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 RPOA_PRRSS              Reviewed;        3838 AA.
A0MD28; A0MD29; Q6U9W7; Q6U9W8;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 2.
10-MAY-2017, entry version 50.
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;
Porcine reproductive and respiratory syndrome virus (isolate
Pig/United States/SD 01-08/2001) (PRRSV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae; unclassified Arteriviridae.
NCBI_TaxID=857306;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15019241; DOI=10.1016/j.virusres.2003.12.026;
Fang Y., Kim D.Y., Ropp S., Steen P., Christopher-Hennings J.,
Nelson E.A., Rowland R.R.;
"Heterogeneity in Nsp2 of European-like porcine reproductive and
respiratory syndrome viruses isolated in the United States.";
Virus Res. 100:229-235(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Infectious clone SD 01-08;
PubMed=16971421; DOI=10.1128/JVI.01032-06;
Fang Y., Rowland R.R., Roof M., Lunney J.K., Christopher-Hennings J.,
Nelson E.A.;
"A full-length cDNA infectious clone of North American type 1 porcine
reproductive and respiratory syndrome virus: expression of green
fluorescent protein in the Nsp2 region.";
J. Virol. 80:11447-11455(2006).
[3]
FUNCTION (NSP2 CYSTEINE PROTEINASE), AND MUTAGENESIS OF CYS-429;
ASP-458; SER-462; ASP-463; ASP-465 AND HIS-498.
PubMed=20504922; DOI=10.1128/JVI.00217-10;
Sun Z., Chen Z., Lawson S.R., Fang Y.;
"The cysteine protease domain of porcine reproductive and respiratory
syndrome virus nonstructural protein 2 possesses deubiquitinating and
interferon antagonism functions.";
J. Virol. 84:7832-7846(2010).
[4]
PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, AND PROTEOLYTIC PROCESSING
OF POLYPROTEIN 1B.
PubMed=22258855; DOI=10.1099/vir.0.039289-0;
Li Y., Tas A., Snijder E.J., Fang Y.;
"Identification of porcine reproductive and respiratory syndrome virus
ORF1a-encoded non-structural proteins in virus-infected cells.";
J. Gen. Virol. 93:829-839(2012).
[5]
SUBCELLULAR LOCATION OF NSP2.
PubMed=23043113; DOI=10.1073/pnas.1211145109;
Fang Y., Treffers E.E., Li Y., Tas A., Sun Z., van der Meer Y.,
de Ru A.H., van Veelen P.A., Atkins J.F., Snijder E.J., Firth A.E.;
"Efficient -2 frameshifting by mammalian ribosomes to synthesize an
additional arterivirus protein.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2920-E2928(2012).
[6]
FUNCTION (NSP2 CYSTEINE PROTEINASE).
PubMed=22258253; DOI=10.1128/JVI.06466-11;
Sun Z., Li Y., Ransburgh R., Snijder E.J., Fang Y.;
"Nonstructural protein 2 of porcine reproductive and respiratory
syndrome virus inhibits the antiviral function of interferon-
stimulated gene 15.";
J. Virol. 86:3839-3850(2012).
-!- 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}.
-!- 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:0000269|PubMed:20504922,
ECO:0000269|PubMed:22258253}.
-!- 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
{ECO:0000250|UniProtKB:Q04561}. Host cytoplasm
{ECO:0000250|UniProtKB:Q04561}.
-!- SUBCELLULAR LOCATION: Nsp1-alpha papain-like cysteine proteinase:
Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm
{ECO:0000250|UniProtKB:Q04561}.
-!- SUBCELLULAR LOCATION: Nsp1-beta papain-like cysteine proteinase:
Host nucleus {ECO:0000250|UniProtKB:Q04561}.
-!- SUBCELLULAR LOCATION: Nsp2 cysteine proteinase: Host endoplasmic
reticulum membrane {ECO:0000305}; Multi-pass membrane protein
{ECO:0000305}.
-!- 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=3;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=A0MD28-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=A0MD28-2; Sequence=VSP_039634;
Note=Produced by conventional translation.;
Name=Truncated polyprotein 1aTF;
IsoId=P0DJY0-1; Sequence=External;
Note=Produced by -2 ribosomal frameshifting in the nsp2 gene.;
-!- 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:0000305}.
-!- 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). Many long-lived processing
intermediates exist such as nsp3-4, nsp5-7, nsp5-8 and nsp3-8.
{ECO:0000250, ECO:0000269|PubMed:22258855}.
-!- SIMILARITY: Belongs to the arteriviridae polyprotein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAR37017.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY375474; AAR37016.1; -; Genomic_RNA.
EMBL; AY375474; AAR37017.1; ALT_INIT; Genomic_RNA.
EMBL; DQ489311; ABF66340.1; -; Genomic_RNA.
EMBL; DQ489311; ABF66341.1; -; Genomic_RNA.
SMR; A0MD28; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000000937; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum 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.
GO; GO:0075523; P:viral translational frameshifting; IDA:UniProtKB.
Gene3D; 3.30.40.20; -; 1.
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; IPR023183; Chymotrypsin-like_domain3.
InterPro; IPR008760; EAV_peptidase_S32.
InterPro; IPR032855; NSP2-B_epitope.
InterPro; IPR032841; NSP2_assoc.
InterPro; IPR027417; P-loop_NTPase.
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; PF14758; NSP2_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; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
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; Complete proteome; 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 3838 Replicase polyprotein 1ab. {ECO:0000250}.
/FTId=PRO_0000397084.
CHAIN 1 385 Nsp1.
/FTId=PRO_0000410830.
CHAIN 1 180 Nsp1-alpha papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000397085.
CHAIN 181 385 Nsp1-beta papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000397086.
CHAIN 386 1446 Nsp2 cysteine proteinase.
/FTId=PRO_0000397087.
CHAIN 1447 1676 Non-structural protein 3.
/FTId=PRO_0000397088.
CHAIN 1677 1879 3C-like serine proteinase.
/FTId=PRO_0000397089.
CHAIN 1880 2334 Non-structural protein 5-6-7.
{ECO:0000250}.
/FTId=PRO_0000397090.
CHAIN 1880 2049 Non-structural protein 5.
/FTId=PRO_0000423134.
CHAIN 2050 2065 Non-structural protein 6.
/FTId=PRO_0000423135.
CHAIN 2066 2214 Non-structural protein 7-alpha.
/FTId=PRO_0000423136.
CHAIN 2215 2334 Non-structural protein 7-beta.
/FTId=PRO_0000423137.
CHAIN 2335 3020 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000397091.
CHAIN 2335 2379 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000397092.
CHAIN 3021 3462 Helicase. {ECO:0000250}.
/FTId=PRO_0000397093.
CHAIN 3463 3686 Non-structural protein 11. {ECO:0000250}.
/FTId=PRO_0000397094.
CHAIN 3687 3838 Non-structural protein 12. {ECO:0000250}.
/FTId=PRO_0000397095.
TRANSMEM 1094 1114 Helical. {ECO:0000255}.
TRANSMEM 1117 1137 Helical. {ECO:0000255}.
TRANSMEM 1162 1182 Helical. {ECO:0000255}.
TRANSMEM 1211 1231 Helical. {ECO:0000255}.
TRANSMEM 1235 1255 Helical. {ECO:0000255}.
TRANSMEM 1450 1470 Helical. {ECO:0000255}.
TRANSMEM 1526 1546 Helical. {ECO:0000255}.
TRANSMEM 1556 1576 Helical. {ECO:0000255}.
TRANSMEM 1592 1612 Helical. {ECO:0000255}.
TRANSMEM 1875 1895 Helical. {ECO:0000255}.
TRANSMEM 1916 1936 Helical. {ECO:0000255}.
TRANSMEM 1960 1980 Helical. {ECO:0000255}.
TRANSMEM 2003 2023 Helical. {ECO:0000255}.
TRANSMEM 2029 2048 Helical. {ECO:0000255}.
DOMAIN 69 180 Peptidase C31. {ECO:0000255|PROSITE-
ProRule:PRU00872}.
DOMAIN 269 385 Peptidase C32. {ECO:0000255|PROSITE-
ProRule:PRU00873}.
DOMAIN 420 527 Peptidase C33. {ECO:0000255|PROSITE-
ProRule:PRU00871}.
DOMAIN 1677 1879 Peptidase S32. {ECO:0000255|PROSITE-
ProRule:PRU00826}.
DOMAIN 2765 2899 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 3021 3084 AV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
DOMAIN 3134 3293 (+)RNA virus helicase ATP-binding.
DOMAIN 3294 3423 (+)RNA virus helicase C-terminal.
ZN_FING 8 28 C4-type; atypical.
NP_BIND 3168 3175 ATP. {ECO:0000250}.
REGION 69 182 PCP1-alpha. {ECO:0000250}.
REGION 269 384 PCP1-beta. {ECO:0000250}.
REGION 418 505 OTU-like.
REGION 1132 1255 HD1. {ECO:0000250}.
REGION 1310 1334 WCCH. {ECO:0000250}.
REGION 1451 1612 HD2. {ECO:0000250}.
REGION 1902 2023 HD3. {ECO:0000250}.
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 276 276 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 345 345 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 429 429 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 498 498 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 1715 1715 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1740 1740 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1793 1793 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
METAL 3027 3027 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3030 3030 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3040 3040 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3045 3045 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3048 3048 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3050 3050 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3052 3052 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3054 3054 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3061 3061 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3063 3063 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3070 3070 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3073 3073 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
SITE 180 181 Cleavage; by autolysis. {ECO:0000255}.
SITE 385 386 Cleavage; by autolysis.
SITE 1446 1447 Cleavage; by CP2. {ECO:0000255}.
SITE 1676 1677 Cleavage; by 3CLSP.
SITE 1879 1880 Cleavage; by 3CLSP.
SITE 2049 2050 Cleavage; by 3CLSP.
SITE 2065 2066 Cleavage; by 3CLSP.
SITE 2214 2215 Cleavage; by 3CLSP.
SITE 2334 2335 Cleavage; by 3CLSP.
SITE 3020 3021 Cleavage; by 3CLSP.
SITE 3071 3071 Involved in mRNA transcription process.
{ECO:0000250}.
SITE 3462 3463 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3686 3687 Cleavage; by 3CLSP. {ECO:0000250}.
VAR_SEQ 2380 3838 Missing (in isoform Replicase polyprotein
1a). {ECO:0000305}.
/FTId=VSP_039634.
VARIANT 666 666 R -> Q (in strain: Infectious clone SD
01-08).
VARIANT 1005 1005 R -> K (in strain: Infectious clone SD
01-08).
VARIANT 1012 1012 N -> S (in strain: Infectious clone SD
01-08).
VARIANT 3092 3092 P -> L (in strain: Infectious clone SD
01-08).
VARIANT 3682 3682 Y -> H (in strain: Infectious clone SD
01-08).
MUTAGEN 429 429 C->A: Lethal.
{ECO:0000269|PubMed:20504922}.
MUTAGEN 458 458 D->A: Slight reduction in the ability of
Nsp2 to impair NF-kappaB activation.
{ECO:0000269|PubMed:20504922}.
MUTAGEN 462 462 S->A: Reduction in the ability of Nsp2 to
impair NF-kappaB activation.
{ECO:0000269|PubMed:20504922}.
MUTAGEN 463 463 D->A: Lethal.
{ECO:0000269|PubMed:20504922}.
MUTAGEN 465 465 D->A: Reduction in the ability of Nsp2 to
impair NF-kappaB activation.
{ECO:0000269|PubMed:20504922}.
MUTAGEN 498 498 H->A: Lethal.
{ECO:0000269|PubMed:20504922}.
SEQUENCE 3838 AA; 418948 MW; 07ADB34E6578FFC9 CRC64;
MSGTFSRCMC TPAARVFWNA GQVFCTRCLS ARPLLSPELQ DTDLGVVGLF YKPKDKIHWK
VPIGIPQVEC TPSGCCWLSA VFPLARMTSG NHNFLQRLVK VADVLYRDGC LAPRHLRELQ
VYERGCSWYP ITGPVPGMGL FANSMHVSDQ PFPGATHVLT NSPLPQRACR QPFCPFEEAH
SDVYRWKKFV IFTDSSPNGR FRMMWTPESD DSAALEVLPP ELERQVEILT RSFPAHHPIN
LADWELTESP ENGFSFGTSH SCGHIVQNPN VFDGKCWLTC FLGQSAEVCY HEEHLANALG
YQTKWGVHGK YLQRRLQVRG MRAVVDPDGP IHVEALSCSQ SWVRHLTLNN DVTPGFVRLT
SIRIVSNTEP TAFRIFRFGA HKWYGAAGKR ARAKRATKSG KDSALAPKIA PPVPTCGITT
YSPPTDGSCG WHVLAAIVNR MINGDFTSPL PQYNRPEDDW ASDYDLAQAI QCLQLPATVV
RNRACPNAKY LIKLNGVHWE VEVRSGMAPR SLSRECVVGV CSEGCVAPPY PADGLPKRAL
EALASAYRLP SDCVSSGIAD FLADPPPQEF WTLDKMLTSP SPERSGFSSL YKLLLEVVPQ
KCGATEGAFV YAVERMLKDC PSPEQAMALL AKIKVPSSKA PSVSLDECFP AGVPADFEPA
FQERPRSPGA AVALCSPDAK GFEGTASEEA QESGHKAVHA VPLAEGPNNE QVQVVAGEQL
ELGGCGLAIG SAQSSSDSKR ENMHNSREDE PLDLSHPAPA ATTTLVGEQT PDNPGSDASA
LPIAVRGFVP TGPILRHVEH CGTESGDSSS PLDLSFAQTL DQPLDLSLAA WPVKATASDP
GWVRGRCEPV FLKPRKAFSD GDSALQFGEL SESSSVIEFD QTKDTLVADA PVDLTTSNEA
LSAVDPSEFV ELRRPRHSAQ ALIDRGGPLA DVHAKIKNRV YEQCLQACEP GSRATPATRE
WLDKMWDRVD MKTWRCTSQF QAGRILASLK FLPDMIQDTP PPVPRKNRAS DNAGLKQLVA
RWDKKLSVTP PPKSAGLVLD QTVPPPTDIQ QEDATPSDGL SHASDFSSRV STSWSWKGLM
LSGTRLAGSA GQRLMTWVFE VYSHLPAFIL TLFSPRGSMA PGDWLFAGVV LLALLLCRSY
PILGCLPLLG VFSGSLRRVR LGVFGSWMAF AVFLFSTPSN PVGSSCDHDS PECHAELLAL
EQRQLWEPVR GLVVGPSGLL CVILGKLLGG SRHLWHVILR LCMLTDLALS LVYVVSQGRC
HKCWGKCIRT APAEVALNVF PFSRATRNSL TSLCDRFQTP KGVDPVHLAT GWRGCWRGES
PIHQPHQKPI AYANLDEKKI SAQTVVAVPY DPSQAIKCLK VLQAGGAIVD QPTPEVVRVS
EIPFSAPFFP KVPVNPDCRI VVDSDTFVAA VRCGYSTAQL VLGRGNFAKL NQTPLRDSAS
TKTTGGASYT LAVAQVSVWT LVHFILGLWF TSPQVCGRGT ADPWCSNPFS YPAYGPGVVC
SSRLCVSADG VTLPLFSAVA QLSGREVGIF ILVLVSLTAL AHRLALKADM LVVFSAFCAY
AWPMSSWLIC FFPILLKWVT LHPLTMLWVH SFLVFCMPAA GILSLGITGL LWAVGRFTQV
AGIITPYDIH QYTSGPRGAA AVATAPEGTY MAAVRRAALT GRTLIFTPSA VGSLLEGAFR
THKPCLNTVN VVGSSLGSGG VFTIDGRKTV VTAAHVLNGD TARVTGDSYN RMHTFKTSGD
YAWSHADDWQ GVAPVVKVAK GYRGRAYWQT STGVEPGVIG EGFAFCFTNC GDSGSPVISE
SGDLIGIHTG SNKLGSGLVT TPEGETCAIK ETKLSDLSRH FAGPSVPLGD IKLSPAIVPD
VTSIPSDLAS LLASVPVMEG GLSTVQLLCV FFLLWRMMGH AWTPIVAVGF FLLNEILPAV
LVRAVFSFAL FILAWATPWS AQVLMIRLLT ASLNRNKLSL AFYALGGVVG LAAEIGAFAG
RLPELSQALS TYCFLPRVLA MASYVPIIII GGLHALGVIL WLFKYRCLHN MLVGDGSFSS
AFFLRYFAEG NLRKGVSQSC GMSNESLTAA LACKLSQADL DFLSSLTNFK CFVSASNMKN
AAGQYIEAAY AKALRQELAS LVQVDKMKGI LSKLEAFAET ATPSLDAGDV VVLLGQHPHG
SILDINVGTE RKTVSVQETR SLGGSKFSVC TVVSNTPVDA LTGIPLQTPT PLFENGPRHR
GEEDDLRVER MKKHCVSLGF HNINGKVYCK IWDKSTGDTF YTDDSRYTQD LAFQDRSADY
RDRDYEGVQT APQQGFDPKS ETPIGTVVIG GITYNRYLIK GKEVLVPKPD NCLEAAKLSL
EQALAGMGQT CDLTAAEVEK LRRIISQLQG LTTEQALNCL LAASGLTRCG RGGLVVTETA
VKIVKYHSRT FTLGPLDLKV TSEAEVKKST EQGHAVVANL CSGVILMRPH PPSLVDVLLK
PGLDTKPGIQ PGHGAGNMGV DGSTWDFETA PTKAELELSK QIIQACEVRR GDAPNLQLPY
KLYPVRGDPE RHGGRLINTR FGDLSYKTPQ DTKSAIHAAC CLHPNGAPVS DGKSTLGTTL
QHGFELYVPT VPYSVMEYLD SRPDTPFMCT KHGTSKAAAE DLQKYDLSTQ GFVLPGVLRL
VRRFIFGHIG KAPPLFLPST YPAKNSMAGI NGQRFPTKDV QSIPEIDEMC ARAVKENWQT
VTPCTLKKQY CSKPKTRTIL GTNNFIALAH RSALSGVTQA FMKKAWKSPI ALGKNKFKEL
HCTVAGRCLE ADLASCDRST PAIVRWFVAN LLYELAGCEE YLPSYVLNCC HDLVATQDGA
FTKRGGLSSG DPVTSVSNTV YSLIIYAQHM VLSALKMGHE IGLKFLEEQL KFEDLLEIQP
MLVYSDDLVL YAERPTFPNY HWWVEHLDLM LGFRTDPKKT VITDKPSFLG CRIEAGRQLV
PNRDRILAAL AYHMKAQNAS EYYASAAAIL MDSCACIDHD PEWYEDLICG IARCARQDGY
SFPGPAFFMS MWEKLRSHNE GKKFRHCGIC DAKADHASAC GLDLCLFHSH FHQHCPVTLS
CGHHAGSREC SQCQSPVGAG RSPLDAVLKQ IPYKPPRTVI MKVGNKTTAL DPGRYQSRRG
LVAVKRGIAG NEVDLPDGDY QVVPLLPTCK DINMVKVACN VLLSKFIVGP PGSGKTTWLL
SQVQDDDVIY TPTHQTMFDI VSALKVCRYS IPGASGLPFP PPARSGPWVR LVASGHVPGR
TSYLDEAGYC NHLDILRLLS KTPLVCLGDL QQLHPVGFDS YCYVFDQMPQ KQLTTIYRFG
PNICAAIQPC YREKLESKAR NTRVVFTTWP VAFGQVLTPY HKDRIGSAIT IDSSQGATFD
IVTLHLPSPK SLNKSRALVA ITRARHGLFI YDPHNQLQEF FNLIPERTDC NLVFSRGDDL
VVLSADNAVT TVAKALGTGP SRFRVSDPRC KSLLAACSAS LEGSCMPLPQ VAHNLGFYFS
PDSPAFAPLP KELAPHWPVV THQNNRAWPD RLVASMRPID ARYSKPMVGA GYVVGPSTFL
GTPGVVSYYL TLYIRGEPQA LPETLVSTGR IATDCREYLD AAEEEAAKEL PHAFIGDVKG
TTVGGCHHIT SKYLPRTLPK DSVAVVGVSS PGRAAKAMCT LTDVYLPELR PYLQPETASK
CWKLKLDFRD VRLMVWKGAT AYFQLEGLTW SALPDYARFI QLPKDAVVYI DPCIGPATAN
RKVVRTTDWR ADLAVTPYDY GAQNILTTAW FEDLGPQWKI LGLQPFRRAF GFENTEDWAI
LARRMSDGKD YTDYNWDCVR ERPHAIYGRA RDHTYHFAPG TELQVELGKP RLPPGREP


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