2.7.7.50: mRNA guanylyltransferase
This is an abbreviated version!
For detailed information about mRNA guanylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.50
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2.7.7.50
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cyclin
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photosystem
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thylakoids
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photoinhibition
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chloroplast
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cyanobacterium
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chlorophyll
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synechocystis
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photodamage
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photochemical
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triphosphatase
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retinoblastoma
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cyclin-dependent
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vaccinia
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reinhardtii
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high-light
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photoprotection
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5'-triphosphatase
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qa
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mantle
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plastoquinone
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synechococcus
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oxygen-evolving
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thermoluminescence
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photoinactivation
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xanthophyl
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7-methylguanosine
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atrazine
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water-splitting
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p-tefb
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lhcii
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non-photochemical
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alpha-32pgtp
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water-oxidizing
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chloroplast-encoded
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biotechnology
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vp3
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diuron
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nsp1
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low-light
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lincomycin
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grana
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herbicide-resistant
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analysis
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psbo
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reoviridae
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cap-binding
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spt5
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photoinhibitory
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flash-induced
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uncapped
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thermosynechococcus
- 2.7.7.50
- cyclin
- photosystem
- thylakoids
-
photoinhibition
- chloroplast
- cyanobacterium
- chlorophyll
- synechocystis
-
photodamage
-
photochemical
- triphosphatase
- retinoblastoma
-
cyclin-dependent
- vaccinia
- reinhardtii
-
high-light
-
photoprotection
- 5'-triphosphatase
- qa
-
mantle
- plastoquinone
- synechococcus
-
oxygen-evolving
-
thermoluminescence
-
photoinactivation
-
xanthophyl
- 7-methylguanosine
- atrazine
-
water-splitting
- p-tefb
- lhcii
-
non-photochemical
-
alpha-32pgtp
-
water-oxidizing
-
chloroplast-encoded
- biotechnology
- vp3
- diuron
- nsp1
-
low-light
- lincomycin
-
grana
-
herbicide-resistant
- analysis
- psbo
- reoviridae
-
cap-binding
- spt5
-
photoinhibitory
-
flash-induced
-
uncapped
- thermosynechococcus
Reaction
Synonyms
A103R, A103R protein, cap guanylyltransferase-methyltransferase, capping enzyme, capping enzyme guanylyltransferase, Ceg1, CET1, CmCeg1, D1 protein, GDP polyribonucleotidyltransferase, GlCeg1, GTase, GTP-RNA guanylyltransferase, GTP:RNA GTase, guanylyltransferase, guanylyltransferase mRNA capping, HCE, L protein, Mce1, messenger RNA guanylyltransferase, More, mRNA capping enzyme, mRNA guanylyl transferase, mRNA-cap, mRNA-capping enzyme, NAD-decapping enzyme, nsP1, NudC, PRNTase, protein lambda2, RNA capping enzyme, RNA guanylyltransferase, RNGTT, TbCgm1, TTM-type RTPase-GTase, VACWR106, VP3
ECTree
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General Information
General Information on EC 2.7.7.50 - mRNA guanylyltransferase
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malfunction
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enzyme knockdown impairs wing development and represses Hedgehog pathway signalling activity. Enzyme knockdown downregulates transcription factor Cubitus interruptus but upregulates smoothend protein levels
metabolism
physiological function
metabolism
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the enzyme regulates Hedgehog pathway signaling activity depending on its capping-enzyme activity in the cytoplasm and through antagonizing protein kinase A
metabolism
Lyssavirus rabies RC-HL
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the enzyme is essential for viral mRNA cap formation
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a disruptive mutation in the polypeptide Spt5 C-terminal domain-binding site of GTase is synthetically lethal with mutations in the polymerase Pol2 C-terminal domain-binding site. C-terminal domain phosphorylation has opposite effects on the interaction of GTase with Pol2 (Ser5-PO4 is required for binding) versus Spt5 (Thr1-PO4 inhibits binding)
physiological function
in Dts36, a temperature sensitive virus mutant affecting the large subunit of the capping enzyme, of the three enzymatic activities required for mRNA capping, the guanylyltransferase and methyltransferase activities are compromised while the triphosphatase activity and the D12 subunit interaction are unaffected. The mutant enzyme is also defective in stimulating early gene transcription termination and intermediate gene transcription initiation in vitro
physiological function
RNA triphosphatase Cet1 and the RNA guanylyltransferase Ceg1 interact to form a mRNA capping enzyme complex. The guanylyltransferase activity of Ceg1 is stimulated by binding with Cet1. RNA trisphosphatase Cet1 is responsible for transport of Ceg1 into the nucleus, while triphosphatase activity of Cet1 is not required. The Cet1 223-549 region is sufficient for nuclear localization of Cet1
physiological function
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a disruptive mutation in the polypeptide Spt5 C-terminal domain-binding site of GTase is synthetically lethal with mutations in the polymerase Pol2 C-terminal domain-binding site. C-terminal domain phosphorylation has opposite effects on the interaction of GTase with Pol2 (Ser5-PO4 is required for binding) versus Spt5 (Thr1-PO4 inhibits binding)
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physiological function
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RNA triphosphatase Cet1 and the RNA guanylyltransferase Ceg1 interact to form a mRNA capping enzyme complex. The guanylyltransferase activity of Ceg1 is stimulated by binding with Cet1. RNA trisphosphatase Cet1 is responsible for transport of Ceg1 into the nucleus, while triphosphatase activity of Cet1 is not required. The Cet1 223-549 region is sufficient for nuclear localization of Cet1
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physiological function
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in Dts36, a temperature sensitive virus mutant affecting the large subunit of the capping enzyme, of the three enzymatic activities required for mRNA capping, the guanylyltransferase and methyltransferase activities are compromised while the triphosphatase activity and the D12 subunit interaction are unaffected. The mutant enzyme is also defective in stimulating early gene transcription termination and intermediate gene transcription initiation in vitro
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