Any feedback?
Information on EC 2.7.7.6 - DNA-directed RNA polymerase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q980Q9
for references in articles please use BRENDA:EC2.7.7.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.6 DNA-directed RNA polymeraseIUBMB Comments
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
Specify your search results
Word Map
- 2.7.7.6
- chromatin
- histone
- rrna
- strand
-
rnaps
- nucleosome
- tata
- drosophila
-
pausing
- pre-mrnas
- tbp
-
nucleolar
- bacteriophage
-
polyadenylation
-
single-stranded
-
cyclin-dependent
-
holoenzyme
- cyclin
-
spacers
- helicase
-
fidelity
- polya
-
coactivator
-
protein-coding
-
transactivation
- adenovirus
- xenopus
- ribonucleoproteins
-
sequence-specific
-
stall
-
pause
-
chip-seq
- vaccinia
-
multisubunit
-
ribozyme
- heptapeptide
- duplex
-
h3k4me3
-
spliceosome
- nucleoplasm
-
run-on
-
supercoiled
-
trimethylation
-
subcomplexes
-
exonuclease
- heterochromatin
-
translesion
- medicine
- primase
- molecular biology
- analysis
- diagnostics
- drug development
-
misincorporation
-
proofread
- synthesis
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
rna polymerase ii, pol ii, t7 rna polymerase, rna polymerase i, pol iii, rna polymerase iii, pol i, rnapii, rnap ii, dna-dependent rna polymerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C RNA formation factors
-
-
-
-
chloroplast soluble RNA polymerase
-
-
-
-
deoxyribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
-
DNA-dependent ribonucleate nucleotidyltransferase
-
-
-
-
DNA-dependent RNA nucleotidyltransferase
-
-
-
-
DNA-dependent RNA polymerase
nucleotidyltransferase, ribonucleate
-
-
-
-
Pol II
ribonucleate nucleotidyltransferase
-
-
-
-
ribonucleate polymerase
-
-
-
-
ribonucleic acid formation factors, C
-
-
-
-
ribonucleic acid nucleotidyltransferase
-
-
-
-
ribonucleic acid polymerase
-
-
-
-
ribonucleic acid transcriptase
-
-
-
-
ribonucleic polymerase
-
-
-
-
ribonucleic transcriptase
-
-
-
-
RNA formation factors, C
-
-
-
-
RNA nucleotidyltransferase
-
-
-
-
RNA nucleotidyltransferase (DNA-directed)
-
-
-
-
RNA polymerase
RNA polymerase I
-
-
-
-
RNA polymerase II
RNA polymerase III
-
-
-
-
RNA transcriptase
-
-
-
-
RNAP
RNAP I
-
-
-
-
RNAP II
RNAP III
-
-
-
-
transcriptase
-
-
-
-
additional information
-
RNA polymerase is a member of the iron-sulfur cluster protein family
DNA-dependent RNA polymerase
-
-
-
-
Pol II
-
-
-
-
RNA polymerase
-
-
-
-
RNA polymerase II
-
-
-
-
RNA polymerase II
Q980R2; P58192; Q980R1; P95989; Q980A3; Q9UXD9; Q980L5; Q980Q9; Q97ZJ9; Q980K0; Q980Z8; Q97ZX7; Q980B8
-
RNAP
-
-
-
-
RNAP II
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed)
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
CAS REGISTRY NUMBER
COMMENTARY
9014-24-8
-
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
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q980R2; P58192; Q980R1; P95989; Q980A3; Q9UXD9; Q980L5; Q980Q9; Q97ZJ9; Q980K0; Q980Z8; Q97ZX7; Q980B8
-
-
-
?
additional information
?
-
-
multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
-
-
?
additional information
?
-
-
RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
-
-
?
additional information
?
-
-
RNAP adds nucleotides to the 3'-end of the growing RNA and translocates reiteratively, in single nucleotide steps. Translocation mechanism models, concerning conformational changes, allosteric effects and isomerization, and model evaluation, overview
-
-
?
additional information
?
-
-
the enzyme active site is located on the back wall of the channel, where an essential Mg2+ ion is chelated by three Asp of the absolutely conserved NADFDGD motif in the A' subunit
-
-
?
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
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q980R2; P58192; Q980R1; P95989; Q980A3; Q9UXD9; Q980L5; Q980Q9; Q97ZJ9; Q980K0; Q980Z8; Q97ZX7; Q980B8
-
-
-
?
additional information
?
-
-
multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
-
-
?
additional information
?
-
-
RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Mg2+
Iron
Q980R2; P58192; Q980R1; P95989; Q980A3; Q9UXD9; Q980L5; Q980Q9; Q97ZJ9; Q980K0; Q980Z8; Q97ZX7; Q980B8
the enzyme possesses a unique Fe-S cluster
Iron
-
RNA polymerase is a member of the iron-sulfur cluster protein family and contains one 4Fe-4S cluster binding motif
Mg2+
-
the enzyme active site is located on the back wall of the channel, where an essential Mg2+ ion is chelated by three Asp of the absolutely conserved NADFDGD motif in the A' subunit
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q980R2: subunit A', P58192: subunit A'', Q980R1: subunit B, P95989: subunit D, Q980A3: subunit E', Q9UXD9: subunit F, Q980L5: subunit G, Q980Q9: subunit H, Q97ZJ9: subunit K, Q980K0: subunit L, Q980Z8: subunit N, Q97ZX7: subunit P, Q980B8: subunit 13
Q980R2; P58192; Q980R1; P95989; Q980A3; Q9UXD9; Q980L5; Q980Q9; Q97ZJ9; Q980K0; Q980Z8; Q97ZX7; Q980B8
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
reverse translocation, i.e. backtracking, by a distance of one or more nucleotides disrupts the configuration of the catalytic center, leading to a temporary, spontaneously resolved, halt of the RNAP, called pausing, or to a transition into an irreversible arrested state. The latter can be restored to functionality by the endonucleolytic cleavage of the RNA or by pushing the backtracked complex from behind. Non-backtracked paused complexes are also described for bacterial RNAPs, where addition of the incoming NTP is hindered owing to isomerization of the active site into an inactive conformation
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
-
structure and modeling of the multi-subunit enzyme complex, RNAP subunits can be divided into three groups concerned with catalysis, assembly of the catalytic subunits and auxiliary functions, overview. The large A and B subunits are split into two polypeptides, A'/A'' and B''/B' according to size, they harbour the binding sites for substrate NTPs, duplex DNA template and a 9 bp DNA-RNA hybrid, and provide the catalytic centre, including three catalytic aspartic acid residues and two Mg2+ ions
additional information
additional information
-
conformational plasticity of the active center and importance of the bridge helix structure for enzyme activity, overview
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea. The enzyme lacks the G subunit
additional information
-
structure analysis, overview, the enzyme contains a subunit Rpo13 located at a groove between the H subunit and the clamp head domain of the A' subunit, model ing including the A' subunit jaw and clamp head domains and RpoG and Rpo13, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination, structure including the A' subunit jaw and clamp head domains and RpoG and Rpo13 subunits
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirata, A.; Klein, B.J.; Murakami, K.S.
The X-ray crystal structure of RNA polymerase from Archaea
Nature
451
851-854
2008
Saccharolobus solfataricus (Q980R2 and P58192 and Q980R1 and P95989 and Q980A3 and Q9UXD9 and Q980L5 and Q980Q9 and Q97ZJ9 and Q980K0 and Q980Z8 and Q97ZX7 and Q980B8), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q980R2 and P58192 and Q980R1 and P95989 and Q980A3 and Q9UXD9 and Q980L5 and Q980Q9 and Q97ZJ9 and Q980K0 and Q980Z8 and Q97ZX7 and Q980B8)
Grohmann, D.; Hirtreiter, A.; Werner, F.
Molecular mechanisms of archaeal RNA polymerase
Biochem. Soc. Trans.
37
12-17
2009
Saccharomyces cerevisiae, Saccharolobus solfataricus, Thermus aquaticus
Svetlov, V.; Nudler, E.
Macromolecular micromovements: how RNA polymerase translocates
Curr. Opin. Struct. Biol.
19
701-707
2009
Saccharomyces cerevisiae, Escherichia coli, Thermus thermophilus, Saccharolobus solfataricus, Thermus aquaticus
Hirata, A.; Murakami, K.S.
Archaeal RNA polymerase
Curr. Opin. Struct. Biol.
19
724-731
2009
Archaeoglobus fulgidus, Saccharomyces cerevisiae, Homo sapiens, Methanocaldococcus jannaschii, Pyrococcus furiosus, Thermococcus kodakarensis, Schizosaccharomyces pombe, Saccharolobus shibatae, Saccharolobus solfataricus
Kwapisz, M.; Beckouet, F.; Thuriaux, P.
Early evolution of eukaryotic DNA-dependent RNA polymerases
Trends Genet.
24
211-215
2008
Saccharomyces cerevisiae, Cenarchaeum symbiosum, Escherichia coli, Emiliania huxleyi, Methanocaldococcus jannaschii, Pyrococcus furiosus, Sulfolobus acidocaldarius, Saccharolobus solfataricus, Nanoarchaeum equitans, Caldivirga maquilingensis, Nitrosopumilus maritimus, Thermofilum pendens
EXTERNAL LINKS (specific for EC-Number 2.7.7.6)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
