus Res.
167
322-328
2012
Severe acute respiratory syndrome-related coronavirus, Severe acute respiratory syndrome-related coronavirus WHU
brenda
Stewart, M.E.; Roy, P.
Structure-based identification of functional residues in the nucleoside-2-O-methylase domain of Bluetongue virus VP4 capping enzyme
FEBS open bio
5
138-146
2015
bluetongue virus (C5IWW0), bluetongue virus
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.
Interactome analysis of the human cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (hMTr1) protein
J. Cell. Biochem.
120
5597-5611
2019
Homo sapiens (Q8N1G2), Homo sapiens
brenda
Toczydlowska-Socha, D.; Zielinska, M.M.; Kurkowska, M.; Astha, M.; Almeida, C.F.; Stefaniak, F.; Purta, E.; Bujnicki, J.M.
Human RNA cap1 methyltransferase CMTr1 cooperates with RNA helicase DHX15 to modify RNAs with highly structured 5 termini
Philos. Trans. R. Soc. Lond. B Biol. Sci.
373
20180161
2018
Homo sapiens
brenda
Quirin, T.; Chen, Y.; Pietilae, M.K.; Guo, D.; Ahola, T.
The RNA capping enzyme domain in protein A is essential for flock house virus replication
Viruses
10
483
2018
Flock house virus
brenda
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