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Information on EC 2.1.1.57 - methyltransferase cap1 and Organism(s) Homo sapiens and UniProt Accession Q8N1G2
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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
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2'-o-methylation
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non-structural
- flaviviruses
- sinefungin
- coronaviridae
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2'-o-ribose
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adomet-dependent
- nsp8
- n7-mtase
- 3clpro
-
replication-transcription
-
guanine-n7
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guanine-n7-methyltransferase
- analysis
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA]
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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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
messenger ribonucleate nucleoside 2'-methyltransferase
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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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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].
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 + 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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-
-
?
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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-
-
-
?
S-adenosyl-L-methionine + G(5')pppA-poly(A)
S-adenosyl-L-homocysteine + G(5')pppA-2'-OMe-poly(A)
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-
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r
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')pppG-RNA
S-adenosyl-L-homocysteine + m7G(5')pppGm-RNA
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cap1 formation is optimal at 0.005 mM S-adenosyl-L-methionine
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-
?
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 + 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 + mononucleotide
?
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such as m7GpppA or GpppA, poor substrates for cap I-methyltransferase
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?
additional information
?
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the enzyme catalyzes specific methylation of the 2'-O-ribose of the first nucleotide of a capped RNA transcript
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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
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unmethylated vaccinia virus mRNA
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-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
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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
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best substrates are poly(A)-nucleosides and poly-(I)-nucleosides with m7G(5')pppN-ends
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-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
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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
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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
?
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 + 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]
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-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP-dependent RNA DHX15 helicase
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CMTR1_HUMAN
835
0
95321
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap heparin column chromatography and HIS Select nickel affinity gel filtration and HiTrap Q column chromatography
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nickel-nitrilotriacetic acid resin column chromatography and heparin-Sepharose 6 column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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