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Genome polyprotein

 G8FGE2_9FLAV            Unreviewed;      3414 AA.
G8FGE2; M4WQV0;
25-JAN-2012, integrated into UniProtKB/TrEMBL.
25-JAN-2012, sequence version 1.
20-DEC-2017, entry version 51.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Tick-borne encephalitis virus.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; tick-borne encephalitis virus group.
NCBI_TaxID=11084 {ECO:0000313|EMBL:AEQ77280.1, ECO:0000313|Proteomes:UP000128307};
[1] {ECO:0000313|EMBL:AEQ77280.1, ECO:0000313|Proteomes:UP000128307}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Irkutsk-12 {ECO:0000313|EMBL:AEQ77280.1};
PubMed=22828779; DOI=10.1007/s00705-012-1412-x;
Kulakova N.V., Andaev E.I., Belikov S.I.;
"Tick-borne encephalitis virus in Eastern Siberia: complete genome
characteristics.";
Arch. Virol. 157:2253-2255(2012).
[2] {ECO:0000313|EMBL:AGI19261.2, ECO:0000313|Proteomes:UP000098425}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Zabaikalye 68B-00 {ECO:0000313|EMBL:AGI19261.2};
Adelshin R.V., Borisova T.I., Sidorova E.A., Nagibina O.A.,
Karan L.S., Andaev E.I.;
"Molecular genetic characteristics of tick-borne encephalitis virus
from Zabaikalsky region.";
Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:AIK20544.1, ECO:0000313|Proteomes:UP000132884}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Sakhalin_6-11 {ECO:0000313|EMBL:AIK20544.1};
Sidorova E.A., Borisova T.I., Adelshin R.V., Karan L.S.,
Vershinin E.A., Tatarnikov S.A., Andaev E.I., Balakhonov S.V.;
"Tick-borne encephalitis virus isolation from mosquitoes pool
(Sakhalin Island).";
Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000256|SAAS:SAAS00892720}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000256|SAAS:SAAS00368577}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000256|SAAS:SAAS00368620}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000256|SAAS:SAAS00232292}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{ECO:0000256|SAAS:SAAS00445805}.
-!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
in which each of the Xaa can be either Arg or Lys and Yaa can be
either Ser or Ala. {ECO:0000256|SAAS:SAAS00232385}.
-!- SUBCELLULAR LOCATION: Host cytoplasm
{ECO:0000256|SAAS:SAAS00937464}. Host endoplasmic reticulum
membrane {ECO:0000256|SAAS:SAAS00944756}; Peripheral membrane
protein {ECO:0000256|SAAS:SAAS00944756}; Lumenal side
{ECO:0000256|SAAS:SAAS00944756}. Host nucleus
{ECO:0000256|SAAS:SAAS00892522}. Secreted
{ECO:0000256|SAAS:SAAS00944768}. Virion membrane
{ECO:0000256|SAAS:SAAS00944678}; Multi-pass membrane protein
{ECO:0000256|SAAS:SAAS00944678}.
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EMBL; JN003209; AEQ77280.1; -; Genomic_RNA.
EMBL; KC422663; AGI19261.2; -; Genomic_RNA.
EMBL; KF826916; AIK20544.1; -; Genomic_RNA.
Proteomes; UP000098425; Genome.
Proteomes; UP000128307; Genome.
Proteomes; UP000132884; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
4: Predicted;
Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00445756};
ATP-binding {ECO:0000256|SAAS:SAAS00058020};
Capsid protein {ECO:0000256|SAAS:SAAS00969288};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000098425,
ECO:0000313|Proteomes:UP000128307, ECO:0000313|Proteomes:UP000132884};
Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3,
ECO:0000256|SAAS:SAAS00139753};
Fusion of virus membrane with host endosomal membrane
{ECO:0000256|SAAS:SAAS00489633};
Fusion of virus membrane with host membrane
{ECO:0000256|SAAS:SAAS00489633};
Helicase {ECO:0000256|SAAS:SAAS00058020};
Host cytoplasm {ECO:0000256|SAAS:SAAS00936979};
Host endoplasmic reticulum {ECO:0000256|SAAS:SAAS00944771};
Host membrane {ECO:0000256|SAAS:SAAS00445977};
Host nucleus {ECO:0000256|SAAS:SAAS00892445};
Host-virus interaction {ECO:0000256|SAAS:SAAS00445756,
ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00892696};
Hydrolase {ECO:0000256|SAAS:SAAS00058020,
ECO:0000256|SAAS:SAAS00462397};
Inhibition of host innate immune response by virus
{ECO:0000256|SAAS:SAAS00892696};
Inhibition of host interferon signaling pathway by virus
{ECO:0000256|SAAS:SAAS00892696};
Inhibition of host STAT2 by virus {ECO:0000256|SAAS:SAAS00892696};
Membrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAAS:SAAS00445977, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4,
ECO:0000256|SAAS:SAAS00940329};
Methyltransferase {ECO:0000256|SAAS:SAAS00817755};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00058020};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
Protease {ECO:0000256|SAAS:SAAS00462397};
RNA-binding {ECO:0000256|SAAS:SAAS00076745};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Secreted {ECO:0000256|SAAS:SAAS00944674};
Serine protease {ECO:0000256|SAAS:SAAS00462397};
Transferase {ECO:0000256|SAAS:SAAS00510600,
ECO:0000256|SAAS:SAAS00817755};
Transmembrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995};
Viral immunoevasion {ECO:0000256|SAAS:SAAS00892696};
Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489633};
Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00969288};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00445995,
ECO:0000256|SAAS:SAAS00489633};
Zinc {ECO:0000256|PIRSR:PIRSR003817-4}.
TRANSMEM 101 119 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 728 749 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 756 776 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1162 1181 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1229 1248 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1296 1317 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1329 1348 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1383 1401 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1455 1480 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2160 2183 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2195 2223 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2243 2259 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2346 2363 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2369 2387 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2433 2451 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1357 1487 FLAVIVIRUS_NS2B.
{ECO:0000259|PROSITE:PS51527}.
DOMAIN 1490 1669 Peptidase S7.
{ECO:0000259|PROSITE:PS51528}.
DOMAIN 1675 1831 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1841 2000 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2512 2776 MRNA cap 0-1 NS5-type MT.
{ECO:0000259|PROSITE:PS51591}.
DOMAIN 3040 3189 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
COILED 2779 2799 {ECO:0000256|SAM:Coils}.
ACT_SITE 1543 1543 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1567 1567 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1627 1627 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
METAL 2950 2950 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2954 2954 Zinc 1; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 2959 2959 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2962 2962 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3224 3224 Zinc 2; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 3240 3240 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3359 3359 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
DISULFID 283 310 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 340 396 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 354 385 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 372 401 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 466 570 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 587 618 {ECO:0000256|PIRSR:PIRSR003817-3}.
SEQUENCE 3414 AA; 377878 MW; 87F8A1532044912A CRC64;
MARKAILKGK GGGPPRRVSK ETAKKTRQSR VQMPNGLVLM RMMGILWHAI AGTARSPVLK
SFWNSVPLKQ ATAALRKIKK AVSTLMVGLQ RRGKKRSTTD WMGWLLVTVL LGVTLAATVR
KEGDGTTVIR AEGKDAATQV RVENGTCVIL ATDMGSWCDD SLSYECVTID QGEEPVDVDC
FCRNVDGVYL EYGRCGKQEG SRSRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW
VWKNKLLALA VVAVVWLTVE SVVTRVAIVV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
VTLVLELGGC VTITAEGKPS MDVWLDSIYQ ENPAKTREYC LHAKLSDTKV AARCPTMGPA
ALAEEHQSGT VCKRDQSDRG WGNHCGLFGK GSIVTCVKVA CEAKKKATGH VYDANKIVYT
VKVEPHTGDY VAANETHSGR KTASFTVSSE KTILTMGDYG DVSLLCRVAS GVDLAQTVIL
ELDKTLEHLP TAWQVHRDWF NDLALPWKHE GAQQWNNAER LVEFGAPHAV KMDVYNLGDQ
TGVLLKSLAG VPVAHIDGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFAWKRTPTD
SGHDTVVMEV TFSGTKPCRI PVRAVAHGSP DVNVAMLITP NPTIENNGGG FIEMQLPPGD
NIIYVGELSH QWFQKGSSIG RVFQKTRKGI ERLTVIGEHA WDFGSTGGFL TSVGKALHTV
LGGAFNSIFG GVGFLPKLLL GVALAWLGLN MRNPTMSMSF LLAGGLVLAM TLGVGADVGC
AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETPGALAS AIKETFEEGN CGIVPQNRLE
MAMWRSAVTE LNLALAEGDA NLTVVVDKLD PTDYRGGVPG LLKKGKDIKV SWKSWGQSMI
WSIPEAPRRF MVGTEGGNEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE PTHECDTGVM
GAAVKNGMAV HTDQSLWMKS VKNDTGTYIV ELLVTDLRNC SWPASHTIDN AEVVDSELFL
PASLAGPRSW YNRIPGYAEQ VKGPWKYSPI RVTREECPGT KVTISADCDK RGASVRSTTE
SGKVIPEWCC RTCALPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP
GIVALFVVLE YVIRRRPATG TAVVWGGVVV LALLVTGMVK IESLVRYVVA VGITFHLELG
PEIVALTLLQ AVFELRVGLL SAFALRRGLT VREMVTIYFL LLVLELGLPG ESLEGLWEWG
DALAMGALIF RACTAEGKAG VGLLLMALMT QRDLVTVHYG LVIFLGVASA CSVWRLIRGH
REQKGLSWIV PLAGLMGGGG SGIRLLAFWE LSTHRGRRSF SEPLTVVGVM LTLAGGMMRH
TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWHP ELVNEGGGVS LRVRQDSMGN
FHLTELEKEE RVMAFWLLAG LAASAFHWSG ILGVMGLWTL SEMMRSARRS DLVFSGQGGH
ERGDRPFEVR DGVYRIFSPG LLWGQRQVGV GYGFKGVLHT MWHVTRGAAL SINDAVAGPY
WADVKEDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH QCQPGELLLD TGRRMGAVPI
DLAKGTSGSP ILNAQGAVVG LYGNGLKTNE TYVSSIAQGE VEKSRPNLPQ AVVGTGWTAK
GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP
AVSDQQVGGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
ENKCALVLMT ATPPGKSEPF PESNGAITSE EKQIPEGEWR DGFDWITEYE GRTAWFVPSI
AKGGVIARTL RQKGKSVICL NSKTFEKDYT RVRDEKPDFV VTTDISEMGA NLDVSRVIDG
RTNIKPEEVD GRVELTGTRR VTTASAAQRR GRVGRHEGRT DEYIYSGQCD DDDSGLVQWK
EAQILLDNIT TLRGPVATFY GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH
VAANVSSVTS RSWTWEGPEE NAVDEANGDL VTFRSPNGAE RTLRPVWRDA RMFREGRDIR
EFVAYASGRR SIGDVLTGMS GVPELLRHRC VSALDVFYTL MHEEPGSRAM RMAERDAPEA
FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS LALLWAGGVS YGNMAGVALI
FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLERTKA DLSTVLWSEQ
EEPRSWGEWT NIDIQPARSW GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ASGAQAMRDL
GGGTPFFGVA GHVMSLGVVS LVGATPTSLV VGVGLAAFHL AIVVSGLEAE LTQRAHKVFF
SAMVRNPMVD GDVINPFGEG ETKPALYERK MSLVLAVVLC LMAVVMNRTV ASITEASAVG
LAAAGQLLRP EVDTLWTMPV ACGLSGVVRG SLWGFLPLGH RLWLRASGSR RGGSEGDTLG
DLWKQRLNSC TKEEFFVYRR TGILETERDR ARELLRKGET NMGLAVSRGT AKLAWLEERG
YATLKGEVVD LGCGRGGWSY YAASRPAVMS VKAYTIGGKG HETPKMVTSL GWNLIKFRAG
MDVFSMQPHR ADTIMCDIGE SSPDAAVEGE RTRRVILLME QWKNRNPTAA CVFKVLAPYR
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAVTGN IVNSVNIQSR KLLARFGDQR
GPTRVPELDL GTGTRCVVLA EDRVREKDVQ ERIRALKEQY GETWHVDGEH PYRTWQYWGS
YRTAPTGSAA SLINGVVKLL SWPWNAREDV VRMAMTDTTA FGQQRVFKEK VDTKAQEPQP
GTKVIMRAVN DWILERLVQK SKPRMCSKEE FIAKVKSNAA LGAWSDEQNR WSNAKEAVED
PVFWQLVDEE RERHLAGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
LGFLNEDHWA SRESSGAGVE GISLNYLGWH LKKLSTLEGG LFYADDTAGW DTKVTNADLE
DEEQILRYME GEHRQLAATI MQKAYHAKVV KVARPSRDGG CIMDVITRRD QRGSGQVVTY
ALNTLTNIKV QLIRMMEGEG VIEASDAHNP RLIRVERWLK EHGEERLGRM LVSGDDCVVR
PIDDRFGKAL YFLNDMAKTR KDIGEWEHSV GFSGWEEVPF CSHHFHELVM KDGRALVVPC
RDQDELVGRA RVSPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA ICSAVPVDWV
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKE RVAEWRDIPY LPKAHDMLCS
SLVGRKERAE WAKNIWGAVE KVRKMIGPEK FRDYLSCMDR HDLHWELRLE SSII


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abx109372 Polyclonal Rabbit Rhinovirus A serotype 89 Genome polyprotein Antibody 100 μg
abx107303 Polyclonal Rabbit Rhinovirus A serotype 89 Genome polyprotein Antibody (FITC) 100 μg
PAB15962 Cricket paralysis virus CrPV Genome polyprotein polyclonal antibody 50 ug
29-197 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science Laboratory in RIKEN. 0.1 mg
28-702 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.05 mg
28-673 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science Laboratory in RIKEN. 0.1 mg
28-654 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.05 mg
28-655 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.1 mg
60B399a Polyclonal Antibodies: polyprotein-(C-terminal); Specificity: polyprotein-(C-terminal) ; Application: IHC 0.1mg
60B395 Polyclonal Antibodies: polyprotein-(N-terminal); Specificity: polyprotein-(N-terminal) ; Application: IHC 0.1mg


 

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