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RNA-directed RNA polymerase subunit beta (EC 2.7.7.48) (RNA replicase beta chain) (RNA-directed RNA polymerase subunit II)

 RDRP_BPQBE              Reviewed;         589 AA.
P14647; D0U1F4; D0U1F8; D0U1G6; G4WZR0; G4WZR4; Q8LTE0;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
15-FEB-2017, sequence version 2.
23-MAY-2018, entry version 75.
RecName: Full=RNA-directed RNA polymerase subunit beta;
EC=2.7.7.48 {ECO:0000269|PubMed:22245970};
AltName: Full=RNA replicase beta chain;
AltName: Full=RNA-directed RNA polymerase subunit II {ECO:0000303|PubMed:816798};
Escherichia phage Qbeta (Bacteriophage Q-beta).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Leviviridae; Allolevivirus.
NCBI_TaxID=39803;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2538637; DOI=10.1016/0022-2836(89)90319-7;
Mills D.R., Priano C., Dimauro P., Binderow B.D.;
"Q-beta replicase: mapping the functional domains of an RNA-dependent
RNA polymerase.";
J. Mol. Biol. 205:751-764(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Mekler P.;
Thesis (1981), University of Zurich, Switzerland.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=14667253; DOI=10.1186/1471-2148-3-24;
Bacher J.M., Bull J.J., Ellington A.D.;
"Evolution of phage with chemically ambiguous proteomes.";
BMC Evol. Biol. 3:24-24(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=QB_1 {ECO:0000312|EMBL:ACY07225.1},
QB_2 {ECO:0000312|EMBL:ACY07229.1}, and
QB_ancestral {ECO:0000312|EMBL:ACY07237.1};
PubMed=19956760; DOI=10.1371/journal.pgen.1000742;
Domingo-Calap P., Cuevas J.M., Sanjuan R.;
"The fitness effects of random mutations in single-stranded DNA and
RNA bacteriophages.";
PLoS Genet. 5:E1000742-E1000742(2009).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Qbeta_1_FR, and Qbeta_2_FR {ECO:0000312|EMBL:AEQ25547.1};
PubMed=21967437; DOI=10.1111/j.1558-5646.2011.01339.x;
Domingo-Calap P., Sanjuan R.;
"Experimental evolution of RNA versus DNA viruses.";
Evolution 65:2987-2994(2011).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Anc;
PubMed=25056887; DOI=10.1128/JVI.01127-14;
Kashiwagi A., Sugawara R., Sano-Tsushima F., Kumagai T., Yomo T.;
"Contribution of silent mutations to thermal adaptation of RNA
bacteriophage Qbeta.";
J. Virol. 88:11459-11468(2014).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-23.
PubMed=1247542; DOI=10.1016/0005-2787(76)90067-8;
Weber H.;
"The binding site for coat protein on bacteriophage Q-beta RNA.";
Biochim. Biophys. Acta 418:175-183(1976).
[8]
FUNCTION, AND SUBUNIT.
PubMed=58611;
Kondo M.;
"Structure and function of RNA replicase of bacteriophage Qbeta.";
Arch. Int. Physiol. Biochim. 83:909-948(1975).
[9]
FUNCTION, AND SUBUNIT.
PubMed=816798;
Carmichael G.G., Landers T.A., Weber K.;
"Immunochemical analysis of the functions of the subunits of phage
Qbeta ribonucleic acid replicase.";
J. Biol. Chem. 251:2744-2748(1976).
[10]
FUNCTION, AND SUBUNIT.
PubMed=6358207;
Guerrier-Takada C., Subramanian A.R., Cole P.E.;
"The activity of discrete fragments of ribosomal protein S1 in Q beta
replicase function.";
J. Biol. Chem. 258:13649-13652(1983).
[11]
CONSTRUCT TO PRODUCE VIRAL CATALYTIC CORE.
PubMed=16781472; DOI=10.1263/jbb.101.421;
Kita H., Cho J., Matsuura T., Nakaishi T., Taniguchi I., Ichikawa T.,
Shima Y., Urabe I., Yomo T.;
"Functional Qbeta replicase genetically fusing essential subunits EF-
Ts and EF-Tu with beta-subunit.";
J. Biosci. Bioeng. 101:421-426(2006).
[12]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF VIRAL CATALYTIC CORE,
FUNCTION, AND SUBUNIT.
PubMed=20534494; DOI=10.1073/pnas.1003015107;
Kidmose R.T., Vasiliev N.N., Chetverin A.B., Andersen G.R.,
Knudsen C.R.;
"Structure of the Qbeta replicase, an RNA-dependent RNA polymerase
consisting of viral and host proteins.";
Proc. Natl. Acad. Sci. U.S.A. 107:10884-10889(2010).
[13]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF VIRAL CATALYTIC CORE IN
COMPLEX WITH CALCIUM, FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF
LYS-78; ARG-153; ARG-164; LYS-214; ARG-220; ASP-274; SER-279; TYR-357;
ASP-359; ASP-360; GLU-395; TYR-411 AND ARG-413.
PubMed=20798060; DOI=10.1073/pnas.1006559107;
Takeshita D., Tomita K.;
"Assembly of Q{beta} viral RNA polymerase with host translational
elongation factors EF-Tu and -Ts.";
Proc. Natl. Acad. Sci. U.S.A. 107:15733-15738(2010).
[14]
X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF VIRAL CATALYTIC CORE IN
COMPLEX WITH CALCIUM, FUNCTION, COFACTOR, SUBUNIT, MUTAGENESIS OF
HIS-168; ARG-241; PHE-329; TYR-357; TYR-511 AND ASN-549, AND CATALYTIC
ACTIVITY.
PubMed=22245970; DOI=10.1038/nsmb.2204;
Takeshita D., Tomita K.;
"Molecular basis for RNA polymerization by Qbeta replicase.";
Nat. Struct. Mol. Biol. 19:229-237(2012).
[15]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF VIRAL CATALYTIC CORE IN
COMPLEX WITH CALCIUM, FUNCTION, COFACTOR, AND SUBUNIT.
PubMed=22884418; DOI=10.1016/j.str.2012.07.004;
Takeshita D., Yamashita S., Tomita K.;
"Mechanism for template-independent terminal adenylation activity of
Qbeta replicase.";
Structure 20:1661-1669(2012).
[16]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-589 OF THE REPLICASE
COMPLEX, FUNCTION, AND SUBUNIT.
PubMed=25122749; DOI=10.1093/nar/gku745;
Takeshita D., Yamashita S., Tomita K.;
"Molecular insights into replication initiation by Qbeta replicase
using ribosomal protein S1.";
Nucleic Acids Res. 42:10809-10822(2014).
[17] {ECO:0000244|PDB:4R71}
X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF THE REPLICASE COMPLEX,
FUNCTION, RNA-BINDING, SUBUNIT, AND MUTAGENESIS OF ARG-132; ARG-133;
LYS-134; LYS-137; GLU-345; ASP-348 AND ASP-350.
PubMed=26578560; DOI=10.1093/nar/gkv1212;
Gytz H., Mohr D., Seweryn P., Yoshimura Y., Kutlubaeva Z., Dolman F.,
Chelchessa B., Chetverin A.B., Mulder F.A., Brodersen D.E.,
Knudsen C.R.;
"Structural basis for RNA-genome recognition during bacteriophage
Qbeta replication.";
Nucleic Acids Res. 43:10893-10906(2015).
-!- FUNCTION: This is the catalytic subunit of the viral RNA-dependent
RNA polymerase complex. This complex is involved in viral RNA
replication that produces (+)-stranded genomes via a
complementary, (-)-stranded intermediate. Binds RNA cooperatively
with the host ribosomal protein S1. {ECO:0000269|PubMed:20534494,
ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749,
ECO:0000269|PubMed:26578560, ECO:0000269|PubMed:58611,
ECO:0000269|PubMed:6358207, ECO:0000269|PubMed:816798}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539,
ECO:0000269|PubMed:22245970}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418};
Note=Binds 2 Mg(2+) per subunit, Ca(2+) is used in crystallization
to prevent RNA polymerase activity. {ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418};
-!- SUBUNIT: Homodimer; the replicase complex can dimerize. Part of
the viral RNA-dependent RNA polymerase complex, the other subunits
are the host ribosomal protein S1, EF-Tu and EF-Ts. S1 is needed
for the initiation of genomic RNA (+)-strand replication.
{ECO:0000269|PubMed:1247542, ECO:0000269|PubMed:20534494,
ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749,
ECO:0000269|PubMed:58611, ECO:0000269|PubMed:6358207,
ECO:0000269|PubMed:816798}.
-!- INTERACTION:
P0A6P1:tsf (xeno); NbExp=2; IntAct=EBI-9010000, EBI-301164;
P0CE47:tufA (xeno); NbExp=2; IntAct=EBI-9010000, EBI-301077;
-!- MISCELLANEOUS: In order to produce high amounts of RNA polymerase
catalytic core, a fusion protein consisting of tsf-tufB-replicase
with a cleavable linker between tufB and the viral replicase
subunit is frequently used. {ECO:0000269|PubMed:16781472,
ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749}.
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EMBL; X14764; CAA32872.1; -; mRNA.
EMBL; AY099114; AAM33128.1; -; Genomic_RNA.
EMBL; GQ153928; ACY07225.1; -; Genomic_RNA.
EMBL; GQ153929; ACY07229.1; -; Genomic_RNA.
EMBL; AB971354; BAP18765.1; -; Genomic_RNA.
EMBL; JF719735; AEQ25543.1; -; Genomic_RNA.
EMBL; JF719736; AEQ25547.1; -; Genomic_RNA.
EMBL; GQ153931; ACY07237.1; -; Genomic_RNA.
EMBL; M24876; AAA50307.1; -; Genomic_RNA.
PIR; S03340; RRBPBQ.
PDB; 3AGP; X-ray; 2.80 A; A=1-589.
PDB; 3AGQ; X-ray; 3.22 A; A=1-589.
PDB; 3AVT; X-ray; 2.61 A; A=1-589.
PDB; 3AVU; X-ray; 2.91 A; A=1-589.
PDB; 3AVV; X-ray; 3.12 A; A=1-589.
PDB; 3AVW; X-ray; 2.60 A; A=1-589.
PDB; 3AVX; X-ray; 2.41 A; A=1-589.
PDB; 3AVY; X-ray; 2.62 A; A=1-589.
PDB; 3MMP; X-ray; 2.50 A; F/G=1-589.
PDB; 3VNU; X-ray; 3.20 A; A=1-589.
PDB; 3VNV; X-ray; 2.60 A; A=1-589.
PDB; 4FWT; X-ray; 3.20 A; A=1-589.
PDB; 4Q7J; X-ray; 2.90 A; C/G=2-589.
PDB; 4R71; X-ray; 3.21 A; B/D=1-589.
PDBsum; 3AGP; -.
PDBsum; 3AGQ; -.
PDBsum; 3AVT; -.
PDBsum; 3AVU; -.
PDBsum; 3AVV; -.
PDBsum; 3AVW; -.
PDBsum; 3AVX; -.
PDBsum; 3AVY; -.
PDBsum; 3MMP; -.
PDBsum; 3VNU; -.
PDBsum; 3VNV; -.
PDBsum; 4FWT; -.
PDBsum; 4Q7J; -.
PDBsum; 4R71; -.
SMR; P14647; -.
DIP; DIP-59375N; -.
IntAct; P14647; 2.
PRIDE; P14647; -.
OrthoDB; VOG090000A5; -.
Proteomes; UP000185268; Genome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR007096; RNA-dir_Rpol_phage_catalytic.
InterPro; IPR005093; RNArep_beta.
Pfam; PF03431; RNA_replicase_B; 1.
PROSITE; PS50522; RDRP_PHAGE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Magnesium; Metal-binding;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
RNA-binding; RNA-directed RNA polymerase; Transferase;
Viral RNA replication.
CHAIN 1 589 RNA-directed RNA polymerase subunit beta.
/FTId=PRO_0000164855.
DOMAIN 259 391 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
METAL 274 274 Magnesium 1.
{ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418}.
METAL 274 274 Magnesium 2.
{ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418}.
METAL 359 359 Magnesium 1.
{ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418}.
METAL 359 359 Magnesium 2.
{ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418}.
METAL 360 360 Magnesium 1.
{ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418}.
METAL 360 360 Magnesium 2.
{ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970,
ECO:0000269|PubMed:22884418}.
VARIANT 71 71 L -> F (in strain:QB_1).
{ECO:0000269|PubMed:19956760}.
VARIANT 130 130 M -> I (in strain: QB_ancestral, QB_1,
QB_2, Qbeta_1_FR and Qbeta_2_FR).
{ECO:0000269|PubMed:19956760,
ECO:0000269|PubMed:21967437}.
VARIANT 198 198 I -> T. {ECO:0000269|PubMed:2538637,
ECO:0000269|Ref.2}.
VARIANT 251 251 L -> R (in strain:QB_1 and Qbeta_2_FR).
{ECO:0000269|PubMed:19956760,
ECO:0000269|PubMed:21967437}.
VARIANT 418 418 S -> G (in strain:QB_1 and Qbeta_2_FR).
{ECO:0000269|PubMed:19956760}.
VARIANT 500 500 D -> G (in strain:QB_2 and Qbeta_2_FR).
{ECO:0000269|PubMed:19956760,
ECO:0000269|PubMed:21967437}.
MUTAGEN 78 78 K->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 132 132 R->M: Complete loss of infectivity; when
associated with M-133.
{ECO:0000269|PubMed:26578560}.
MUTAGEN 133 133 R->M: Complete loss of infectivity; when
associated with M-132.
{ECO:0000269|PubMed:26578560}.
MUTAGEN 134 134 K->A: Complete loss of infectivity.
{ECO:0000269|PubMed:26578560}.
MUTAGEN 137 137 K->M: Complete loss of infectivity.
{ECO:0000269|PubMed:26578560}.
MUTAGEN 153 153 R->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 164 164 R->A: 80% loss of RNA polymerase
activity. {ECO:0000269|PubMed:20798060}.
MUTAGEN 168 168 H->A: 80% loss of RNA polymerase
activity. {ECO:0000269|PubMed:22245970}.
MUTAGEN 214 214 K->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 220 220 R->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 241 241 R->A: Decreased initiation of RNA
polymerase activity.
{ECO:0000269|PubMed:22245970}.
MUTAGEN 274 274 D->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 279 279 S->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 329 329 F->A: Decreased initiation of RNA
polymerase activity.
{ECO:0000269|PubMed:22245970}.
MUTAGEN 345 345 E->A: Almost complete loss of
infectivity.
{ECO:0000269|PubMed:26578560}.
MUTAGEN 348 348 D->A: 80% loss of infectivity.
{ECO:0000269|PubMed:26578560}.
MUTAGEN 350 350 D->A: 95% loss of infectivity.
{ECO:0000269|PubMed:26578560}.
MUTAGEN 357 357 Y->A: Decreased initiation of RNA
polymerase activity.
{ECO:0000269|PubMed:20798060,
ECO:0000269|PubMed:22245970}.
MUTAGEN 359 359 D->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 360 360 D->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 395 395 E->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 411 411 Y->A: 60% loss of RNA polymerase
activity. {ECO:0000269|PubMed:20798060}.
MUTAGEN 413 413 R->A: Loss of RNA polymerase activity.
{ECO:0000269|PubMed:20798060}.
MUTAGEN 511 511 Y->A: 50% loss of RNA polymerase
activity. {ECO:0000269|PubMed:22245970}.
MUTAGEN 549 549 N->A: 25% loss of RNA polymerase
activity. {ECO:0000269|PubMed:22245970}.
MUTAGEN 549 549 N->G: 50% loss of RNA polymerase
activity. {ECO:0000269|PubMed:22245970}.
STRAND 5 7 {ECO:0000244|PDB:4R71}.
HELIX 9 19 {ECO:0000244|PDB:3AVX}.
HELIX 29 40 {ECO:0000244|PDB:3AVX}.
STRAND 48 50 {ECO:0000244|PDB:3VNU}.
HELIX 51 53 {ECO:0000244|PDB:3AVX}.
HELIX 63 75 {ECO:0000244|PDB:3AVX}.
TURN 76 78 {ECO:0000244|PDB:3AVX}.
STRAND 84 86 {ECO:0000244|PDB:3AVV}.
HELIX 90 110 {ECO:0000244|PDB:3AVX}.
STRAND 116 118 {ECO:0000244|PDB:3AVX}.
HELIX 123 139 {ECO:0000244|PDB:3AVX}.
HELIX 145 151 {ECO:0000244|PDB:3AVX}.
STRAND 160 162 {ECO:0000244|PDB:4Q7J}.
HELIX 164 166 {ECO:0000244|PDB:3AVX}.
HELIX 169 174 {ECO:0000244|PDB:3AVX}.
STRAND 177 179 {ECO:0000244|PDB:3AVX}.
TURN 181 183 {ECO:0000244|PDB:3AVX}.
HELIX 184 191 {ECO:0000244|PDB:3AVX}.
STRAND 200 203 {ECO:0000244|PDB:3AVX}.
STRAND 205 212 {ECO:0000244|PDB:3AVX}.
STRAND 215 217 {ECO:0000244|PDB:3AVV}.
STRAND 220 224 {ECO:0000244|PDB:3AVX}.
HELIX 227 244 {ECO:0000244|PDB:3AVX}.
HELIX 245 247 {ECO:0000244|PDB:3AVX}.
HELIX 255 267 {ECO:0000244|PDB:3AVX}.
STRAND 270 273 {ECO:0000244|PDB:3AVX}.
STRAND 275 277 {ECO:0000244|PDB:3VNV}.
HELIX 278 281 {ECO:0000244|PDB:3AVX}.
HELIX 284 288 {ECO:0000244|PDB:3AVX}.
HELIX 293 302 {ECO:0000244|PDB:3AVX}.
STRAND 306 308 {ECO:0000244|PDB:3AVX}.
STRAND 310 312 {ECO:0000244|PDB:3AGQ}.
STRAND 314 316 {ECO:0000244|PDB:3AVX}.
STRAND 318 320 {ECO:0000244|PDB:3AVX}.
STRAND 325 327 {ECO:0000244|PDB:3AVW}.
HELIX 328 346 {ECO:0000244|PDB:3AVX}.
HELIX 351 353 {ECO:0000244|PDB:3AVX}.
STRAND 355 357 {ECO:0000244|PDB:3AVX}.
STRAND 360 364 {ECO:0000244|PDB:3AVX}.
HELIX 365 367 {ECO:0000244|PDB:3AVX}.
HELIX 368 377 {ECO:0000244|PDB:3AVX}.
HELIX 384 386 {ECO:0000244|PDB:3AVX}.
STRAND 388 396 {ECO:0000244|PDB:3AVX}.
STRAND 399 402 {ECO:0000244|PDB:3AVX}.
HELIX 419 433 {ECO:0000244|PDB:3AVX}.
STRAND 434 437 {ECO:0000244|PDB:3AGP}.
HELIX 441 451 {ECO:0000244|PDB:3AVX}.
HELIX 456 460 {ECO:0000244|PDB:3AVX}.
STRAND 465 467 {ECO:0000244|PDB:3AVV}.
STRAND 469 474 {ECO:0000244|PDB:3AVX}.
TURN 476 478 {ECO:0000244|PDB:3AVX}.
STRAND 483 485 {ECO:0000244|PDB:3AVX}.
STRAND 488 500 {ECO:0000244|PDB:3AVX}.
HELIX 505 520 {ECO:0000244|PDB:3AVX}.
HELIX 536 542 {ECO:0000244|PDB:3MMP}.
HELIX 543 545 {ECO:0000244|PDB:3AVX}.
STRAND 554 566 {ECO:0000244|PDB:3AVX}.
SEQUENCE 589 AA; 65531 MW; 8C02DB50F7202DEF CRC64;
MSKTASSRNS LSAQLRRAAN TRIEVEGNLA LSIANDLLLA YGQSPFNSEA ECISFSPRFD
GTPDDFRINY LKAEIMSKYD DFSLGIDTEA VAWEKFLAAE AECALTNARL YRPDYSEDFN
FSLGESCIHM ARRKIAKLIG DVPSVEGMLR HCRFSGGATT TNNRSYGHPS FKFALPQACT
PRALKYVLAL RASTHFDIRI SDISPFNKAV TVPKNSKTDR CIAIEPGWNM FFQLGIGGIL
RDRLRCWGID LNDQTINQRR AHEGSVTNNL ATVDLSAASD SISLALCELL LPPGWFEVLM
DLRSPKGRLP DGSVVTYEKI SSMGNGYTFE LESLIFASLA RSVCEILDLD SSEVTVYGDD
IILPSCAVPA LREVFKYVGF TTNTKKTFSE GPFRESCGKH YYSGVDVTPF YIRHRIVSPA
DLILVLNNLY RWATIDGVWD PRAHSVYLKY RKLLPKQLQR NTIPDGYGDG ALVGSVLINP
FAKNRGWIRY VPVITDHTRD RERAELGSYL YDLFSRCLSE SNDGLPLRGP SGCDSADLFA
IDQLICRSNP TKISRSTGKF DIQYIACSSR VLAPYGVFQG TKVASLHEA


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EIAAB35812 C128,DNA-directed RNA polymerase III 127.6 kDa polypeptide,DNA-directed RNA polymerase III subunit B,DNA-directed RNA polymerase III subunit RPC2,Homo sapiens,Human,POLR3B,RNA polymerase III subunit C
EIAAB35792 DNA-directed RNA polymerase II 140 kDa polypeptide,DNA-directed RNA polymerase II subunit B,DNA-directed RNA polymerase II subunit RPB2,Homo sapiens,Human,POLR2B,RNA polymerase II subunit 2,RNA polyme
EIAAB35735 A194,DNA-directed RNA polymerase I largest subunit,DNA-directed RNA polymerase I subunit A,DNA-directed RNA polymerase I subunit RPA1,Polr1a,Rat,Rattus norvegicus,RNA polymerase I 194 kDa subunit,RNA
EIAAB35737 DNA-directed RNA polymerase I largest subunit,DNA-directed RNA polymerase I subunit A,DNA-directed RNA polymerase I subunit RPA1,Mouse,Mus musculus,Polr1a,RNA polymerase I 194 kDa subunit,RNA polymera
EIAAB35808 DNA-directed RNA polymerase III largest subunit,DNA-directed RNA polymerase III subunit A,DNA-directed RNA polymerase III subunit RPC1,Homo sapiens,Human,POLR3A,RNA polymerase III 155 kDa subunit,RNA
EIAAB35791 DNA-directed RNA polymerase II 140 kDa polypeptide,DNA-directed RNA polymerase II subunit B,DNA-directed RNA polymerase II subunit RPB2,Mouse,Mus musculus,Polr2b,RNA polymerase II subunit 2,RNA polyme
EIAAB35813 C128,DNA-directed RNA polymerase III 127.6 kDa polypeptide,DNA-directed RNA polymerase III subunit B,DNA-directed RNA polymerase III subunit RPC2,Mouse,Mus musculus,Polr3b,RNA polymerase III subunit C
EIAAB35793 DNA-directed RNA polymerase II 33 kDa polypeptide,DNA-directed RNA polymerase II subunit C,DNA-directed RNA polymerase II subunit RPB3,Mouse,Mus musculus,Polr2c,RNA polymerase II subunit 3,RNA polymer
EIAAB35832 Bos taurus,Bovine,DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide,DNA-directed RNA polymerase III subunit H,DNA-directed RNA polymerase III subunit RPC8,POLR3H,RNA polymerase III subunit
EIAAB35833 DNA-directed RNA polymerase III subunit H,DNA-directed RNA polymerase III subunit RPC8,Homo sapiens,Human,KIAA1665,POLR3H,RNA polymerase III subunit 22.9 kDa subunit,RNA polymerase III subunit C8,RPC2
EIAAB35809 DNA-directed RNA polymerase III subunit K,DNA-directed RNA polymerase III subunit RPC10,Homo sapiens,hRPC11,HsC11p,Human,My010,POLR3K,RNA polymerase III 12.5 kDa subunit,RNA polymerase III subunit C10
EIAAB35787 DNA-directed RNA polymerase II subunit J-1,DNA-directed RNA polymerase II subunit RPB11-a,Homo sapiens,Human,POLR2J,POLR2J1,RNA polymerase II 13.3 kDa subunit,RNA polymerase II subunit B11-a,RPB11a
EIAAB35750 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Homo sapiens,Human,PAF53,POLR1E,PRAF1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB35749 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Mouse,Mus musculus,Paf53,Polr1e,Praf1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB35786 DNA-directed RNA polymerase II subunit J,DNA-directed RNA polymerase II subunit RPB11,Mouse,Mus musculus,Polr2j,RNA polymerase II 13.3 kDa subunit,RNA polymerase II subunit B11,RPB14,Rpo2-4
EIAAB35815 DNA-directed RNA polymerase III subunit C,DNA-directed RNA polymerase III subunit RPC3,Homo sapiens,Human,POLR3C,RNA polymerase III 62 kDa subunit,RNA polymerase III subunit C3,RPC62
EIAAB35825 DNA-directed RNA polymerase III subunit F,DNA-directed RNA polymerase III subunit RPC6,Homo sapiens,Human,POLR3F,RNA polymerase III 39 kDa subunit,RNA polymerase III subunit C6,RPC39
EIAAB35802 DNA-directed RNA polymerase II subunit I,DNA-directed RNA polymerase II subunit RPB9,Homo sapiens,Human,POLR2I,RNA polymerase II 14.5 kDa subunit,RNA polymerase II subunit B9,RPB14.5
EIAAB35827 DNA-directed RNA polymerase III subunit G,DNA-directed RNA polymerase III subunit RPC7,Homo sapiens,Human,POLR3G,RNA polymerase III 32 kDa subunit,RNA polymerase III subunit C7,RPC32
EIAAB35796 DNA-directed RNA polymerase II subunit D,DNA-directed RNA polymerase II subunit RPB4,Homo sapiens,Human,POLR2D,RNA polymerase II 16 kDa subunit,RNA polymerase II subunit B4,RPB16
EIAAB35811 DNA-directed RNA polymerase III subunit K,DNA-directed RNA polymerase III subunit RPC10,Mouse,Mus musculus,Polr3k,RNA polymerase III subunit C10,RNA polymerase III subunit C11,RPC11


 

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