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 RPOA_PRRSL              Reviewed;        3855 AA.
Q04561;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 3.
10-MAY-2017, entry version 130.
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 Lelystad)
(PRRSV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae; unclassified Arteriviridae.
NCBI_TaxID=11049;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8517032; DOI=10.1006/viro.1993.1008;
Meulenberg J.J.M., Hulst M.M., de Meijer E.J., Moonen P.L.J.M.,
den Besten A., de Kluyver E.P., Wensvoort G., Moormann R.J.M.;
"Lelystad virus, the causative agent of porcine epidemic abortion and
respiratory syndrome (PEARS), is related to LDV and EAV.";
Virology 192:62-72(1993).
[2]
SEQUENCE REVISION TO 3327.
Kroese M.V., Moormann R.J.M.;
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 3323-3855.
STRAIN=Isolate Boxmeer 10;
PubMed=8438574; DOI=10.1006/viro.1993.1129;
Conzelmann K.K., Visser N., van Woensel P., Thiel H.J.;
"Molecular characterization of porcine reproductive and respiratory
syndrome virus, a member of the arterivirus group.";
Virology 193:329-339(1993).
[4]
ACTIVE SITES OF PCP1-ALPHA AND PCP1-BETA, AND MUTAGENESIS OF CYS-76;
HIS-92; HIS-115; HIS-146; HIS-157; HIS-157; CYS-276 AND HIS-345.
PubMed=7769711;
den Boon J.A., Faaberg K.S., Meulenberg J.J.M., Wassenaar A.L.M.,
Plagemann P.G.W., Gorbalenya A.E., Snijder E.J.;
"Processing and evolution of the N-terminal region of the arterivirus
replicase ORF1a protein: identification of two papainlike cysteine
proteases.";
J. Virol. 69:4500-4505(1995).
[5]
FUNCTION (HELICASE).
PubMed=12127789; DOI=10.1006/viro.2002.1495;
Bautista E.M., Faaberg K.S., Mickelson D., McGruder E.D.;
"Functional properties of the predicted helicase of porcine
reproductive and respiratory syndrome virus.";
Virology 298:258-270(2002).
[6]
FUNCTION (3C-LIKE SERINE PROTEINASE), AND ACTIVE SITE (3C-LIKE SERINE
PROTEINASE).
STRAIN=JXA1;
PubMed=19646449; DOI=10.1016/j.jmb.2009.07.062;
Tian X., Lu G., Gao F., Peng H., Feng Y., Ma G., Bartlam M., Tian K.,
Yan J., Hilgenfeld R., Gao G.F.;
"Structure and cleavage specificity of the chymotrypsin-like serine
protease (3CLSP/nsp4) of Porcine Reproductive and Respiratory Syndrome
Virus (PRRSV).";
J. Mol. Biol. 392:977-993(2009).
[7]
FUNCTION (NON-STRUCTURAL PROTEIN 5-6-7), AND SUBCELLULAR LOCATION
(NON-STRUCTURAL PROTEIN 5-6-7).
PubMed=21799305; DOI=10.4161/auto.7.11.16642;
Cottam E.M., Maier H.J., Manifava M., Vaux L.C.,
Chandra-Schoenfelder P., Gerner W., Britton P., Ktistakis N.T.,
Wileman T.;
"Coronavirus nsp6 proteins generate autophagosomes from the
endoplasmic reticulum via an omegasome intermediate.";
Autophagy 7:1335-1347(2011).
[8]
FUNCTION (NSP1-ALPHA PAPAIN-LIKE CYSTEINE PROTEINASE), AND SUBCELLULAR
LOCATION (NSP1-ALPHA PAPAIN-LIKE CYSTEINE PROTEINASE).
STRAIN=PA8;
PubMed=23287061; DOI=10.1016/j.virusres.2012.12.012;
Han M., Du Y., Song C., Yoo D.;
"Degradation of CREB-binding protein and modulation of type I
interferon induction by the zinc finger motif of the porcine
reproductive and respiratory syndrome virus nsp1alpha subunit.";
Virus Res. 172:54-65(2013).
[9]
FUNCTION (3C-LIKE SERINE PROTEINASE).
STRAIN=CH-1a;
PubMed=23936003; DOI=10.1371/journal.pone.0069387;
Ma Z., Wang Y., Zhao H., Xu A.T., Wang Y., Tang J., Feng W.H.;
"Porcine reproductive and respiratory syndrome virus nonstructural
protein 4 induces apoptosis dependent on its 3C-like serine protease
activity.";
PLoS ONE 8:E69387-E69387(2013).
[10]
FUNCTION (NON-STRUCTURAL PROTEIN 3), SUBCELLULAR LOCATION
(NON-STRUCTURAL PROTEIN 3), AND INTERACTION WITH HOST IFITM1
(NON-STRUCTURAL PROTEIN 3).
STRAIN=JXwn06;
PubMed=25102331; DOI=10.1016/j.virusres.2014.07.025;
Wang X., Li C., Zhou L., Zhang N., Wang X., Ge X., Guo X., Yang H.;
"Porcine reproductive and respiratory syndrome virus counteracts the
porcine intrinsic virus restriction factors-IFITM1 and Tetherin in
MARC-145 cells.";
Virus Res. 191:92-100(2014).
[11]
FUNCTION (RNA-DIRECTED RNA POLYMERASE), INTERACTION WITH HOST DDX5
(RNA-DIRECTED RNA POLYMERASE), AND SUBCELLULAR LOCATION (RNA-DIRECTED
RNA POLYMERASE).
STRAIN=JXwn06;
PubMed=25449571; DOI=10.1016/j.virusres.2014.10.021;
Zhao S., Ge X., Wang X., Liu A., Guo X., Zhou L., Yu K., Yang H.;
"The DEAD-box RNA helicase 5 positively regulates the replication of
porcine reproductive and respiratory syndrome virus by interacting
with viral Nsp9 in vitro.";
Virus Res. 195:217-224(2015).
[12]
FUNCTION (NON-STRUCTURAL PROTEIN 11).
STRAIN=BJ-4;
PubMed=26398903; DOI=10.1089/dna.2015.2929;
Wang C., Shi X., Zhang X., Wang A., Wang L., Chen J., Deng R.,
Zhang G.;
"The endoribonuclease activity essential for the nonstructural protein
11 of porcine reproductive and respiratory syndrome virus to inhibit
NLRP3 inflammasome-Mediated IL-1beta induction.";
DNA Cell Biol. 34:728-735(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-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:Q9WJB2,
ECO:0000269|PubMed:23287061}.
-!- 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:0000250|UniProtKB:Q9WJB2}.
-!- 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:0000269|PubMed:25102331}.
-!- 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:0000269|PubMed:19646449, ECO:0000269|PubMed:23936003}.
-!- FUNCTION: Non-structural protein 5-6-7: Plays a role in the
initial induction of autophagosomes from host reticulum
endoplasmic. {ECO:0000269|PubMed:21799305}.
-!- FUNCTION: RNA-directed RNA polymerase: Responsible for replication
and transcription of the viral RNA genome.
{ECO:0000269|PubMed:25449571}.
-!- FUNCTION: Helicase: Displays RNA and DNA duplex-unwinding
activities with 5' to 3' polarity. {ECO:0000269|PubMed:12127789}.
-!- 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:0000269|PubMed:26398903}.
-!- 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:0000269|PubMed:25102331, ECO:0000269|PubMed:25449571}.
-!- SUBCELLULAR LOCATION: Nsp1: Host nucleus
{ECO:0000269|PubMed:23287061}. Host cytoplasm
{ECO:0000269|PubMed:23287061}.
-!- SUBCELLULAR LOCATION: Nsp1-alpha papain-like cysteine proteinase:
Host nucleus {ECO:0000269|PubMed:23287061}. Host cytoplasm
{ECO:0000269|PubMed:23287061}.
-!- SUBCELLULAR LOCATION: Nsp1-beta papain-like cysteine proteinase:
Host nucleus {ECO:0000269|PubMed:23287061}.
-!- SUBCELLULAR LOCATION: Nsp2 cysteine proteinase: Host 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:0000269|PubMed:21799305}. 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:0000269|PubMed:25449571}. 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=Q04561-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=Q04561-2; Sequence=VSP_032892;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1TF;
IsoId=P0DJZ9-1; Sequence=External;
Note=Produced by a -2 ribosomal frameshift.;
-!- 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=AAA46273.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAA46274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M96262; AAA46273.2; ALT_INIT; Genomic_RNA.
EMBL; M96262; AAA46274.1; ALT_INIT; Genomic_RNA.
EMBL; L04493; AAA47101.1; -; Genomic_RNA.
PIR; A36861; A36861.
PIR; A45392; A45392.
PIR; B36861; B36861.
SMR; Q04561; -.
IntAct; Q04561; 2.
MEROPS; C32.001; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006687; Genome.
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:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
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.
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;
Activation of host autophagy by virus; 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;
Reference proteome; Ribosomal frameshifting;
RNA-directed RNA polymerase; Serine protease; Thiol protease;
Transferase; Transmembrane; Transmembrane helix; Viral immunoevasion;
Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 3855 Replicase polyprotein 1ab.
/FTId=PRO_0000036683.
CHAIN 1 384 Nsp1. {ECO:0000250}.
/FTId=PRO_0000410828.
CHAIN 1 180 Nsp1-alpha papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000036685.
CHAIN 181 385 Nsp1-beta papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000036686.
CHAIN 386 1463 Nsp2 cysteine proteinase. {ECO:0000255}.
/FTId=PRO_0000036687.
CHAIN 1464 1693 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000036688.
CHAIN 1694 1896 3C-like serine proteinase. {ECO:0000250}.
/FTId=PRO_0000036689.
CHAIN 1897 2351 Non-structural protein 5-6-7.
{ECO:0000250}.
/FTId=PRO_0000036690.
CHAIN 1897 2066 Non-structural protein 5. {ECO:0000250}.
/FTId=PRO_0000423126.
CHAIN 2067 2082 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000423127.
CHAIN 2083 2231 Non-structural protein 7-alpha.
{ECO:0000250}.
/FTId=PRO_0000423128.
CHAIN 2232 2351 Non-structural protein 7-beta.
{ECO:0000250}.
/FTId=PRO_0000423129.
CHAIN 2352 3037 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000036691.
CHAIN 2352 2396 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000036692.
CHAIN 3038 3479 Helicase. {ECO:0000250}.
/FTId=PRO_0000036693.
CHAIN 3480 3703 Non-structural protein 11. {ECO:0000250}.
/FTId=PRO_0000036694.
CHAIN 3704 3855 Non-structural protein 12. {ECO:0000250}.
/FTId=PRO_0000036695.
TRANSMEM 1134 1154 Helical. {ECO:0000255}.
TRANSMEM 1179 1199 Helical. {ECO:0000255}.
TRANSMEM 1252 1272 Helical. {ECO:0000255}.
TRANSMEM 1468 1488 Helical. {ECO:0000255}.
TRANSMEM 1521 1541 Helical. {ECO:0000255}.
TRANSMEM 1543 1563 Helical. {ECO:0000255}.
TRANSMEM 1573 1593 Helical. {ECO:0000255}.
TRANSMEM 1609 1629 Helical. {ECO:0000255}.
TRANSMEM 1919 1939 Helical. {ECO:0000255}.
TRANSMEM 1943 1963 Helical. {ECO:0000255}.
TRANSMEM 1977 1997 Helical. {ECO:0000255}.
TRANSMEM 2020 2040 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 1694 1896 Peptidase S32. {ECO:0000255|PROSITE-
ProRule:PRU00826}.
DOMAIN 2783 2917 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 3038 3101 AV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
DOMAIN 3151 3310 (+)RNA virus helicase ATP-binding.
DOMAIN 3311 3440 (+)RNA virus helicase C-terminal.
ZN_FING 8 28 C4-type; atypical.
NP_BIND 3186 3193 ATP. {ECO:0000250}.
REGION 69 182 PCP1-alpha.
REGION 269 384 PCP1-beta.
REGION 418 505 OTU-like.
REGION 1149 1272 HD1.
REGION 1327 1351 WCCH.
REGION 1468 1629 HD2.
REGION 1919 2040 HD3.
ACT_SITE 76 76 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872,
ECO:0000269|PubMed:7769711}.
ACT_SITE 146 146 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872,
ECO:0000269|PubMed:7769711}.
ACT_SITE 276 276 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873,
ECO:0000269|PubMed:7769711}.
ACT_SITE 345 345 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873,
ECO:0000269|PubMed:7769711}.
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 1732 1732 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826,
ECO:0000269|PubMed:19646449}.
ACT_SITE 1757 1757 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826,
ECO:0000269|PubMed:19646449}.
ACT_SITE 1810 1810 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826,
ECO:0000269|PubMed:19646449}.
METAL 3044 3044 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3047 3047 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3057 3057 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3062 3062 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3065 3065 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3067 3067 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3069 3069 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3071 3071 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3078 3078 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3080 3080 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3087 3087 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3090 3090 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
SITE 180 181 Cleavage; by autolysis. {ECO:0000255}.
SITE 385 386 Cleavage; by autolysis. {ECO:0000250}.
SITE 1463 1464 Cleavage; by CP2. {ECO:0000255}.
SITE 1693 1694 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 1896 1897 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2066 2067 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2082 2083 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2231 2232 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2351 2352 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3037 3038 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3088 3088 Involved in mRNA transcription process.
{ECO:0000250}.
SITE 3479 3480 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3703 3704 Cleavage; by 3CLSP. {ECO:0000250}.
VAR_SEQ 2397 3855 Missing (in isoform Replicase polyprotein
1a). {ECO:0000305}.
/FTId=VSP_032892.
MUTAGEN 76 76 C->G,S: Complete loss of cleavage between
nsp1-alpha and nsp1-beta.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 92 92 H->F,Y: No effect.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 115 115 H->A: No effect.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 115 115 H->Y: 50% loss of cleavage between nsp1-
alpha and nsp1-beta.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 146 146 H->D,F,I,N,Y: Complete loss of cleavage
between nsp1-alpha and nsp1-beta.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 157 157 H->D: 20% loss of cleavage between nsp1-
alpha and nsp1-beta.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 157 157 H->I: 90% loss of cleavage between nsp1-
alpha and nsp1-beta.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 157 157 H->N: 50% loss of cleavage between nsp1-
alpha and nsp1-beta.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 157 157 H->Y: No effect.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 276 276 C->I,L,R,S: Complete loss of cleavage
between nsp1-beta and nsp2.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 345 345 H->D,Y: Complete loss of cleavage between
nsp1-beta and nsp2.
{ECO:0000269|PubMed:7769711}.
CONFLICT 3502 3502 T -> V (in Ref. 3; AAA47101).
{ECO:0000305}.
CONFLICT 3740 3740 V -> I (in Ref. 3; AAA47101).
{ECO:0000305}.
SEQUENCE 3855 AA; 421332 MW; 421F613ED2E4858F CRC64;
MSGTFSRCMC TPAARVFWNA GQVFCTRCLS ARSLLSPELQ DTDLGAVGLF YKPRDKLHWK
VPIGIPQVEC TPSGCCWLSA VFPLARMTSG NHNFLQRLVK VADVLYRDGC LAPRHLRELQ
VYERGCNWYP ITGPVPGMGL FANSMHVSDQ PFPGATHVLT NSPLPQQACR QPFCPFEEAH
SSVYRWKKFV VFTDSSLNGR SRMMWTPESD DSAALEVLPP ELERQVEILI RSFPAHHPVD
LADWELTESP ENGFSFNTSH SCGHLVQNPD VFDGKCWLSC FLGQSVEVRC HEEHLADAFG
YQTKWGVHGK YLQRRLQVRG IRAVVDPDGP IHVEALSCPQ SWIRHLTLDD DVTPGFVRLT
SLRIVPNTEP TTSRIFRFGA HKWYGAAGKR ARAKRAAKSE KDSAPTPKVA LPVPTCGITT
YSPPTDGSCG WHVLAAIMNR MINGDFTSPL TQYNRPEDDW ASDYDLVQAI QCLRLPATVV
RNRACPNAKY LIKLNGVHWE VEVRSGMAPR SLSRECVVGV CSEGCVAPPY PADGLPKRAL
EALASAYRLP SDCVSSGIAD FLANPPPQEF WTLDKMLTSP SPERSGFSSL YKLLLEVVPQ
KCGATEGAFI YAVERMLKDC PSSKQAMALL AKIKVPSSKA PSVSLDECFP TDVLADFEPA
SQERPQSSGA AVVLCSPDAK EFEEAAPEEV QESGHKAVHS ALLAEGPNNE QVQVVAGEQL
KLGGCGLAVG NAHEGALVSA GLINLVGGNL SPSDPMKENM LNSREDEPLD LSQPAPASTT
TLVREQTPDN PGSDAGALPV TVREFVPTGP ILCHVEHCGT ESGDSSSPLD LSDAQTLDQP
LNLSLAAWPV RATASDPGWV HGRREPVFVK PRNAFSDGDS ALQFGELSES SSVIEFDRTK
DAPVVDAPVD LTTSNEALSV VDPFEFAELK RPRFSAQALI DRGGPLADVH AKIKNRVYEQ
CLQACEPGSR ATPATREWLD KMWDRVDMKT WRCTSQFQAG RILASLKFLP DMIQDTPPPV
PRKNRASDNA GLKQLVAQWD RKLSVTPPPK PVGPVLDQIV PPPTDIQQED VTPSDGPPHA
PDFPSRVSTG GSWKGLMLSG TRLAGSISQR LMTWVFEVFS HLPAFMLTLF SPRGSMAPGD
WLFAGVVLLA LLLCRSYPIL GCLPLLGVFS GSLRRVRLGV FGSWMAFAVF LFSTPSNPVG
SSCDHDSPEC HAELLALEQR QLWEPVRGLV VGPSGLLCVI LGKLLGGSRY LWHVLLRLCM
LADLALSLVY VVSQGRCHKC WGKCIRTAPA EVALNVFPFS RATRVSLVSL CDRFQTPKGV
DPVHLATGWR GCWRGESPIH QPHQKPIAYA NLDEKKMSAQ TVVAVPYDPS QAIKCLKVLQ
AGGAIVDQPT PEVVRVSEIP FSAPFFPKVP VNPDCRVVVD SDTFVAAVRC GYSTAQLVLG
RGNFAKLNQT PPRNSISTKT TGGASYTLAV AQVSAWTLVH FILGLWFTSP QVCGRGTADP
WCSNPFSYPT YGPGVVCSSR LCVSADGVTL PLFSAVAQLS GREVGIFILV LVSLTALAHR
MALKADMLVV FSAFCAYAWP MSSWLICFFP ILLKWVTLHP LTMLWVHSFL VFCLPAAGIL
SLGITGLLWA IGRFTQVAGI ITPYDIHQYT SGPRGAAAVA TAPEGTYMAA VRRAALTGRT
LIFTPSAVGS LLEGAFRTHK PCLNTVNVVG SSLGSGGVFT IDGRRTVVTA AHVLNGDTAR
VTGDSYNRMH TFKTNGDYAW SHADDWQGVA PVVKVAKGYR GRAYWQTSTG VEPGIIGEGF
AFCFTNCGDS GSPVISESGD LIGIHTGSNK LGSGLVTTPE GETCTIKETK LSDLSRHFAG
PSVPLGDIKL SPAIIPDVTS IPSDLASLLA SVPVVEGGLS TVQLLCVFFL LWRMMGHAWT
PIVAVGFFLL NEILPAVLVR AVFSFALFVL AWATPWSAQV LMIRLLTASL NRNKLSLAFY
ALGGVVGLAA EIGTFAGRLS ELSQALSTYC FLPRVLAMTS CVPTIIIGGL HTLGVILWLF
KYRCLHNMLV GDGSFSSAFF LRYFAEGNLR KGVSQSCGMN NESLTAALAC KLSQADLDFL
SSLTNFKCFV SASNMKNAAG QYIEAAYAKA LRQELASLVQ IDKMKGVLSK LEAFAETATP
SLDIGDVIVL LGQHPHGSIL DINVGTERKT VSVQETRSLG GSKFSVCTVV SNTPVDALTG
IPLQTPTPLF ENGPRHRSEE DDLKVERMKK HCVSLGFHNI NGKVYCKIWD KSTGDTFYTD
DSRYTQDHAF QDRSADYRDR DYEGVQTTPQ QGFDPKSETP VGTVVIGGIT YNRYLIKGKE
VLVPKPDNCL EAAKLSLEQA LAGMGQTCDL TAAEVEKLKR IISQLQGLTT EQALNCLLAA
SGLTRCGRGG LVVTETAVKI IKYHSRTFTL GPLDLKVTSE VEVKKSTEQG HAVVANLCSG
VILMRPHPPS LVDVLLKPGL DTIPGIQPGH GAGNMGVDGS IWDFETAPTK AELELSKQII
QACEVRRGDA PNLQLPYKLY PVRGDPERHK GRLINTRFGD LPYKTPQDTK SAIHAACCLH
PNGAPVSDGK STLGTTLQHG FELYVPTVPY SVMEYLDSRP DTPFMCTKHG TSKAAAEDLQ
KYDLSTQGFV LPGVLRLVRR FIFGHIGKAP PLFLPSTYPA KNSMAGINGQ RFPTKDVQSI
PEIDEMCARA VKENWQTVTP CTLKKQYCSK PKTRTILGTN NFIALAHRSA LSGVTQAFMK
KAWKSPIALG KNKFKELHCT VAGRCLEADL ASCDRSTPAI VRWFVANLLY ELAGCEEYLP
SYVLNCCHDL VATQDGAFTK RGGLSSGDPV TSVSNTVYSL VIYAQHMVLS ALKMGHEIGL
KFLEEQLKFE DLLEIQPMLV YSDDLVLYAE RPTFPNYHWW VEHLDLMLGF RTDPKKTVIT
DKPSFLGCRI EAGRQLVPNR DRILAALAYH MKAQNASEYY ASAAAILMDS CACIDHDPEW
YEDLICGIAR CARQDGYSFP GPAFFMSMWE KLRSHNEGKK FRHCGICDAK ADYASACGLD
LCLFHSHFHQ HCPVTLSCGH HAGSKECSQC QSPVGAGRSP LDAVLKQIPY KPPRTVIMKV
GNKTTALDPG RYQSRRGLVA VKRGIAGNEV DLSDGDYQVV PLLPTCKDIN MVKVACNVLL
SKFIVGPPGS GKTTWLLSQV QDDDVIYTPT HQTMFDIVSA LKVCRYSIPG ASGLPFPPPA
RSGPWVRLIA SGHVPGRVSY LDEAGYCNHL DILRLLSKTP LVCLGDLQQL HPVGFDSYCY
VFDQMPQKQL TTIYRFGPNI CAAIQPCYRE KLESKARNTR VVFTTRPVAF GQVLTPYHKD
RIGSAITIDS SQGATFDIVT LHLPSPKSLN KSRALVAITR ARHGLFIYDP HNQLQEFFNL
TPERTDCNLV FSRGDELVVL NADNAVTTVA KALETGPSRF RVSDPRCKSL LAACSASLEG
SCMPLPQVAH NLGFYFSPDS PTFAPLPKEL APHWPVVTHQ NNRAWPDRLV ASMRPIDARY
SKPMVGAGYV VGPSTFLGTP GVVSYYLTLY IRGEPQALPE TLVSTGRIAT DCREYLDAAE
EEAAKELPHA FIGDVKGTTV GGCHHITSKY LPRSLPKDSV AVVGVSSPGR AAKAVCTLTD
VYLPELRPYL QPETASKCWK LKLDFRDVRL MVWKGATAYF QLEGLTWSAL PDYARFIQLP
KDAVVYIDPC IGPATANRKV VRTTDWRADL AVTPYDYGAQ NILTTAWFED LGPQWKILGL
QPFRRAFGFE NTEDWAILAR RMNDGKDYTD YNWNCVRERP HAIYGRARDH TYHFAPGTEL
QVELGKPRLP PGQVP


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