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Information on EC 2.7.7.48 - RNA-directed RNA polymerase and Organism(s) Homo sapiens

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EC Tree
IUBMB Comments
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
rna polymerase, rna-binding protein, rna-dependent rna polymerase, rdrp, nonstructural protein, transcriptase, vp1 protein, pol iv, rna-dependent rna polymerases, ns5b polymerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
111 kDa protein
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-
-
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180 kDa protein
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-
-
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182 kDa protein
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-
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183 kDa protein
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-
-
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186 kDa protein
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-
-
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216.5 kDa protein
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-
-
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2A protein
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-
-
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3D pol
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-
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3D polymerase
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-
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69.6 kDa protein
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-
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core protein
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-
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core protein VP1
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-
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inner layer protein VP1
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-
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L protein
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-
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large structural protein
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-
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M1 phosphoprotein
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-
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NIB
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-
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nonstructural phosphoprotein
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nonstructural protein
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-
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nonstructural protein 5B
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-
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NS5B
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NS5B protein
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nucleocapsid phosphoprotein
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nucleotidyltransferase, ribonucleate, RNA-dependent
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ORF1
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ORF1A
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ORF1B
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-
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P protein
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-
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P180
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-
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P3D
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-
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P66
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-
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P70
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-
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P88 protein
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-
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PB1
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-
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PB1 proteins
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-
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PB2
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PB2 proteins
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Phage f2 replicase
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Pol
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polymerase acidic protein
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polymerase basic 1 protein
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polymerase L
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proteins PB1
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proteins, PB 2
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proteins, specific or class, lambda3, of reovirus
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proteins, specific or class, PB 1
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proteins, specific or class, PB 2
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Q-beta replicase
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Qbeta replicase
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Qbeta-replicase
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replicase, phage f2
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replicase, Qbeta
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ribonucleic acid replicase
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ribonucleic acid-dependent ribonucleate nucleotidyltransferase
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ribonucleic acid-dependent ribonucleic acid polymerase
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ribonucleic replicase
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ribonucleic synthetase
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RNA nucleotidyltransferase (RNA-directed)
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RNA replicase
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RNA synthetase
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RNA transcriptase
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RNA-binding protein
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RNA-dependent ribonucleate nucleotidyltransferase
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RNA-dependent RNA polymerase
RNA-dependent RNA replicase
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RNA-dependent RNA-polymerase
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RNA-directed RNA polymerase
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sigma NS protein
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transcriptase
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VP1
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VP1 protein
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (RNA-directed)
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-28-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
additional information
?
-
-
RNA polymerase II (PolII) acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Pol II extends B2 RNA by 18 nt on its 3'-end in an internally templated reaction. The RNA product resulting from extension of B2 RNA by the Pol II RdRP can be removed from Pol II by a factor present in nuclear extracts
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
B2 RNA is a substrate for RNA dependent RNA polymerization by Pol II
-
-
?
additional information
?
-
-
RNA polymerase II (PolII) acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Pol II extends B2 RNA by 18 nt on its 3'-end in an internally templated reaction. The RNA product resulting from extension of B2 RNA by the Pol II RdRP can be removed from Pol II by a factor present in nuclear extracts
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
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1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
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1-(2,5-difluorophenyl)-3-phenyltriazene
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1-(2,5-difluorophenyl)azopyrrolidine
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1-(3,4-dichlorophenyl)azopyrrolidine
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1-(3-bromophenyl)azopiperidine
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1-(3-bromophenyl)azopyrrolidine
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1-(3-chloro)-3-phenyltriazene N-methyl
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1-(3-chlorophenyl)azopiperidine
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1-(3-chlorophenyl)azopyrrolidine
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1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
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1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
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1-(3-nitrophenyl)-3-phenyltriazene
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1-(3-nitrophenyl)azopiperidine
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1-(3-nitrophenyl)azopyrrolidine
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1-(3-trifluoromethylphenyl)azopyrrolidine
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1-(4-bromophenyl)azopiperidine
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1-(4-bromophenyl)azopyrrolidine
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1-(4-chlorophenyl)azopiperidine
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1-(4-chlorophenyl)azopyrrolidine
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1-(4-methoxyphenyl)azopyrrolidine
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1-(4-methylphenyl)-3-methyl-3-phenyltriazene
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1-(4-nitrophenyl)azopyrrolidine
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1-methyl-4-(2,5-difluorophenylazo)piperazine
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1-methyl-4-(phenylazo)piperazine
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1-phenyl-3-(3'-trifluoromethylphenyl)triazene
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1-phenyl-3-benzyltriazene
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1-phenyl-3-methyl-3-benzyltriazene
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1-phenyl-3-phenyltriazene
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1-phenyl-azopiperidine
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1-phenyl-azopyrrolidine
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1-phenylazo-4-oxopiperidine
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1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
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1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
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1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
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1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
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2'-C-ethynylcytidine
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2'-C-methylguanosine
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2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
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2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
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3-(3-nitrophenylazo)cytisine
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3-(4-chlorophenylazo)cytisine
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3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
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4-phenylazo-1-(phenyl)piperazine
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4-phenylazo-1-(pyrimidin-2'-yl)piperazine
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4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
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4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
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6-azauridine
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acycloguanosine
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alpha-Amanitin
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alpha-amanitin inhibits extension of B2 RNA by Pol II in vitro
Ethyl 4-(phenylazo)-piperazincarboxylate
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Mycophenolic acid
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N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
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N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
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N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
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N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
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N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
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N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
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N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
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N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
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N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
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N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
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N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
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ribavirin
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[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
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additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
CD4+ human T cells containing an integrated HTLV-1 genome
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
RNA polymerase II acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Mammalian Pol II acts as an RdRP to control the stability of a cellular RNA by extending its 3'-end. Extended B2 RNA can repress transcription, but with decreased potency
additional information
-
treatment of cells with a-amanitin or actinomycin D revealed that extension of B2 RNA by Pol II destabilizes the RNA
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RPB1_HUMAN
1970
0
217176
Swiss-Prot
other Location (Reliability: 3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tonelli, M.; Vazzana, I.; Tasso, B.; Boido, V.; Sparatore, F.; Fermeglia, M.; Paneni, M.S.; Posocco, P.; Pricl, S.; La Colla, P.; Ibba, C.; Secci, B.; Collu, G.; Loddo, R.
Antiviral and cytotoxic activities of aminoarylazo compounds and aryltriazene derivatives
Bioorg. Med. Chem.
17
4425-4440
2009
Chlorocebus aethiops, Bos taurus, Cricetulus griseus, Human alphaherpesvirus 1, Homo sapiens, Reovirus sp., Yellow fever virus, Coxsackievirus B2, Respiratory syncytial virus, Bovine viral diarrhea virus 1 (P19711), Bovine viral diarrhea virus 1
Manually annotated by BRENDA team
Wagner, S.D.; Yakovchuk, P.; Gilman, B.; Ponicsan, S.L.; Drullinger, L.F.; Kugel, J.F.; Goodrich, J.A.
RNA polymerase II acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA
EMBO J.
32
781-790
2013
Homo sapiens
Manually annotated by BRENDA team