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 POLG_BVDVN              Reviewed;        3988 AA.
P19711;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
10-MAY-2017, entry version 153.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=N-terminal protease;
Short=N-pro;
EC=3.4.22.-;
AltName: Full=Autoprotease p20;
Contains:
RecName: Full=Capsid protein C;
Contains:
RecName: Full=E(rns) glycoprotein;
AltName: Full=gp44/48;
Contains:
RecName: Full=Envelope glycoprotein E1;
AltName: Full=gp33;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=gp55;
Contains:
RecName: Full=p7;
Contains:
RecName: Full=Non-structural protein 2-3;
Contains:
RecName: Full=Cysteine protease NS2;
EC=3.4.22.-;
AltName: Full=Non-structural protein 2;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.113;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=Non-structural protein 5A;
Short=NS5A;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=NS5B;
Bovine viral diarrhea virus (isolate NADL) (BVDV) (Mucosal disease
virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Pestivirus.
NCBI_TaxID=11100;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2838957; DOI=10.1016/0042-6822(88)90672-1;
Collett M.S., Larson R., Gold C., Strick D., Anderson D.K.,
Purchio A.F.;
"Molecular cloning and nucleotide sequence of the pestivirus bovine
viral diarrhea virus.";
Virology 165:191-199(1988).
[2]
GENOMIC ORGANIZATION.
PubMed=2838958; DOI=10.1016/0042-6822(88)90673-3;
Collett M.S., Larson R., Belzer S.K., Retzel E.;
"Proteins encoded by bovine viral diarrhea virus: the genomic
organization of a pestivirus.";
Virology 165:200-208(1988).
[3]
PROTEIN SEQUENCE OF 2363-2376; 2427-2441; 2774-2788 AND 3270-3284, AND
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=9188600;
Xu J., Mendez E., Caron P.R., Lin C., Murcko M.A., Collett M.S.,
Rice C.M.;
"Bovine viral diarrhea virus NS3 serine proteinase: polyprotein
cleavage sites, cofactor requirements, and molecular model of an
enzyme essential for pestivirus replication.";
J. Virol. 71:5312-5322(1997).
[4]
SUBCELLULAR LOCATION.
PubMed=10355762;
Weiland F., Weiland E., Unger G., Saalmuller A., Thiel H.-J.;
"Localization of pestiviral envelope proteins E(rns) and E2 at the
cell surface and on isolated particles.";
J. Gen. Virol. 80:1157-1165(1999).
[5]
ROLE OF BOVINE LOW-DENSITY-LIPOPROTEIN RECEPTOR IN VIRUS ATTACHMENT TO
HOST CELL.
PubMed=10535997; DOI=10.1073/pnas.96.22.12766;
Agnello V., Abel G., Elfahal M., Knight G.B., Zhang Q.X.;
"Hepatitis C virus and other flaviviridae viruses enter cells via low
density lipoprotein receptor.";
Proc. Natl. Acad. Sci. U.S.A. 96:12766-12771(1999).
[6]
INTERACTION OF E(RNS) WITH CELL SURFACE GLYCOSAMINOGLYCANS.
PubMed=10644844;
Iqbal M., Flick-Smith H., McCauley J.W.;
"Interactions of bovine viral diarrhoea virus glycoprotein E(rns) with
cell surface glycosaminoglycans.";
J. Gen. Virol. 81:451-459(2000).
[7]
FUNCTION OF NS2-3.
STRAIN=Isolate NADL Jiv 90(-);
PubMed=14963137; DOI=10.1128/JVI.78.5.2414-2425.2004;
Agapov E.V., Murray C.L., Frolov I., Qu L., Myers T.M., Rice C.M.;
"Uncleaved NS2-3 is required for production of infectious bovine viral
diarrhea virus.";
J. Virol. 78:2414-2425(2004).
[8]
INTERACTION OF VIRUS WITH BOVINE CD46.
PubMed=14747544; DOI=10.1128/JVI.78.4.1792-1799.2004;
Maurer K., Krey T., Moennig V., Thiel H.-J., Ruemenapf T.;
"CD46 is a cellular receptor for bovine viral diarrhea virus.";
J. Virol. 78:1792-1799(2004).
[9]
FUNCTION OF E1/E2 HETERODIMER.
PubMed=16051874; DOI=10.1128/JVI.79.16.10826-10829.2005;
Lecot S., Belouzard S., Dubuisson J., Rouille Y.;
"Bovine viral diarrhea virus entry is dependent on clathrin-mediated
endocytosis.";
J. Virol. 79:10826-10829(2005).
-!- FUNCTION: Initial binding to target cell probably involves
interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are
responsible of cell attachment with CD46 and subsequent fusion
after internalization of the virion by endocytosis (Probable).
{ECO:0000305}.
-!- FUNCTION: P7 forms a leader sequence to properly orient NS2 in the
membrane. {ECO:0000250}.
-!- FUNCTION: Uncleaved NS2-3 is required for production of infectious
virus.
-!- FUNCTION: NS2 protease seems to play a vital role in viral RNA
replication control and in the pathogenicity of the virus.
-!- FUNCTION: NS3 displays three enzymatic activities: serine
protease, NTPase and RNA helicase.
-!- FUNCTION: NS4A is a cofactor for the NS3 protease activity.
{ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+)
and (-) genome.
-!- CATALYTIC ACTIVITY: Leu is conserved at position P1 for all four
cleavage sites. Alanine is found at position P1' of the NS4A-NS4B
cleavage site, whereas serine is found at position P1' of the NS3-
NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: The E(rns) glycoprotein is found as a homodimer;
disulfide-linked. The E1 and E2 envelope glycoproteins form
disulfide-linked homodimers as well as heterodimers.
{ECO:0000250}.
-!- INTERACTION:
F1MUM9:ADAR (xeno); NbExp=6; IntAct=EBI-9350731, EBI-9350738;
Q95J56:DNAJC14 (xeno); NbExp=2; IntAct=EBI-9612504, EBI-9612178;
P68103:EEF1A1 (xeno); NbExp=6; IntAct=EBI-9350549, EBI-352178;
Q32PH0:TRAPPC9 (xeno); NbExp=7; IntAct=EBI-9350549, EBI-9522367;
-!- SUBCELLULAR LOCATION: E(rns) glycoprotein: Host membrane;
Peripheral membrane protein. Virion membrane; Peripheral membrane
protein {ECO:0000305}. Note=The C-terminus membrane anchor of Erns
represents an amphipathic helix embedded in plane into the
membrane. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Host cell surface.
-!- SUBCELLULAR LOCATION: Cysteine protease NS2: Host membrane
{ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane
protein {ECO:0000255|PROSITE-ProRule:PRU01029}.
-!- PTM: The E(rns) glycoprotein is heavily glycosylated.
{ECO:0000250}.
-!- PTM: The viral RNA of pestiviruses is expressed as a single
polyprotein which undergoes post-translational proteolytic
processing resulting in the production of at least eleven
individual proteins. The N-terminal protease cleaves itself from
the nascent polyprotein autocatalytically and thereby generates
the N-terminus of the adjacent viral capsid protein C (By
similarity). {ECO:0000250}.
-!- PTM: Cleavage between E2 and p7 is partial. {ECO:0000250}.
-!- PTM: Cleavage between NS2 and NS3 is partial.
-!- MISCELLANEOUS: BVDV is divided in two types: cytopathic and non-
cytopathic. Both types of viruses can be found in animals
suffering from mucosal disease, as a cytopathic BVDV can develop
from a non-cytopathic virus within the infected animal by
deletions, mutations or insertions. Both types express uncleaved
NS2-3, but cytopathic strains also express NS3. The cytopathic
NADL strain contains an insertion (Jiv 90) that potentiate the
partial cleavage of NS2-3. Removal of this insertion in the NADL
Jiv 90(-) strain results in a non-cytopathic strain in which NS2-3
remains uncleaved.
-!- SIMILARITY: Belongs to the pestivirus polyprotein family.
{ECO:0000305}.
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EMBL; M31182; AAA42854.1; -; Genomic_RNA.
PIR; A29198; GNWVBV.
RefSeq; NP_040937.1; NC_001461.1.
PDB; 1S48; X-ray; 3.00 A; A=3340-3948.
PDB; 1S49; X-ray; 3.00 A; A=3340-3948.
PDB; 1S4F; X-ray; 3.00 A; A/B/C/D=3348-3948.
PDB; 4ILD; X-ray; 3.27 A; A/B=781-1030.
PDB; 4JNT; X-ray; 4.09 A; A/B=693-1030.
PDBsum; 1S48; -.
PDBsum; 1S49; -.
PDBsum; 1S4F; -.
PDBsum; 4ILD; -.
PDBsum; 4JNT; -.
DisProt; DP00675; -.
ProteinModelPortal; P19711; -.
SMR; P19711; -.
IntAct; P19711; 59.
DrugBank; DB04137; Guanosine-5'-Triphosphate.
MEROPS; C74.001; -.
GeneID; 1489735; -.
KEGG; vg:1489735; -.
OrthoDB; VOG090000UX; -.
BRENDA; 2.7.7.48; 925.
EvolutionaryTrace; P19711; -.
Proteomes; UP000002317; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
GO; GO:0044161; C:host cell cytoplasmic vesicle; IDA:AgBase.
GO; GO:0044177; C:host cell Golgi apparatus; IDA:AgBase.
GO; GO:0033650; C:host cell mitochondrion; IDA:AgBase.
GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IDA:AgBase.
GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:CAFA.
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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IDA:CAFA.
GO; GO:1990814; F:DNA/DNA annealing activity; IDA:CAFA.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IDA:CAFA.
GO; GO:0033592; F:RNA strand annealing activity; IDA:CAFA.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0043489; P:RNA stabilization; IDA:CAFA.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR021824; Capsid-C_pestivirus.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR032843; Jiv.
InterPro; IPR022120; NS2.
InterPro; IPR030399; NS2_C74.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008751; Peptidase_C53.
InterPro; IPR032521; Pestivirus_E2.
InterPro; IPR000280; Pestivirus_NS3_S31.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
InterPro; IPR001568; RNase_T2-like.
InterPro; IPR033130; RNase_T2_His_AS_2.
Pfam; PF11889; DUF3409; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF14901; Jiv90; 1.
Pfam; PF05550; Peptidase_C53; 1.
Pfam; PF12387; Peptidase_C74; 1.
Pfam; PF05578; Peptidase_S31; 1.
Pfam; PF16329; Pestivirus_E2; 1.
Pfam; PF00998; RdRP_3; 1.
PRINTS; PR00729; CDVENDOPTASE.
ProDom; PD003091; Peptidase_C53; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55895; SSF55895; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS00531; RNASE_T2_2; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Direct protein sequencing; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host membrane; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host IRF3 by virus;
Inhibition of host RLR pathway by virus; Ion channel; Ion transport;
Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease;
Reference proteome; RNA-directed RNA polymerase; Serine protease;
Thiol protease; Transferase; Transmembrane; Transmembrane helix;
Transport; Viral attachment to host cell; Viral immunoevasion;
Viral ion channel; Viral penetration into host cytoplasm;
Viral RNA replication; Virion; Virus endocytosis by host;
Virus entry into host cell.
CHAIN 1 168 N-terminal protease. {ECO:0000250}.
/FTId=PRO_0000038024.
CHAIN 169 270 Capsid protein C. {ECO:0000250}.
/FTId=PRO_0000038025.
CHAIN 271 497 E(rns) glycoprotein. {ECO:0000250}.
/FTId=PRO_0000038026.
CHAIN 498 659 Envelope glycoprotein E1. {ECO:0000250}.
/FTId=PRO_0000038027.
CHAIN 660 1066 Envelope glycoprotein E2. {ECO:0000250}.
/FTId=PRO_0000038028.
CHAIN 1067 1136 p7. {ECO:0000250}.
/FTId=PRO_0000038029.
CHAIN 1137 2362 Non-structural protein 2-3.
/FTId=PRO_0000038030.
CHAIN 1137 1679 Cysteine protease NS2.
/FTId=PRO_0000038031.
CHAIN 1680 2362 Serine protease NS3.
/FTId=PRO_0000038032.
CHAIN 2363 2426 Non-structural protein 4A. {ECO:0000250}.
/FTId=PRO_0000038033.
CHAIN 2427 2773 Non-structural protein 4B. {ECO:0000250}.
/FTId=PRO_0000038034.
CHAIN 2774 3269 Non-structural protein 5A. {ECO:0000250}.
/FTId=PRO_0000038035.
CHAIN 3270 3988 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000038036.
TRANSMEM 1144 1164 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1189 1209 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1217 1237 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1247 1267 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1281 1301 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1360 1380 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1658 1678 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
DOMAIN 1 168 Peptidase C53.
DOMAIN 1441 1679 Peptidase C74. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
DOMAIN 1680 1853 Peptidase S31. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
DOMAIN 1892 2050 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 2068 2233 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 3608 3731 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
ACT_SITE 22 22 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 49 49 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 69 69 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 1447 1447 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1461 1461 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1512 1512 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1748 1748 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
ACT_SITE 1785 1785 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
ACT_SITE 1842 1842 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
SITE 168 169 Cleavage; by autolysis. {ECO:0000250}.
SITE 270 271 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 497 498 Cleavage.
SITE 659 660 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1066 1067 Cleavage; by host signal peptidase;
partial. {ECO:0000250}.
SITE 1136 1137 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1679 1680 Cleavage; partial; cysteine protease NS2.
SITE 2362 2363 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 2426 2427 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 2773 2774 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 3269 3270 Cleavage; by serine protease NS3.
{ECO:0000250}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 487 487 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 597 597 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 809 809 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 878 878 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 922 922 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 990 990 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1357 1357 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1419 1419 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1451 1451 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1803 1803 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2224 2224 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2307 2307 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2584 2584 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2772 2772 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2981 2981 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3778 3778 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3867 3867 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3883 3883 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
STRAND 784 786 {ECO:0000244|PDB:4ILD}.
STRAND 793 795 {ECO:0000244|PDB:4ILD}.
STRAND 797 799 {ECO:0000244|PDB:4ILD}.
STRAND 803 805 {ECO:0000244|PDB:4ILD}.
STRAND 807 809 {ECO:0000244|PDB:4ILD}.
STRAND 811 814 {ECO:0000244|PDB:4ILD}.
STRAND 817 820 {ECO:0000244|PDB:4ILD}.
STRAND 828 835 {ECO:0000244|PDB:4ILD}.
STRAND 837 839 {ECO:0000244|PDB:4ILD}.
STRAND 842 850 {ECO:0000244|PDB:4ILD}.
STRAND 863 866 {ECO:0000244|PDB:4ILD}.
STRAND 869 875 {ECO:0000244|PDB:4ILD}.
TURN 878 880 {ECO:0000244|PDB:4ILD}.
STRAND 882 886 {ECO:0000244|PDB:4ILD}.
STRAND 894 899 {ECO:0000244|PDB:4ILD}.
STRAND 902 906 {ECO:0000244|PDB:4ILD}.
STRAND 910 914 {ECO:0000244|PDB:4ILD}.
STRAND 916 922 {ECO:0000244|PDB:4ILD}.
STRAND 925 928 {ECO:0000244|PDB:4ILD}.
STRAND 934 936 {ECO:0000244|PDB:4ILD}.
STRAND 939 941 {ECO:0000244|PDB:4ILD}.
STRAND 946 951 {ECO:0000244|PDB:4ILD}.
STRAND 954 960 {ECO:0000244|PDB:4ILD}.
STRAND 969 971 {ECO:0000244|PDB:4ILD}.
STRAND 987 993 {ECO:0000244|PDB:4ILD}.
TURN 1005 1007 {ECO:0000244|PDB:4ILD}.
STRAND 1014 1022 {ECO:0000244|PDB:4ILD}.
HELIX 3364 3372 {ECO:0000244|PDB:1S48}.
STRAND 3373 3376 {ECO:0000244|PDB:1S48}.
STRAND 3382 3384 {ECO:0000244|PDB:1S48}.
STRAND 3388 3392 {ECO:0000244|PDB:1S48}.
STRAND 3402 3404 {ECO:0000244|PDB:1S48}.
HELIX 3406 3414 {ECO:0000244|PDB:1S48}.
HELIX 3419 3421 {ECO:0000244|PDB:1S48}.
STRAND 3422 3427 {ECO:0000244|PDB:1S48}.
HELIX 3431 3440 {ECO:0000244|PDB:1S48}.
HELIX 3453 3462 {ECO:0000244|PDB:1S48}.
HELIX 3467 3469 {ECO:0000244|PDB:1S48}.
TURN 3470 3472 {ECO:0000244|PDB:1S4F}.
HELIX 3478 3481 {ECO:0000244|PDB:1S48}.
TURN 3482 3484 {ECO:0000244|PDB:1S48}.
HELIX 3501 3504 {ECO:0000244|PDB:1S48}.
HELIX 3507 3518 {ECO:0000244|PDB:1S48}.
STRAND 3527 3531 {ECO:0000244|PDB:1S48}.
STRAND 3535 3537 {ECO:0000244|PDB:1S48}.
HELIX 3539 3543 {ECO:0000244|PDB:1S48}.
STRAND 3549 3551 {ECO:0000244|PDB:1S48}.
STRAND 3555 3558 {ECO:0000244|PDB:1S48}.
HELIX 3563 3570 {ECO:0000244|PDB:1S48}.
HELIX 3572 3575 {ECO:0000244|PDB:1S48}.
HELIX 3586 3588 {ECO:0000244|PDB:1S48}.
HELIX 3591 3593 {ECO:0000244|PDB:1S48}.
HELIX 3594 3603 {ECO:0000244|PDB:1S48}.
STRAND 3605 3612 {ECO:0000244|PDB:1S48}.
STRAND 3615 3617 {ECO:0000244|PDB:1S4F}.
HELIX 3618 3621 {ECO:0000244|PDB:1S48}.
HELIX 3624 3637 {ECO:0000244|PDB:1S48}.
HELIX 3640 3642 {ECO:0000244|PDB:1S48}.
HELIX 3643 3652 {ECO:0000244|PDB:1S48}.
STRAND 3655 3660 {ECO:0000244|PDB:1S48}.
STRAND 3665 3668 {ECO:0000244|PDB:1S48}.
HELIX 3679 3699 {ECO:0000244|PDB:1S48}.
HELIX 3703 3705 {ECO:0000244|PDB:1S48}.
HELIX 3706 3709 {ECO:0000244|PDB:1S48}.
STRAND 3710 3715 {ECO:0000244|PDB:1S48}.
STRAND 3718 3724 {ECO:0000244|PDB:1S48}.
HELIX 3725 3741 {ECO:0000244|PDB:1S48}.
STRAND 3750 3753 {ECO:0000244|PDB:1S4F}.
STRAND 3756 3759 {ECO:0000244|PDB:1S48}.
HELIX 3760 3762 {ECO:0000244|PDB:1S48}.
STRAND 3768 3775 {ECO:0000244|PDB:1S48}.
STRAND 3780 3785 {ECO:0000244|PDB:1S48}.
HELIX 3788 3797 {ECO:0000244|PDB:1S48}.
STRAND 3802 3804 {ECO:0000244|PDB:1S48}.
STRAND 3808 3810 {ECO:0000244|PDB:1S48}.
HELIX 3811 3822 {ECO:0000244|PDB:1S48}.
HELIX 3826 3837 {ECO:0000244|PDB:1S48}.
STRAND 3846 3854 {ECO:0000244|PDB:1S48}.
HELIX 3856 3864 {ECO:0000244|PDB:1S48}.
HELIX 3868 3870 {ECO:0000244|PDB:1S48}.
STRAND 3871 3874 {ECO:0000244|PDB:1S48}.
HELIX 3876 3882 {ECO:0000244|PDB:1S48}.
HELIX 3885 3888 {ECO:0000244|PDB:1S48}.
HELIX 3896 3908 {ECO:0000244|PDB:1S48}.
STRAND 3910 3912 {ECO:0000244|PDB:1S48}.
TURN 3915 3918 {ECO:0000244|PDB:1S48}.
HELIX 3920 3926 {ECO:0000244|PDB:1S48}.
STRAND 3935 3939 {ECO:0000244|PDB:1S48}.
SEQUENCE 3988 AA; 449163 MW; 4474212F338661B8 CRC64;
MELITNELLY KTYKQKPVGV EEPVYDQAGD PLFGERGAVH PQSTLKLPHK RGERDVPTNL
ASLPKRGDCR SGNSRGPVSG IYLKPGPLFY QDYKGPVYHR APLELFEEGS MCETTKRIGR
VTGSDGKLYH IYVCIDGCII IKSATRSYQR VFRWVHNRLD CPLWVTTCSD TKEEGATKKK
TQKPDRLERG KMKIVPKESE KDSKTKPPDA TIVVEGVKYQ VRKKGKTKSK NTQDGLYHNK
NKPQESRKKL EKALLAWAII AIVLFQVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH
GIWPEKICTG VPSHLATDIE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW
ILVMNRTQAN LTEGQPPREC AVTCRYDRAS DLNVVTQARD SPTPLTGCKK GKNFSFAGIL
MRGPCNFEIA ASDVLFKEHE RISMFQDTTL YLVDGLTNSL EGARQGTAKL TTWLGKQLGI
LGKKLENKSK TWFGAYAASP YCDVDRKIGY IWYTKNCTPA CLPKNTKIVG PGKFGTNAED
GKILHEMGGH LSEVLLLSLV VLSDFAPETA SVMYLILHFS IPQSHVDVMD CDKTQLNLTV
ELTTAEVIPG SVWNLGKYVC IRPNWWPYET TVVLAFEEVS QVVKLVLRAL RDLTRIWNAA
TTTAFLVCLV KIVRGQMVQG ILWLLLITGV QGHLDCKPEF SYAIAKDERI GQLGAEGLTT
TWKEYSPGMK LEDTMVIAWC EDGKLMYLQR CTRETRYLAI LHTRALPTSV VFKKLFDGRK
QEDVVEMNDN FEFGLCPCDA KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCTSFNMDTL
ATTVVRTYRR SKPFPHRQGC ITQKNLGEDL HNCILGGNWT CVPGDQLLYK GGSIESCKWC
GYQFKESEGL PHYPIGKCKL ENETGYRLVD STSCNREGVA IVPQGTLKCK IGKTTVQVIA
MDTKLGPMPC RPYEIISSEG PVEKTACTFN YTKTLKNKYF EPRDSYFQQY MLKGEYQYWF
DLEVTDHHRD YFAESILVVV VALLGGRYVL WLLVTYMVLS EQKALGIQYG SGEVVMMGNL
LTHNNIEVVT YFLLLYLLLR EESVKKWVLL LYHILVVHPI KSVIVILLMI GDVVKADSGG
QEYLGKIDLC FTTVVLIVIG LIIARRDPTI VPLVTIMAAL RVTELTHQPG VDIAVAVMTI
TLLMVSYVTD YFRYKKWLQC ILSLVSAVFL IRSLIYLGRI EMPEVTIPNW RPLTLILLYL
ISTTIVTRWK VDVAGLLLQC VPILLLVTTL WADFLTLILI LPTYELVKLY YLKTVRTDTE
RSWLGGIDYT RVDSIYDVDE SGEGVYLFPS RQKAQGNFSI LLPLIKATLI SCVSSKWQLI
YMSYLTLDFM YYMHRKVIEE ISGGTNIISR LVAALIELNW SMEEEESKGL KKFYLLSGRL
RNLIIKHKVR NETVASWYGE EEVYGMPKIM TIIKASTLSK SRHCIICTVC EGREWKGGTC
PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGMCSR CQGKHRRFEM DREPKSARYC
AECNRLHPAE EGDFWAESSM LGLKITYFAL MDGKVYDITE WAGCQRVGIS PDTHRVPCHI
SFGSRMPFRQ EYNGFVQYTA RGQLFLRNLP VLATKVKMLM VGNLGEEIGN LEHLGWILRG
PAVCKKITEH EKCHINILDK LTAFFGIMPR GTTPRAPVRF PTSLLKVRRG LETAWAYTHQ
GGISSVDHVT AGKDLLVCDS MGRTRVVCQS NNRLTDETEY GVKTDSGCPD GARCYVLNPE
AVNISGSKGA VVHLQKTGGE FTCVTASGTP AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV
GKNEESKPTK IMSGIQTVSK NRADLTEMVK KITSMNRGDF KQITLATGAG KTTELPKAVI
EEIGRHKRVL VLIPLRAAAE SVYQYMRLKH PSISFNLRIG DMKEGDMATG ITYASYGYFC
QMPQPKLRAA MVEYSYIFLD EYHCATPEQL AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG
QKHPIEEFIA PEVMKGEDLG SQFLDIAGLK IPVDEMKGNM LVFVPTRNMA VEVAKKLKAK
GYNSGYYYSG EDPANLRVVT SQSPYVIVAT NAIESGVTLP DLDTVIDTGL KCEKRVRVSS
KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK PGRYYRSQET ATGSKDYHYD LLQAQRYGIE
DGINVTKSFR EMNYDWSLYE EDSLLITQLE ILNNLLISED LPAAVKNIMA RTDHPEPIQL
AYNSYEVQVP VLFPKIRNGE VTDTYENYSF LNARKLGEDV PVYIYATEDE DLAVDLLGLD
WPDPGNQQVV ETGKALKQVT GLSSAENALL VALFGYVGYQ ALSKRHVPMI TDIYTIEDQR
LEDTTHLQYA PNAIKTDGTE TELKELASGD VEKIMGAISD YAAGGLEFVK SQAEKIKTAP
LFKENAEAAK GYVQKFIDSL IENKEEIIRY GLWGTHTALY KSIAARLGHE TAFATLVLKW
LAFGGESVSD HVKQAAVDLV VYYVMNKPSF PGDSETQQEG RRFVASLFIS ALATYTYKTW
NYHNLSKVVE PALAYLPYAT SALKMFTPTR LESVVILSTT IYKTYLSIRK GKSDGLLGTG
ISAAMEILSQ NPVSVGISVM LGVGAIAAHN AIESSEQKRT LLMKVFVKNF LDQAATDELV
KENPEKIIMA LFEAVQTIGN PLRLIYHLYG VYYKGWEAKE LSERTAGRNL FTLIMFEAFE
LLGMDSQGKI RNLSGNYILD LIYGLHKQIN RGLKKMVLGW APAPFSCDWT PSDERIRLPT
DNYLRVETRC PCGYEMKAFK NVGGKLTKVE ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE
IKPVAKLEGQ VEHYYKGVTA KIDYSKGKML LATDKWEVEH GVITRLAKRY TGVGFNGAYL
GDEPNHRALV ERDCATITKN TVQFLKMKKG CAFTYDLTIS NLTRLIELVH RNNLEEKEIP
TATVTTWLAY TFVNEDVGTI KPVLGERVIP DPVVDINLQP EVQVDTSEVG ITIIGRETLM
TTGVTPVLEK VEPDASDNQN SVKIGLDEGN YPGPGIQTHT LTEEIHNRDA RPFIMILGSR
NSISNRAKTA RNINLYTGND PREIRDLMAA GRMLVVALRD VDPELSEMVD FKGTFLDREA
LEALSLGQPK PKQVTKEAVR NLIEQKKDVE IPNWFASDDP VFLEVALKND KYYLVGDVGE
LKDQAKALGA TDQTRIIKEV GSRTYAMKLS SWFLKASNKQ MSLTPLFEEL LLRCPPATKS
NKGHMASAYQ LAQGNWEPLG CGVHLGTIPA RRVKIHPYEA YLKLKDFIEE EEKKPRVKDT
VIREHNKWIL KKIRFQGNLN TKKMLNPGKL SEQLDREGRK RNIYNHQIGT IMSSAGIRLE
KLPIVRAQTD TKTFHEAIRD KIDKSENRQN PELHNKLLEI FHTIAQPTLK HTYGEVTWEQ
LEAGVNRKGA AGFLEKKNIG EVLDSEKHLV EQLVRDLKAG RKIKYYETAI PKNEKRDVSD
DWQAGDLVVE KRPRVIQYPE AKTRLAITKV MYNWVKQQPV VIPGYEGKTP LFNIFDKVRK
EWDSFNEPVA VSFDTKAWDT QVTSKDLQLI GEIQKYYYKK EWHKFIDTIT DHMTEVPVIT
ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT MMYGFCESTG VPYKSFNRVA RIHVCGDDGF
LITEKGLGLK FANKGMQILH EAGKPQKITE GEKMKVAYRF EDIEFCSHTP VPVRWSDNTS
SHMAGRDTAV ILSKMATRLD SSGERGTTAY EKAVAFSFLL MYSWNPLVRR ICLLVLSQQP
ETDPSKHATY YYKGDPIGAY KDVIGRNLSE LKRTGFEKLA NLNLSLSTLG VWTKHTSKRI
IQDCVAIGKE EGNWLVKPDR LISSKTGHLY IPDKGFTLQG KHYEQLQLRT ETNPVMGVGT
ERYKLGPIVN LLLRRLKILL MTAVGVSS


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