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 RPOA_PRRSR              Reviewed;        3960 AA.
Q9WJB2; Q80KX0; Q80KX1; Q9WJB3;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 2.
25-OCT-2017, entry version 112.
RecName: Full=Replicase polyprotein 1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Nsp1;
EC=3.4.22.-;
Contains:
RecName: Full=Nsp1-alpha papain-like cysteine proteinase;
EC=3.4.22.-;
AltName: Full=PCP1-alpha;
Contains:
RecName: Full=Nsp1-beta papain-like cysteine proteinase;
EC=3.4.22.-;
AltName: Full=PCP1-beta;
Contains:
RecName: Full=Nsp2 cysteine proteinase;
EC=3.4.19.12;
EC=3.4.22.-;
AltName: Full=CP2;
Short=CP;
Contains:
RecName: Full=Non-structural protein 3;
Short=Nsp3;
Contains:
RecName: Full=3C-like serine proteinase;
Short=3CLSP;
EC=3.4.21.-;
AltName: Full=Nsp4;
Contains:
RecName: Full=Non-structural protein 5-6-7;
Short=Nsp5-6-7;
Contains:
RecName: Full=Non-structural protein 5;
Short=Nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=Nsp6;
Contains:
RecName: Full=Non-structural protein 7-alpha;
Short=Nsp7-alpha;
Contains:
RecName: Full=Non-structural protein 7-beta;
Short=Nsp7-beta;
Contains:
RecName: Full=Non-structural protein 8;
Short=Nsp8;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=Nsp9;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=Nsp10;
Contains:
RecName: Full=Non-structural protein 11;
Short=Nsp11;
Contains:
RecName: Full=Non-structural protein 12;
Short=Nsp12;
Name=rep; ORFNames=1a-1b;
Porcine reproductive and respiratory syndrome virus (strain VR-2332)
(PRRSV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae; unclassified Arteriviridae.
NCBI_TaxID=300559;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=9847330;
Nelsen C.J., Murtaugh M.P., Faaberg K.S.;
"Porcine reproductive and respiratory syndrome virus comparison:
divergent evolution on two continents.";
J. Virol. 73:270-280(1999).
[2]
SEQUENCE REVISION.
Murtaugh M.P., Faaberg K.S., Nelsen C.J.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Infectious clone VR-2332;
PubMed=12610145; DOI=10.1128/JVI.77.6.3702-3711.2003;
Nielsen H.S., Liu G., Nielsen J., Oleksiewicz M.B., Botner A.,
Storgaard T., Faaberg K.S.;
"Generation of an infectious clone of VR-2332, a highly virulent North
American-type isolate of porcine reproductive and respiratory syndrome
virus.";
J. Virol. 77:3702-3711(2003).
[4]
FUNCTION OF NSP2.
PubMed=18078692; DOI=10.1016/j.chom.2007.09.014;
Frias-Staheli N., Giannakopoulos N.V., Kikkert M., Taylor S.L.,
Bridgen A., Paragas J., Richt J.A., Rowland R.R., Schmaljohn C.S.,
Lenschow D.J., Snijder E.J., Garcia-Sastre A., Virgin H.W.;
"Ovarian tumor domain-containing viral proteases evade ubiquitin- and
ISG15-dependent innate immune responses.";
Cell Host Microbe 2:404-416(2007).
[5]
FUNCTION (NSP1-ALPHA PAPAIN-LIKE CYSTEINE PROTEINASE), AND SUBCELLULAR
LOCATION (NSP1-ALPHA PAPAIN-LIKE CYSTEINE PROTEINASE).
PubMed=20850164; DOI=10.1016/j.virol.2010.08.025;
Song C., Krell P., Yoo D.;
"Nonstructural protein 1alpha subunit-based inhibition of NF-kappaB
activation and suppression of interferon-beta production by porcine
reproductive and respiratory syndrome virus.";
Virology 407:268-280(2010).
[6]
FUNCTION OF NSP1-ALPHA, FUNCTION OF NSP1-BETA, PROTEOLYTIC PROCESSING
OF POLYPROTEIN, AND PROTEIN SEQUENCE OF 181-190 AND 384-393.
STRAIN=Isolate SD23983;
PubMed=20006994; DOI=10.1016/j.virol.2009.11.033;
Chen Z., Lawson S., Sun Z., Zhou X., Guan X., Christopher-Hennings J.,
Nelson E.A., Fang Y.;
"Identification of two auto-cleavage products of nonstructural protein
1 (nsp1) in porcine reproductive and respiratory syndrome virus
infected cells: nsp1 function as interferon antagonist.";
Virology 398:87-97(2010).
[7]
FUNCTION OF NSP1-ALPHA, AND MUTAGENESIS OF CYS-76; HIS-146 AND
CYS-270.
STRAIN=BJ-4;
PubMed=21438756; DOI=10.1089/dna.2010.1188;
Shi X., Zhang G., Wang L., Li X., Zhi Y., Wang F., Fan J., Deng R.;
"The nonstructural protein 1 papain-like cysteine protease was
necessary for porcine reproductive and respiratory syndrome virus
nonstructural protein 1 to inhibit interferon-beta induction.";
DNA Cell Biol. 30:355-362(2011).
[8]
FUNCTION (NSP1-BETA PAPAIN-LIKE CYSTEINE PROTEINASE).
PubMed=23449802; DOI=10.1128/JVI.02643-12;
Wang R., Nan Y., Yu Y., Zhang Y.J.;
"Porcine reproductive and respiratory syndrome virus Nsp1beta inhibits
interferon-activated JAK/STAT signal transduction by inducing
karyopherin-alpha1 degradation.";
J. Virol. 87:5219-5228(2013).
[9]
TOPOLOGY (NSP2 CYSTEINE PROTEINASE).
PubMed=25768891; DOI=10.1016/j.virol.2015.01.028;
Kappes M.A., Miller C.L., Faaberg K.S.;
"Porcine reproductive and respiratory syndrome virus nonstructural
protein 2 (nsp2) topology and selective isoform integration in
artificial membranes.";
Virology 481:51-62(2015).
-!- FUNCTION: Replicase polyprotein 1ab: contains the activities
necessary for the transcription of negative stranded RNA, leader
RNA, subgenomic mRNAs and progeny virion RNA as well as
proteinases responsible for the cleavage of the polyprotein into
functional products.
-!- FUNCTION: Nsp1: essential for viral subgenomic mRNA synthesis.
{ECO:0000250}.
-!- FUNCTION: Nsp1-alpha papain-like cysteine proteinase: inhibits
host IFN-beta production. Plays a role in the degradation of the
host transcriptional activator CREBBP protein. The degradation of
host CREBBP which is a key component of the IFN enhanceosome is
likely responsible for the inhibition of interferon mediated by
Nsp1-alpha. Participates also in the inhibition of host NF-kappa-B
activation. {ECO:0000250|UniProtKB:Q04561,
ECO:0000269|PubMed:20850164}.
-!- FUNCTION: Nsp1-beta papain-like cysteine proteinase: plays a role
in the inhibition of the interferon-activated JAK/STAT signal
transduction by mediating the ubiquitination and subsequent
proteasomal degradation of host KPNA1.
{ECO:0000269|PubMed:23449802}.
-!- FUNCTION: Nsp2 cysteine proteinase: multifunctional protein that
acts as a viral protease and as a viral antagonist of host immune
response. Cleaves the nsp2/nsp3 site in the viral polyprotein.
Displays deubiquitinating activity that cleaves both ubiquitinated
and ISGylated products and therefore inhibits ubiquitin and ISG15-
dependent host innate immunity. Deubiquitinates also host NFKBIA,
thereby interfering with NFKBIA degradation and impairing
subsequent NF-kappa-B activation. {ECO:0000250|UniProtKB:A0MD28}.
-!- FUNCTION: Non-structural protein 3: plays a role in the inhibition
of the immune response by interacting with host IFITM1. This
interaction leads to the proteasomal degradation of the IFN-
induced antiviral protein IFITM1. {ECO:0000250|UniProtKB:Q04561}.
-!- FUNCTION: 3C-like serine proteinase: Cleaves the majority of
cleavage sites present in the C-terminus of the polyprotein.
Triggers host apoptosis through caspase-3, -8, and -9 activations.
{ECO:0000250|UniProtKB:Q04561}.
-!- FUNCTION: Non-structural protein 5-6-7: Plays a role in the
initial induction of autophagosomes from host reticulum
endoplasmic. {ECO:0000250|UniProtKB:Q04561}.
-!- FUNCTION: RNA-directed RNA polymerase: Responsible for replication
and transcription of the viral RNA genome.
{ECO:0000250|UniProtKB:Q04561}.
-!- FUNCTION: Helicase: Displays RNA and DNA duplex-unwinding
activities with 5' to 3' polarity. {ECO:0000250|UniProtKB:Q04561}.
-!- FUNCTION: Non-structural protein 11: Plays a role in the
inhibition of the secretion of host IL-1beta by the NLRP3
inflammasome through its endonuclease activity.
{ECO:0000250|UniProtKB:Q04561}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBUNIT: Nsp3 interacts with host IFITM1. Nsp9 interacts with host
DDX5. {ECO:0000250|UniProtKB:Q04561}.
-!- SUBCELLULAR LOCATION: Nsp1: Host nucleus. Host cytoplasm
{ECO:0000250|UniProtKB:Q04561}.
-!- SUBCELLULAR LOCATION: Nsp1-alpha papain-like cysteine proteinase:
Host nucleus {ECO:0000269|PubMed:20850164}. Host cytoplasm
{ECO:0000269|PubMed:20850164}.
-!- SUBCELLULAR LOCATION: Nsp1-beta papain-like cysteine proteinase:
Host nucleus {ECO:0000250|UniProtKB:Q04561}.
-!- SUBCELLULAR LOCATION: Nsp2 cysteine proteinase: Host membrane
{ECO:0000269|Ref.2}; Multi-pass membrane protein
{ECO:0000269|Ref.2}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 5-6-7: Host
endoplasmic reticulum {ECO:0000250|UniProtKB:Q04561}. Host
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: 3C-like serine proteinase: Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host cytoplasm
{ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear
region {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Helicase: Host cytoplasm, host perinuclear
region {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=Q9WJB2-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=Q9WJB2-2; Sequence=VSP_032893;
Note=Produced by conventional translation.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane. {ECO:0000250}.
-!- DOMAIN: The OTU-like region is responsible for the
deubiquitinating and deISGylation activities of Nsp2.
{ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. Nsp1 is autocleaved into two subunits,
Nsp1-alpha and Nsp1-beta. There are two alternative pathways for
processing. Either nsp4-5 is cleaved, which represents the major
pathway or the nsp5-6 and nsp6-7 are processed, which represents
the minor pathway. The major pathway occurs when nsp2 acts as
cofactor for nsp4 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the arteriviridae polyprotein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD12125.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAO13192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U87392; AAD12132.2; -; Genomic_RNA.
EMBL; U87392; AAD12125.1; ALT_INIT; Genomic_RNA.
EMBL; AY150564; AAO13191.1; -; Genomic_RNA.
EMBL; AY150564; AAO13192.1; ALT_INIT; Genomic_RNA.
ProteinModelPortal; Q9WJB2; -.
SMR; Q9WJB2; -.
GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; 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:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR031932; Arteri_nsp7a.
InterPro; IPR008743; Arterivirus_Nsp2_C33.
InterPro; IPR023338; Arterivirus_NSP4_peptidase.
InterPro; IPR008741; AV_PCPalpha.
InterPro; IPR025773; AV_PCPbeta.
InterPro; IPR027355; AV_ZBD.
InterPro; IPR008760; EAV_peptidase_S32.
InterPro; IPR037227; EndoU-like.
InterPro; IPR032855; NSP2-B_epitope.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR032785; Pdase_C33_assoc.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF16749; Arteri_nsp7a; 1.
Pfam; PF14757; NSP2-B_epitope; 1.
Pfam; PF14756; Pdase_C33_assoc; 1.
Pfam; PF05410; Peptidase_C31; 1.
Pfam; PF05411; Peptidase_C32; 1.
Pfam; PF05412; Peptidase_C33; 1.
Pfam; PF05579; Peptidase_S32; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF01443; Viral_helicase1; 1.
SUPFAM; SSF142877; SSF142877; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51538; AV_CP; 1.
PROSITE; PS51493; AV_NSP4_PRO; 1.
PROSITE; PS51539; AV_PCP_ALPHA; 1.
PROSITE; PS51540; AV_PCP_BETA; 1.
PROSITE; PS51652; AV_ZBD; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
ATP-binding; Direct protein sequencing; Helicase; Host cytoplasm;
Host endoplasmic reticulum; Host membrane; Host nucleus;
Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host ISG15 by virus;
Inhibition of host NF-kappa-B by virus;
Inhibition of host STAT1 by virus; Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Protease;
Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
Thiol protease; Transferase; Transmembrane; Transmembrane helix;
Viral immunoevasion; Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 3960 Replicase polyprotein 1ab.
/FTId=PRO_0000036696.
CHAIN 1 382 Nsp1. {ECO:0000250}.
/FTId=PRO_0000410829.
CHAIN 1 180 Nsp1-alpha papain-like cysteine
proteinase.
/FTId=PRO_0000036698.
CHAIN 181 383 Nsp1-beta papain-like cysteine
proteinase.
/FTId=PRO_0000036699.
CHAIN 384 1579 Nsp2 cysteine proteinase. {ECO:0000255}.
/FTId=PRO_0000036700.
CHAIN 1580 1809 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000036701.
CHAIN 1810 2013 3C-like serine proteinase. {ECO:0000250}.
/FTId=PRO_0000036702.
CHAIN 2014 2458 Non-structural protein 5-6-7.
{ECO:0000250}.
/FTId=PRO_0000036703.
CHAIN 2014 2183 Non-structural protein 5. {ECO:0000250}.
/FTId=PRO_0000423130.
CHAIN 2184 2199 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000423131.
CHAIN 2200 2348 Non-structural protein 7-alpha.
{ECO:0000250}.
/FTId=PRO_0000423132.
CHAIN 2349 2458 Non-structural protein 7-beta.
{ECO:0000250}.
/FTId=PRO_0000423133.
CHAIN 2459 3143 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000036704.
CHAIN 2459 2503 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000036705.
CHAIN 3144 3584 Helicase. {ECO:0000250}.
/FTId=PRO_0000036706.
CHAIN 3585 3807 Non-structural protein 11. {ECO:0000250}.
/FTId=PRO_0000036707.
CHAIN 3808 3960 Non-structural protein 12. {ECO:0000250}.
/FTId=PRO_0000036708.
TRANSMEM 1266 1286 Helical. {ECO:0000255}.
TRANSMEM 1296 1316 Helical. {ECO:0000255}.
TRANSMEM 1345 1365 Helical. {ECO:0000255}.
TRANSMEM 1368 1388 Helical. {ECO:0000255}.
TRANSMEM 1583 1603 Helical. {ECO:0000255}.
TRANSMEM 1650 1670 Helical. {ECO:0000255}.
TRANSMEM 1685 1705 Helical. {ECO:0000255}.
TRANSMEM 1719 1739 Helical. {ECO:0000255}.
TRANSMEM 2012 2032 Helical. {ECO:0000255}.
TRANSMEM 2060 2080 Helical. {ECO:0000255}.
TRANSMEM 2092 2112 Helical. {ECO:0000255}.
TRANSMEM 2137 2157 Helical. {ECO:0000255}.
TRANSMEM 2164 2184 Helical. {ECO:0000255}.
DOMAIN 69 180 Peptidase C31. {ECO:0000255|PROSITE-
ProRule:PRU00872}.
DOMAIN 263 383 Peptidase C32. {ECO:0000255|PROSITE-
ProRule:PRU00873}.
DOMAIN 428 535 Peptidase C33. {ECO:0000255|PROSITE-
ProRule:PRU00871}.
DOMAIN 1810 2013 Peptidase S32. {ECO:0000255|PROSITE-
ProRule:PRU00826}.
DOMAIN 2889 3023 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 3144 3207 AV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
DOMAIN 3264 3416 (+)RNA virus helicase ATP-binding.
DOMAIN 3417 3545 (+)RNA virus helicase C-terminal.
ZN_FING 8 28 C4-type; atypical.
NP_BIND 3292 3299 ATP. {ECO:0000250}.
REGION 69 182 PCP1-alpha.
REGION 263 382 PCP1-beta.
REGION 426 513 OTU-like.
REGION 1266 1388 HD1.
REGION 1583 1745 HD2.
REGION 2036 2157 HD3.
COMPBIAS 808 930 Pro-rich.
COMPBIAS 2329 2344 Pro-rich.
ACT_SITE 76 76 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872}.
ACT_SITE 146 146 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872}.
ACT_SITE 270 270 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 339 339 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 437 437 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 506 506 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 1848 1848 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1873 1873 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1927 1927 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
METAL 3150 3150 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3153 3153 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3163 3163 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3168 3168 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3171 3171 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3173 3173 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3175 3175 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3177 3177 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3184 3184 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3186 3186 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3193 3193 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3196 3196 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
SITE 180 181 Cleavage; by autolysis.
SITE 383 384 Cleavage; by autolysis.
SITE 1579 1580 Cleavage; by CP2. {ECO:0000255}.
SITE 1809 1810 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2013 2014 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2183 2184 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2199 2200 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2348 2349 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2458 2459 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3143 3144 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3194 3194 Involved in mRNA transcription process.
{ECO:0000250}.
SITE 3584 3585 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3807 3808 Cleavage; by 3CLSP. {ECO:0000250}.
VAR_SEQ 2504 3960 Missing (in isoform Replicase polyprotein
1a). {ECO:0000305}.
/FTId=VSP_032893.
VARIANT 188 188 H -> R (in strain: BJ-4).
VARIANT 386 386 K -> R (in strain: BJ-4).
VARIANT 393 393 S -> H (in strain: BJ-4).
VARIANT 1498 1498 S -> A (in strain: Isolate infectious
clone VR-2332).
VARIANT 1777 1777 T -> I (in strain: Isolate infectious
clone VR-2332).
VARIANT 2222 2222 D -> N (in strain: Isolate infectious
clone VR-2332).
VARIANT 3257 3257 G -> E (in strain: Isolate infectious
clone VR-2332).
VARIANT 3539 3539 C -> R (in strain: Isolate infectious
clone VR-2332).
VARIANT 3623 3623 S -> T (in strain: Isolate infectious
clone VR-2332).
VARIANT 3678 3678 G -> E (in strain: Isolate infectious
clone VR-2332).
VARIANT 3714 3714 G -> A (in strain: Isolate infectious
clone VR-2332).
MUTAGEN 76 76 C->S: Complete loss of papain-like
cysteine protease activity of nsp1-alpha.
Loss of inhibition of IFN-beta
production. Loss of inhibition of IRF-3
phosphorylation.
{ECO:0000269|PubMed:21438756}.
MUTAGEN 146 146 H->D: Complete loss of papain-like
cysteine protease activity of nsp1-alpha.
{ECO:0000269|PubMed:21438756}.
MUTAGEN 270 270 C->S: No effect on inhibition of IRF-3
phosphorylation.
{ECO:0000269|PubMed:21438756}.
SEQUENCE 3960 AA; 432887 MW; F219409DA3F3B73F CRC64;
MSGILDRCTC TPNARVFMAE GQVYCTRCLS ARSLLPLNLQ VSELGVLGLF YRPEEPLRWT
LPRAFPTVEC SPAGACWLSA IFPIARMTSG NLNFQQRMVR VAAELYRAGQ LTPAVLKALQ
VYERGCRWYP IVGPVPGVAV FANSLHVSDK PFPGATHVLT NLPLPQRPKP EDFCPFECAM
ATVYDIGHDA VMYVAERKVS WAPRGGDEVK FEAVPGELKL IANRLRTSFP PHHTVDMSKF
AFTAPGCGVS MRVERQHGCL PADTVPEGNC WWSLFDLLPL EVQNKEIRHA NQFGYQTKHG
VSGKYLQRRL QVNGLRAVTD LNGPIVVQYF SVKESWIRHL KLAGEPSYSG FEDLLRIRVE
PNTSPLADKE EKIFRFGSHK WYGAGKRARK ARSCATATVA GRALSVRETR QAKEHEVAGA
NKAEHLKHYS PPAEGNCGWH CISAIANRMV NSKFETTLPE RVRPPDDWAT DEDLVNAIQI
LRLPAALDRN GACTSAKYVL KLEGEHWTVT VTPGMSPSLL PLECVQGCCG HKGGLGSPDA
VEVSGFDPAC LDRLAEVMHL PSSAIPAALA EMSGDSDRSA SPVTTVWTVS QFFARHSGGN
HPDQVRLGKI ISLCQVIEDC CCSQNKTNRV TPEEVAAKID LYLRGATNLE ECLARLEKAR
PPRVIDTSFD WDVVLPGVEA ATQTIKLPQV NQCRALVPVV TQKSLDNNSV PLTAFSLANY
YYRAQGDEVR HRERLTAVLS KLEKVVREEY GLMPTEPGPR PTLPRGLDEL KDQMEEDLLK
LANAQTTSDM MAWAVEQVDL KTWVKNYPRW TPPPPPPKVQ PRKTKPVKSL PERKPVPAPR
RKVGSDCGSP VSLGGDVPNS WEDLAVSSPF DLPTPPEPAT PSSELVIVSS PQCIFRPATP
LSEPAPIPAP RGTVSRPVTP LSEPIPVPAP RRKFQQVKRL SSAAAIPPYQ DEPLDLSASS
QTEYEASPPA PPQSGGVLGV EGHEAEETLS EISDMSGNIK PASVSSSSSL SSVRITRPKY
SAQAIIDSGG PCSGHLQEVK ETCLSVMREA CDATKLDDPA TQEWLSRMWD RVDMLTWRNT
SVYQAICTLD GRLKFLPKMI LETPPPYPCE FVMMPHTPAP SVGAESDLTI GSVATEDVPR
ILEKIENVGE MANQGPLAFS EDKPVDDQLV NDPRISSRRP DESTSAPSAG TGGAGSFTDL
PPSDGADADG GGPFRTVKRK AERLFDQLSR QVFDLVSHLP VFFSRLFYPG GGYSPGDWGF
AAFTLLCLFL CYSYPAFGIA PLLGVFSGSS RRVRMGVFGC WLAFAVGLFK PVSDPVGAAC
EFDSPECRNI LHSFELLKPW DPVRSLVVGP VGLGLAILGR LLGGARCIWH FLLRLGIVAD
CILAGAYVLS QGRCKKCWGS CIRTAPNEVA FNVFPFTRAT RSSLIDLCDR FCAPKGMDPI
FLATGWRGCW AGRSPIEQPS EKPIAFAQLD EKKITARTVV AQPYDPNQAV KCLRVLQSGG
AMVAKAVPKV VKVSAVPFRA PFFPTGVKVD PDCRVVVDPD TFTAALRSGY STTNLVLGVG
DFAQLNGLKI RQISKPSGGG PHLMAALHVA CSMALHMLAG IYVTAVGSCG TGTNDPWCAN
PFAVPGYGPG SLCTSRLCIS QHGLTLPLTA LVAGFGIQEI ALVVLIFVSI GGMAHRLSCK
ADMLCVLLAI ASYVWVPLTW LLCVFPCWLR CFSLHPLTIL WLVFFLISVN MPSGILAMVL
LVSLWLLGRY TNVAGLVTPY DIHHYTSGPR GVAALATAPD GTYLAAVRRA ALTGRTMLFT
PSQLGSLLEG AFRTRKPSLN TVNVIGSSMG SGGVFTIDGK VKCVTAAHVL TGNSARVSGV
GFNQMLDFDV KGDFAIADCP NWQGAAPKTQ FCTDGWTGRA YWLTSSGVEP GVIGKGFAFC
FTACGDSGSP VITEAGELVG VHTGSNKQGG GIVTRPSGQF CNVAPIKLSE LSEFFAGPKV
PLGDVKVGSH IIKDISEVPS DLCALLAAKP ELEGGLSTVQ LLCVFFLLWR MMGHAWTPLV
AVSFFILNEV LPAVLVRSVF SFGMFVLSWL TPWSAQVLMI RLLTAALNRN RWSLAFFSLG
AVTGFVADLA ATQGHPLQAV MNLSTYAFLP RMMVVTSPVP VITCGVVHLL AIILYLFKYR
GPHHILVGDG VFSAAFFLRY FAEGKLREGV SQSCGMNHES LTGALAMRLN DEDLDFLMKW
TDFKCFVSAS NMRNAAGQFI EAAYAKALRV ELAQLVQVDK VRGTLAKLEA FADTVAPQLS
PGDIVVALGH TPVGSIFDLK VGSTKHTLQA IETRVLAGSK MTVARVVDPT PTPPPAPVPI
PLPPKVLENG PNAWGDEDRL NKKKRRRMEA LGIYVMGGKK YQKFWDKNSG DVFYEEVHNN
TDEWECLRVG DPADFDPEKG TLCGHVTIEN KAYHVYTSPS GKKFLVPVNP ENGRVQWEAA
KLSVEQALGM MNVDGELTAK ELEKLKRIID KLQGLTKEQC LNCLAASDLT RCGRGGLVVT
ETAVKIVKFH NRTFTLGPVN LKVASEVELK DAVEHNQHPV ARPIDGGVVL LRSAVPSLID
VLISGADASP KLLAHHGPGN TGIDGTLWDF ESEATKEEVA LSAQIIQACD IRRGDAPEIG
LPYKLYPVRG NPERVKGVLQ NTRFGDIPYK TPSDTGSPVH AAACLTPNAT PVTDGRSVLA
TTMPPGFELY VPTIPASVLD YLDSRPDCPK QLTEHGCEDA ALKDLSKYDL STQGFVLPGV
LRLVRKYLFA HVGKCPPVHR PSTYPAKNSM AGINGNRFPT KDIQSVPEID VLCAQAVREN
WQTVTPCTLK KQYCGKKKTR TILGTNNFIA LAHRAVLSGV TQGFMKKAFN SPIALGKNKF
KELQTPVLGR CLEADLASCD RSTPAIVRWF AANLLYELAC AEEHLPSYVL NCCHDLLVTQ
SGAVTKRGGL SSGDPITSVS NTIYSLVIYA QHMVLSYFKS GHPHGLLFLQ DQLKFEDMLK
VQPLIVYSDD LVLYAESPTM PNYHWWVEHL NLMLGFQTDP KKTAITDSPS FLGCRIINGR
QLVPNRDRIL AALAYHMKAS NVSEYYASAA AILMDSCACL EYDPEWFEEL VVGIAQCARK
DGYSFPGTPF FMSMWEKLRS NYEGKKSRVC GYCGAPAPYA TACGLDVCIY HTHFHQHCPV
TIWCGHPAGS GSCSECKSPV GKGTSPLDEV LEQVPYKPPR TVIMHVEQGL TPLDPGRYQT
RRGLVSVRRG IRGNEVGLPD GDYASTALLP TCKEINMVAV ASNVLRSRFI IGPPGAGKTY
WLLQQVQDGD VIYTPTHQTM LDMIRALGTC RFNVPAGTTL QFPVPSRTGP WVRILAGGWC
PGKNSFLDEA AYCNHLDVLR LLSKTTLTCL GDFKQLHPVG FDSHCYVFDI MPQTQLKTIW
RFGQNICDAI QPDYRDKLMS MVNTTRVTYV EKPVRYGQVL TPYHRDREDD AITIDSSQGA
TFDVVTLHLP TKDSLNRQRA LVAITRARHA IFVYDPHRQL QGLFDLPAKG TPVNLAVHCD
GQLIVLDRNN KECTVAQALG NGDKFRATDK RVVDSLRAIC ADLEGSSSPL PKVAHNLGFY
FSPDLTQFAK LPVELAPHWP VVSTQNNEKW PDRLVASLRP IHKYSRACIG AGYMVGPSVF
LGTPGVVSYY LTKFVKGGAQ VLPETVFSTG RIEVDCREYL DDREREVAAS LPHGFIGDVK
GTTVGGCHHV TSRYLPRVLP KESVAVVGVS SPGKAAKALC TLTDVYLPDL EAYLHPETQS
KCWKMMLDFK EVRLMVWKDK TAYFQLEGRY FTWYQLASYA SYIRVPVNST VYLDPCMGPA
LCNRRVVGST HWGADLAVTP YDYGAKIILS SAYHGEMPPG YKILACAEFS LDDPVKYKHT
WGFESDTAYL YEFTGNGEDW EDYNDAFRAR QEGKIYKATA TSLKFYFPPG PVIEPTLGLN


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