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Information on EC 2.7.7.6 - DNA-directed RNA polymerase and Organism(s) Saccharolobus shibatae and UniProt Accession B8YB55

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.6 DNA-directed RNA polymerase
IUBMB 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).
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Saccharolobus shibatae
UNIPROT: B8YB55 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus shibatae
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
-
-
multi-subunit RNA polymerase
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nucleotidyltransferase, ribonucleate
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-
-
-
Pol II
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-
-
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ribonucleate nucleotidyltransferase
-
-
-
-
ribonucleate polymerase
-
-
-
-
ribonucleic acid formation factors, C
-
-
-
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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 I
-
-
-
-
RNAP II
-
-
-
-
RNAP III
-
-
-
-
transcriptase
-
-
-
-
additional information
-
RNA polymerase is a member of the iron-sulfur cluster protein family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9014-24-8
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
RNA polymerase is a member of the iron-sulfur cluster protein family and contains one 4Fe-4S cluster binding motif
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RPO1N_SACSH
880
0
99625
Swiss-Prot
-
RPO11_SACSH
92
0
10198
Swiss-Prot
-
RPO5_SACSH
84
0
9671
Swiss-Prot
-
RPO1C_SACSH
395
0
43732
Swiss-Prot
-
RPO12_SACSH
48
0
5597
Swiss-Prot
-
RPO13_SACSH
104
0
12148
Swiss-Prot
-
RPO7_SACSH
180
0
20303
Swiss-Prot
-
RPO8_SACSH
132
0
15120
Swiss-Prot
-
RPO4_SACSH
113
0
12808
Swiss-Prot
-
RPO2_SACSH
1131
0
127409
Swiss-Prot
-
RPO6_SACSH
95
0
10716
Swiss-Prot
-
RPO10_SACSH
66
0
7606
Swiss-Prot
-
RPO3_SACSH
265
0
30142
Swiss-Prot
-
A0A8F5GX69_SACSH
95
0
10716
TrEMBL
-
A0A8F5BXY8_SACSH
84
0
9671
TrEMBL
-
A0A8F5BRZ9_SACSH
1131
0
127409
TrEMBL
-
A0A8F5H0G9_SACSH
104
0
12148
TrEMBL
-
A0A8F5C3S3_SACSH
131
0
14989
TrEMBL
-
A0A8F5C3Q4_SACSH
90
0
10403
TrEMBL
-
A0A8F5C3F3_SACSH
48
0
5597
TrEMBL
-
A0A8F5GYF1_SACSH
131
0
15061
TrEMBL
-
A0A8F5C3P7_SACSH
180
0
20285
TrEMBL
-
A0A8F5BSF0_SACSH
265
0
30159
TrEMBL
-
A0A8F5GXA0_SACSH
113
0
12808
TrEMBL
-
A0A8F5BXM4_SACSH
104
0
12234
TrEMBL
-
A0A8F5BSN0_SACSH
66
0
7606
TrEMBL
-
A0A8F5C3Y8_SACSH
92
0
10198
TrEMBL
-
A0A8F5BY30_SACSH
880
0
99625
TrEMBL
-
A0A8F5BSB7_SACSH
392
0
43390
TrEMBL
-
A0A8F5BXW7_SACSH
1128
0
127053
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
structure analysis and modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
mapping of methylation and acetylation sites, all observed methyl-lysines are on the surface of the enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination
-
crystallization of the enzyme with DNA fragments, crystal growth is optimized using a nanoseeding technique, of the various crystals screened, one diffracts to 4.3 A resolution
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microbatch under oil technique, hanging-drop vapour diffusion technique, crystal structure at 3.35 A resolution
vapour diffusion technique using nanolitre sitting-drop, crystal structures of the DNA-bound and free form of the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Wojtas, M.N.; Abrescia, N.G.
Soaking of DNA into crystals of archaeal RNA polymerase achieved by desalting in droplet
Acta Crystallogr. Sect. F
68
1134-1138
2012
Saccharolobus shibatae
Manually annotated by BRENDA team
Wojtas, M.; Peralta, B.; Ondiviela, M.; Mogni, M.; Bell, S.D.; Abrescia, N.G.
Archaeal RNA polymerase: the influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit
Biochem. Soc. Trans.
39
25-30
2011
Saccharolobus shibatae (B8YB53 and B8YB55 and B8YB54 and B8YB56 and B8YB57 and B8YB58 and B8YB59 and B8YB60 and B8YB61 and B8YB65 and B8YB62 and B8YB63 and B8YB64), Saccharolobus shibatae B12 (B8YB53 and B8YB55 and B8YB54 and B8YB56 and B8YB57 and B8YB58 and B8YB59 and B8YB60 and B8YB61 and B8YB65 and B8YB62 and B8YB63 and B8YB64)
Manually annotated by BRENDA team
Azkargorta, M.; Wojtas, M.; Nicola, A.; Elortza, F.
Lysine methylation mapping of crenarchaeal DNA-directed RNA polymerases by collision-induced and electron-transfer dissociation mass spectrometry
J. Proteome Res.
13
2637-2648
2014
Sulfolobus acidocaldarius, Saccharolobus shibatae
Manually annotated by BRENDA team
Wojtas, M.N.; Mogni, M.; Millet, O.; Bell, S.D.; Abrescia, N.G.
Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA
Nucleic Acids Res.
40
9941-9952
2012
Saccharolobus shibatae (B8YB53), Saccharolobus shibatae B12 (B8YB53)
Manually annotated by BRENDA team
Korkhin, Y.; Unligil, U.M.; Littlefield, O.; Nelson, P.J.; Stuart, D.I.; Sigler, P.B.; Bell, S.D.; Abrescia, N.G.
Evolution of complex RNA polymerases: the complete archaeal RNA polymerase structure
PLoS Biol.
7
e100010
2009
Saccharolobus shibatae (B8YB53 and B8YB55 and B8YB54 and B8YB56 and B8YB57 and B8YB58 and B8YB59 and B8YB60 and B8YB61 and B8YB65 and B8YB62 and B8YB63 and B8YB64), Saccharolobus shibatae, Saccharolobus shibatae B12 (B8YB53 and B8YB55 and B8YB54 and B8YB56 and B8YB57 and B8YB58 and B8YB59 and B8YB60 and B8YB61 and B8YB65 and B8YB62 and B8YB63 and B8YB64)
Manually annotated by BRENDA team