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 R1A_CVHSA               Reviewed;        4382 AA.
P0C6U8; P59641;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 86.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=Leader protein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65 homolog;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=PL2-PRO;
AltName: Full=Papain-like proteinase;
Short=PL-PRO;
AltName: Full=SARS coronavirus main proteinase;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome
coronavirus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=227859;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9675; Paguma larvata (Masked palm civet).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Urbani;
PubMed=12730500; DOI=10.1126/science.1085952;
Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R.,
Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H.,
Tong S., Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D.,
Erdman D.D., Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E.,
Sanchez A., Liffick S., Holloway B., Limor J., McCaustland K.,
Olsen-Rasmussen M., Fouchier R., Guenther S., Osterhaus A.D.M.E.,
Drosten C., Pallansch M.A., Anderson L.J., Bellini W.J.;
"Characterization of a novel coronavirus associated with severe acute
respiratory syndrome.";
Science 300:1394-1399(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Tor2;
PubMed=12730501; DOI=10.1126/science.1085953;
Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A.,
Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y.,
Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L.,
Leach S.R., Mayo M., McDonald H., Montgomery S.B., Pandoh P.K.,
Petrescu A.S., Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E.,
Stott J.M., Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N.,
Bernard K., Booth T.F., Bowness D., Czub M., Drebot M., Fernando L.,
Flick R., Garbutt M., Gray M., Grolla A., Jones S., Feldmann H.,
Meyers A., Kabani A., Li Y., Normand S., Stroher U., Tipples G.A.,
Tyler S., Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M.,
Petric M., Skowronski D.M., Upton C., Roper R.L.;
"The genome sequence of the SARS-associated coronavirus.";
Science 300:1399-1404(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1;
PubMed=12853594; DOI=10.1056/NEJM200307103490216;
Tsui S.K.W., Chim S.S.C., Lo Y.M.D.;
"Coronavirus genomic-sequence variations and the epidemiology of the
severe acute respiratory syndrome.";
N. Engl. J. Med. 349:187-188(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate GZ50, Isolate SZ16, and Isolate SZ3;
PubMed=12958366; DOI=10.1126/science.1087139;
Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L.,
Luo S.W., Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L.,
Chan K.W., Lim W., Shortridge K.F., Yuen K.Y., Peiris J.S.M.,
Poon L.L.M.;
"Isolation and characterization of viruses related to the SARS
coronavirus from animals in southern China.";
Science 302:276-278(2003).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU-39849;
PubMed=12876307; DOI=10.1177/15353702-0322807-13;
Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C.,
Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B.,
Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.;
"The complete genome sequence of severe acute respiratory syndrome
coronavirus strain HKU-39849 (HK-39).";
Exp. Biol. Med. 228:866-873(2003).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Sin2500, Isolate Sin2677, Isolate Sin2679,
Isolate Sin2748, and Isolate sin2774;
PubMed=12781537; DOI=10.1016/S0140-6736(03)13414-9;
Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M.,
Liu E.T.;
"Comparative full-length genome sequence analysis of 14 SARS
coronavirus isolates and common mutations associated with putative
origins of infection.";
Lancet 361:1779-1785(2003).
[7]
ERRATUM.
Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M.,
Liu E.T.;
Lancet 361:1832-1832(2003).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate ZJ01;
PubMed=14527350;
Li L., Wang Z., Lu Y., Bao Q., Chen S., Wu N., Cheng S., Weng J.,
Zhang Y., Yan J., Mei L., Wang X., Zhu H., Yu Y., Zhang M., Li M.,
Yao J., Lu Q., Yao P., Bo X., Wo J., Wang S., Hu S.;
"Severe acute respiratory syndrome-associated coronavirus genotype and
its characterization.";
Chin. Med. J. 116:1288-1292(2003).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and
Isolate GD01;
Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W.,
Jiang T., Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y.,
Li X., Lu F., Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L.,
Deng Y., Dong W., Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H.,
Li S., Li S., Li W., Li W., Lin W., Liu J., Liu Z., Lu H., Ni P.,
Qi Q., Sun Y., Tang L., Tong Z., Wang J., Wang X., Wu Q., Xi Y.,
Xu Z., Yang L., Ye C., Ye J., Zhang B., Zhang F., Zhang J., Zhang X.,
Zhou J., Yang H.;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TW1;
Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.;
"The complete genome of SARS coronavirus clone TW1.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate FRA;
PubMed=14645828; DOI=10.1126/science.302.5650.1504b;
Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K.,
Censini S., Guidotti S., Masignani V., Scarselli M., Mora M.,
Donati C., Han J.H., Song H.C., Abrignani S., Covacci A., Rappuoli R.;
"Phylogeny of the SARS coronavirus.";
Science 302:1504-1505(2003).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Frankfurt-1;
Thiel V., Hertzig T., Putics A., Ivanov K.A., Schelle B., Bayer S.,
Scheiner B., Weinand H., Weissbrich B., Ziebuhr J.;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TWC;
Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee S.C., Lin Y.-C.,
Hsu C.-K., Chen H.-Y., Chang J.G., Chen P.-J., Su I.-J.;
"Genomic sequence of SARS isolate from the first fatal case in
Taiwan.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Shanghai QXC1;
Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
"Analysis of SARS coronavirus genome in Shanghai isolates.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HSR 1;
Canducci F., Clementi M., Poli G., Vicenzi E.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3;
Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L.,
Shih M.-C.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and
Isolate TWY;
Shu H.Y., Wu K.M., Tsai S.F.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[18]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate AS;
Balotta C., Corvasce S., Violin M., Galli M., Moroni M.,
Vigevani G.M., Ruan Y.J., Salemi M.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[19]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate ZJ01;
Wang Z., Cheng S., Zhang Y.;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[20]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-507 AND 1655-4382.
STRAIN=Isolate Shanghai LY;
Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[21]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=12917450; DOI=10.1099/vir.0.19424-0;
Thiel V., Ivanov K.A., Putics A., Hertzig T., Schelle B., Bayer S.,
Weissbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E.,
Ziebuhr J.;
"Mechanisms and enzymes involved in SARS coronavirus genome
expression.";
J. Gen. Virol. 84:2305-2315(2003).
[22]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=15331731; DOI=10.1128/JVI.78.18.9977-9986.2004;
Prentice E., McAuliffe J., Lu X., Subbarao K., Denison M.R.;
"Identification and characterization of severe acute respiratory
syndrome coronavirus replicase proteins.";
J. Virol. 78:9977-9986(2004).
[23]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
STRAIN=Isolate Urbani;
PubMed=15564471; DOI=10.1128/JVI.78.24.13600-13612.2004;
Harcourt B.H., Jukneliene D., Kanjanahaluethai A., Bechill J.,
Severson K.M., Smith C.M., Rota P.A., Baker S.C.;
"Identification of severe acute respiratory syndrome coronavirus
replicase products and characterization of papain-like protease
activity.";
J. Virol. 78:13600-13612(2004).
[24]
FUNCTION OF NSP8.
PubMed=17024178; DOI=10.1038/sj.emboj.7601368;
Imbert I., Guillemot J.-C., Bourhis J.-M., Bussetta C., Coutard B.,
Egloff M.-P., Ferron F., Gorbalenya A.E., Canard B.;
"A second, non-canonical RNA-dependent RNA polymerase in SARS
coronavirus.";
EMBO J. 25:4933-4942(2006).
[25]
FUNCTION OF NSP3.
PubMed=17692280; DOI=10.1016/j.abb.2007.07.006;
Lindner H.A., Lytvyn V., Qi H., Lachance P., Ziomek E., Menard R.;
"Selectivity in ISG15 and ubiquitin recognition by the SARS
coronavirus papain-like protease.";
Arch. Biochem. Biophys. 466:8-14(2007).
[26]
FUNCTION OF NSP3.
PubMed=19369340; DOI=10.1128/JVI.02220-08;
Frieman M., Ratia K., Johnston R.E., Mesecar A.D., Baric R.S.;
"Severe acute respiratory syndrome coronavirus papain-like protease
ubiquitin-like domain and catalytic domain regulate antagonism of IRF3
and NF-kappaB signaling.";
J. Virol. 83:6689-6705(2009).
[27]
FUNCTION OF NSP1.
PubMed=22174690; DOI=10.1371/journal.ppat.1002433;
Huang C., Lokugamage K.G., Rozovics J.M., Narayanan K., Semler B.L.,
Makino S.;
"SARS coronavirus nsp1 protein induces template-dependent
endonucleolytic cleavage of mRNAs: viral mRNAs are resistant to nsp1-
induced RNA cleavage.";
PLoS Pathog. 7:E1002433-E1002433(2011).
[28]
FUNCTION OF NSP1.
PubMed=23035226; DOI=10.1128/JVI.01958-12;
Lokugamage K.G., Narayanan K., Huang C., Makino S.;
"Severe acute respiratory syndrome coronavirus protein nsp1 is a novel
eukaryotic translation inhibitor that represses multiple steps of
translation initiation.";
J. Virol. 86:13598-13608(2012).
[29]
3D-STRUCTURE MODELING OF 3241-3540, AND CHARACTERIZATION.
PubMed=12746549; DOI=10.1126/science.1085658;
Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.;
"Coronavirus main proteinase (3CLpro) structure: basis for design of
anti-SARS drugs.";
Science 300:1763-1767(2003).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4118-4230 (NSP9).
STRAIN=Isolate Frankfurt-1;
PubMed=12925794; DOI=10.1107/S0907444903016779;
Campanacci V., Egloff M.-P., Longhi S., Ferron F., Rancurel C.,
Salomoni A., Durousseau C., Tocque F., Bremond N., Dobbe J.C.,
Snijder E.J., Canard B., Cambillau C.;
"Structural genomics of the SARS coronavirus: cloning, expression,
crystallization and preliminary crystallographic study of the Nsp9
protein.";
Acta Crystallogr. D 59:1628-1631(2003).
[31]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 4118-4230.
PubMed=15007178; DOI=10.1073/pnas.0307877101;
Egloff M.-P., Ferron F., Campanacci V., Longhi S., Rancurel C.,
Dutartre H., Snijder E.J., Gorbalenya A.E., Cambillau C., Canard B.;
"The severe acute respiratory syndrome-coronavirus replicative protein
nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus
world.";
Proc. Natl. Acad. Sci. U.S.A. 101:3792-3796(2004).
[32]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230.
PubMed=14962394; DOI=10.1016/j.str.2004.01.016;
Sutton G., Fry E., Carter L., Sainsbury S., Walter T., Nettleship J.,
Berrow N., Owens R., Gilbert R., Davidson A., Siddell S., Poon L.L.M.,
Diprose J., Alderton D., Walsh M., Grimes J.M., Stuart D.I.;
"The nsp9 replicase protein of SARS-coronavirus, structure and
functional insights.";
Structure 12:341-353(2004).
[33]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 3837-4117 AND 3920-4117, AND
INTERACTION OF NSP7 WITH NSP8.
PubMed=16228002; DOI=10.1038/nsmb999;
Zhai Y., Sun F., Li X., Pang H., Xu X., Bartlam M., Rao Z.;
"Insights into SARS-CoV transcription and replication from the
structure of the nsp7-nsp8 hexadecamer.";
Nat. Struct. Mol. Biol. 12:980-986(2005).
[34]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1002-1176.
PubMed=16271890; DOI=10.1016/j.str.2005.07.022;
Saikatendu K.S., Joseph J.S., Subramanian V., Clayton T., Griffith M.,
Moy K., Velasquez J., Neuman B.W., Buchmeier M.J., Stevens R.C.,
Kuhn P.;
"Structural basis of severe acute respiratory syndrome coronavirus
ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of
nsP3.";
Structure 13:1665-1675(2005).
[35]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1541-1854.
PubMed=16581910; DOI=10.1073/pnas.0510851103;
Ratia K., Saikatendu K.S., Santarsiero B.D., Barretto N., Baker S.C.,
Stevens R.C., Mesecar A.D.;
"Severe acute respiratory syndrome coronavirus papain-like protease:
structure of a viral deubiquitinating enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 103:5717-5722(2006).
[36]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4240-4362.
STRAIN=Isolate Tor2;
PubMed=16873246; DOI=10.1128/JVI.00467-06;
Joseph J.S., Saikatendu K.S., Subramanian V., Neuman B.W., Brooun A.,
Griffith M., Moy K., Yadav M.K., Velasquez J., Buchmeier M.J.,
Stevens R.C., Kuhn P.;
"Crystal structure of nonstructural protein 10 from the severe acute
respiratory syndrome coronavirus reveals a novel fold with two zinc-
binding motifs.";
J. Virol. 80:7894-7901(2006).
[37]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4231-4378.
PubMed=16873247; DOI=10.1128/JVI.00483-06;
Su D., Lou Z., Sun F., Zhai Y., Yang H., Zhang R., Joachimiak A.,
Zhang X.C., Bartlam M., Rao Z.;
"Dodecamer structure of severe acute respiratory syndrome coronavirus
nonstructural protein nsp10.";
J. Virol. 80:7902-7908(2006).
[38]
STRUCTURE BY NMR OF 13-127.
PubMed=17202208; DOI=10.1128/JVI.01939-06;
Almeida M.S., Johnson M.A., Herrmann T., Geralt M., Wuthrich K.;
"Novel beta-barrel fold in the nuclear magnetic resonance structure of
the replicase nonstructural protein 1 from the severe acute
respiratory syndrome coronavirus.";
J. Virol. 81:3151-3161(2007).
[39]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3241-3546.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of Sars coronavirus main proteinase(3CLPRO).";
Submitted (JUL-2007) to the PDB data bank.
-!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for
the cleavages located at the N-terminus of replicase polyprotein.
In addition, PL-PRO possesses a deubiquitinating/deISGylating
activity and processes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains from cellular substrates. Antagonizes innate
immune induction of type I interferon by blocking the
phosphorylation, dimerization and subsequent nuclear translocation
of host IRF-3.
-!- FUNCTION: The main proteinase 3CL-PRO is responsible for the
majority of cleavages as it cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog
Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity). Also contains an
ADP-ribose-1''-phosphate (ADRP)-binding function.
{ECO:0000255|PROSITE-ProRule:PRU00772,
ECO:0000269|PubMed:17024178, ECO:0000269|PubMed:17692280,
ECO:0000269|PubMed:19369340, ECO:0000269|PubMed:22174690,
ECO:0000269|PubMed:23035226}.
-!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity
to the polymerase, maybe by binding to dsRNA or by producing
primers utilized by the latter.
-!- FUNCTION: Nsp9 is a ssRNA-binding protein.
-!- FUNCTION: Non-structural protein 1: binds to the 40S ribosomal
subunit and inhibits host translation. The nsp1-40S ribosome
complex further induces an endonucleolytic cleavage near the 5'UTR
of host mRNAs, targeting them for degradation. Viral mRNAs are not
susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks
to the presence of a 5'-end leader sequence and are therefore
protected from degradation. By suppressing host gene expression,
nsp1 facilitates efficient viral gene expression in infected cells
and evasion from host immune response.
-!- 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).
-!- CATALYTIC ACTIVITY: TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the
two peptides corresponding to the two self-cleavage sites of the
SARS 3C-like proteinase are the two most reactive peptide
substrates. The enzyme exhibits a strong preference for substrates
containing Gln at P1 position and Leu at P2 position.
-!- SUBUNIT: Eight copies of nsp7 and eight copies of nsp8 assemble to
form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a
dodecamer.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 6: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 7: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 8: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 9: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 10: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6U8-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X7-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. 3CL-PRO and PL-PRO proteinases are
autocatalytically processed (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- CAUTION: Isolates SZ3 and SZ16 have been isolated from Paguma
larvata and are described as SARS-like in literature.
{ECO:0000305}.
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EMBL; AY278741; AAP13439.1; -; Genomic_RNA.
EMBL; AY274119; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY278554; AAP13575.1; -; Genomic_RNA.
EMBL; AY282752; AAP30712.1; -; Genomic_RNA.
EMBL; AY304495; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY304486; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY304488; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283795; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283796; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283797; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283798; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY286320; AAR16181.1; -; Genomic_RNA.
EMBL; AY278488; AAP30029.1; -; Genomic_RNA.
EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY278489; AAP51226.1; -; Genomic_RNA.
EMBL; AY291451; AAP37016.1; -; Genomic_RNA.
EMBL; AY310120; AAP50484.1; -; Genomic_RNA.
EMBL; AY291315; AAP33695.1; -; Genomic_RNA.
EMBL; AY323977; AAP72974.2; -; Genomic_RNA.
EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY338174; AAQ01595.1; -; Genomic_RNA.
EMBL; AY338175; AAQ01607.1; -; Genomic_RNA.
EMBL; AY348314; AAP97880.1; -; Genomic_RNA.
EMBL; AP006557; BAC81347.1; -; Genomic_RNA.
EMBL; AP006558; BAC81361.1; -; Genomic_RNA.
EMBL; AP006559; BAC81375.1; -; Genomic_RNA.
EMBL; AP006560; BAC81389.1; -; Genomic_RNA.
EMBL; AP006561; BAC81403.1; -; Genomic_RNA.
EMBL; AY427439; AAQ94059.1; -; Genomic_RNA.
EMBL; AY322205; AAP82966.1; -; Genomic_RNA.
EMBL; AY322206; AAP82976.1; -; Genomic_RNA.
EMBL; AY463059; -; NOT_ANNOTATED_CDS; Genomic_RNA.
RefSeq; NP_828850.1; NC_004718.3. [P0C6U8-1]
PDB; 1P76; Model; -; A=3241-3541, B=4225-4231.
PDB; 1P9T; Model; -; A=3241-3544.
PDB; 1PA5; Model; -; A=3241-3546.
PDB; 1PUK; Model; -; A=3241-3550.
PDB; 1Q1X; Model; -; A=3241-3542.
PDB; 1Q2W; X-ray; 1.86 A; A/B=3241-3544.
PDB; 1QZ8; X-ray; 2.70 A; A/B=4118-4230.
PDB; 1UJ1; X-ray; 1.90 A; A/B=3241-3546.
PDB; 1UK2; X-ray; 2.20 A; A/B=3241-3546.
PDB; 1UK3; X-ray; 2.40 A; A/B=3241-3546.
PDB; 1UK4; X-ray; 2.50 A; A/B=3241-3546.
PDB; 1UW7; X-ray; 2.80 A; A=4118-4230.
PDB; 1WOF; X-ray; 2.00 A; A/B=3241-3546.
PDB; 1YSY; NMR; -; A=3837-3919.
PDB; 1Z1I; X-ray; 2.80 A; A=3241-3546.
PDB; 1Z1J; X-ray; 2.80 A; A/B=3241-3546.
PDB; 2A5A; X-ray; 2.08 A; A=3241-3546.
PDB; 2A5I; X-ray; 1.88 A; A=3241-3546.
PDB; 2A5K; X-ray; 2.30 A; A/B=3241-3546.
PDB; 2ACF; X-ray; 1.40 A; A/B/C/D=1002-1176.
PDB; 2AHM; X-ray; 2.40 A; A/B/C/D=3837-3919, E/F/G/H=3920-4117.
PDB; 2AJ5; Model; -; A=3241-3546.
PDB; 2ALV; X-ray; 1.90 A; A=3241-3543.
PDB; 2AMD; X-ray; 1.85 A; A/B=3241-3546.
PDB; 2AMQ; X-ray; 2.30 A; A/B=3241-3546.
PDB; 2BX3; X-ray; 2.00 A; A=3241-3546.
PDB; 2BX4; X-ray; 2.79 A; A=3241-3546.
PDB; 2C3S; X-ray; 1.90 A; A=3241-3546.
PDB; 2D2D; X-ray; 2.70 A; A/B=3241-3546.
PDB; 2DUC; X-ray; 1.70 A; A/B=3241-3546.
PDB; 2FAV; X-ray; 1.80 A; A/B/C=1000-1173.
PDB; 2FE8; X-ray; 1.85 A; A/B/C=1541-1854.
PDB; 2FYG; X-ray; 1.80 A; A=4240-4362.
PDB; 2G9T; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=4231-4382.
PDB; 2GA6; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=4231-4382.
PDB; 2GDT; NMR; -; A=13-127.
PDB; 2GRI; NMR; -; A=819-930.
PDB; 2GT7; X-ray; 1.82 A; A/B=3241-3546.
PDB; 2GT8; X-ray; 2.00 A; A=3241-3546.
PDB; 2GTB; X-ray; 2.00 A; A=3241-3546.
PDB; 2GX4; X-ray; 1.93 A; A=3241-3546.
PDB; 2GZ7; X-ray; 1.86 A; A=3241-3546.
PDB; 2GZ8; X-ray; 1.97 A; A=3241-3546.
PDB; 2GZ9; X-ray; 2.17 A; A=3241-3546.
PDB; 2H2Z; X-ray; 1.60 A; A=3241-3546.
PDB; 2HOB; X-ray; 1.95 A; A=3241-3546.
PDB; 2HSX; NMR; -; A=13-127.
PDB; 2IDY; NMR; -; A=819-930.
PDB; 2KAF; NMR; -; A=1473-1538.
PDB; 2KQV; NMR; -; A=1345-1538.
PDB; 2KQW; NMR; -; A=1345-1538.
PDB; 2KYS; NMR; -; A=3837-3919.
PDB; 2LIZ; NMR; -; A=3427-3546.
PDB; 2OP9; X-ray; 1.80 A; A/B=3241-3541.
PDB; 2PWX; X-ray; 2.50 A; A=3241-3546.
PDB; 2W2G; X-ray; 2.22 A; A/B=1207-1470.
PDB; 2WCT; X-ray; 2.79 A; A/B/C/D=1207-1470.
PDB; 2Z3C; X-ray; 1.79 A; A=3241-3546.
PDB; 2Z3D; X-ray; 2.10 A; A=3241-3546.
PDB; 2Z3E; X-ray; 2.32 A; A=3241-3546.
PDB; 2ZU4; X-ray; 1.93 A; A=3241-3546.
PDB; 2ZU5; X-ray; 1.65 A; A=3241-3546.
PDB; 3ATW; X-ray; 2.36 A; A/B=3241-3546.
PDB; 3AVZ; X-ray; 2.46 A; A=3241-3546.
PDB; 3AW0; X-ray; 2.30 A; A=3241-3546.
PDB; 3AW1; X-ray; 2.00 A; A/B=3241-3546.
PDB; 3E91; X-ray; 2.55 A; A/B=3241-3546.
PDB; 3EA7; X-ray; 2.65 A; A/B=3241-3546.
PDB; 3EA8; X-ray; 2.25 A; A=3241-3546.
PDB; 3EA9; X-ray; 2.40 A; A=3241-3546.
PDB; 3EAJ; X-ray; 2.70 A; A/B=3241-3546.
PDB; 3EE7; X-ray; 2.60 A; A/B/C/D=4118-4230.
PDB; 3F9E; X-ray; 2.50 A; A=3241-3546.
PDB; 3F9F; X-ray; 2.30 A; A/B=3241-3546.
PDB; 3F9G; X-ray; 2.60 A; A/B=3241-3541.
PDB; 3F9H; X-ray; 2.90 A; A/B=3241-3546.
PDB; 3FZD; X-ray; 2.35 A; A=3241-3541.
PDB; 3IWM; X-ray; 3.20 A; A/B/C/D=3241-3546.
PDB; 3M3S; X-ray; 2.30 A; A/B=3241-3546.
PDB; 3M3T; X-ray; 2.90 A; A=3241-3546.
PDB; 3M3V; X-ray; 2.70 A; A/B=3241-3546.
PDB; 3MJ5; X-ray; 2.63 A; A/B=1541-1855.
PDB; 3R24; X-ray; 2.00 A; B=4240-4382.
PDB; 3SN8; X-ray; 1.99 A; A=3241-3546.
PDB; 3SNA; X-ray; 3.05 A; A=3241-3541.
PDB; 3SNB; X-ray; 2.40 A; A=3241-3546.
PDB; 3SNC; X-ray; 2.58 A; A=3241-3546.
PDB; 3SND; X-ray; 1.89 A; A/B=3241-3546.
PDB; 3SNE; X-ray; 2.60 A; A=3241-3546.
PDB; 3SZN; X-ray; 1.69 A; A=3241-3546.
PDB; 3TIT; X-ray; 1.99 A; A=3241-3546.
PDB; 3TIU; X-ray; 2.08 A; A=3241-3546.
PDB; 3TNS; X-ray; 1.99 A; A=3241-3546.
PDB; 3TNT; X-ray; 1.59 A; A=3241-3546.
PDB; 3V3M; X-ray; 1.96 A; A=3241-3546.
PDB; 3VB3; X-ray; 2.20 A; A/B=3241-3546.
PDB; 3VB4; X-ray; 2.20 A; A/B=3241-3546.
PDB; 3VB5; X-ray; 1.95 A; A/B=3241-3546.
PDB; 3VB6; X-ray; 2.50 A; A/B=3241-3546.
PDB; 3VB7; X-ray; 1.95 A; A/B=3241-3546.
PDB; 4HI3; X-ray; 2.09 A; A/B=3241-3546.
PDB; 4M0W; X-ray; 1.40 A; A=1541-1858.
PDB; 4MDS; X-ray; 1.60 A; A=3241-3542.
PDB; 4MM3; X-ray; 2.75 A; B=1541-1855.
PDB; 4OVZ; X-ray; 2.50 A; A/B=1541-1855.
PDB; 4OW0; X-ray; 2.10 A; A/B=1541-1855.
PDB; 5F22; X-ray; 2.15 A; A=3837-3919.
PDBsum; 1P76; -.
PDBsum; 1P9T; -.
PDBsum; 1PA5; -.
PDBsum; 1PUK; -.
PDBsum; 1Q1X; -.
PDBsum; 1Q2W; -.
PDBsum; 1QZ8; -.
PDBsum; 1UJ1; -.
PDBsum; 1UK2; -.
PDBsum; 1UK3; -.
PDBsum; 1UK4; -.
PDBsum; 1UW7; -.
PDBsum; 1WOF; -.
PDBsum; 1YSY; -.
PDBsum; 1Z1I; -.
PDBsum; 1Z1J; -.
PDBsum; 2A5A; -.
PDBsum; 2A5I; -.
PDBsum; 2A5K; -.
PDBsum; 2ACF; -.
PDBsum; 2AHM; -.
PDBsum; 2AJ5; -.
PDBsum; 2ALV; -.
PDBsum; 2AMD; -.
PDBsum; 2AMQ; -.
PDBsum; 2BX3; -.
PDBsum; 2BX4; -.
PDBsum; 2C3S; -.
PDBsum; 2D2D; -.
PDBsum; 2DUC; -.
PDBsum; 2FAV; -.
PDBsum; 2FE8; -.
PDBsum; 2FYG; -.
PDBsum; 2G9T; -.
PDBsum; 2GA6; -.
PDBsum; 2GDT; -.
PDBsum; 2GRI; -.
PDBsum; 2GT7; -.
PDBsum; 2GT8; -.
PDBsum; 2GTB; -.
PDBsum; 2GX4; -.
PDBsum; 2GZ7; -.
PDBsum; 2GZ8; -.
PDBsum; 2GZ9; -.
PDBsum; 2H2Z; -.
PDBsum; 2HOB; -.
PDBsum; 2HSX; -.
PDBsum; 2IDY; -.
PDBsum; 2KAF; -.
PDBsum; 2KQV; -.
PDBsum; 2KQW; -.
PDBsum; 2KYS; -.
PDBsum; 2LIZ; -.
PDBsum; 2OP9; -.
PDBsum; 2PWX; -.
PDBsum; 2W2G; -.
PDBsum; 2WCT; -.
PDBsum; 2Z3C; -.
PDBsum; 2Z3D; -.
PDBsum; 2Z3E; -.
PDBsum; 2ZU4; -.
PDBsum; 2ZU5; -.
PDBsum; 3ATW; -.
PDBsum; 3AVZ; -.
PDBsum; 3AW0; -.
PDBsum; 3AW1; -.
PDBsum; 3E91; -.
PDBsum; 3EA7; -.
PDBsum; 3EA8; -.
PDBsum; 3EA9; -.
PDBsum; 3EAJ; -.
PDBsum; 3EE7; -.
PDBsum; 3F9E; -.
PDBsum; 3F9F; -.
PDBsum; 3F9G; -.
PDBsum; 3F9H; -.
PDBsum; 3FZD; -.
PDBsum; 3IWM; -.
PDBsum; 3M3S; -.
PDBsum; 3M3T; -.
PDBsum; 3M3V; -.
PDBsum; 3MJ5; -.
PDBsum; 3R24; -.
PDBsum; 3SN8; -.
PDBsum; 3SNA; -.
PDBsum; 3SNB; -.
PDBsum; 3SNC; -.
PDBsum; 3SND; -.
PDBsum; 3SNE; -.
PDBsum; 3SZN; -.
PDBsum; 3TIT; -.
PDBsum; 3TIU; -.
PDBsum; 3TNS; -.
PDBsum; 3TNT; -.
PDBsum; 3V3M; -.
PDBsum; 3VB3; -.
PDBsum; 3VB4; -.
PDBsum; 3VB5; -.
PDBsum; 3VB6; -.
PDBsum; 3VB7; -.
PDBsum; 4HI3; -.
PDBsum; 4M0W; -.
PDBsum; 4MDS; -.
PDBsum; 4MM3; -.
PDBsum; 4OVZ; -.
PDBsum; 4OW0; -.
PDBsum; 5F22; -.
ProteinModelPortal; P0C6U8; -.
SMR; P0C6U8; -.
DIP; DIP-48580N; -.
IntAct; P0C6U8; 1.
BindingDB; P0C6U8; -.
ChEMBL; CHEMBL3927; -.
DrugBank; DB08732; NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE.
MEROPS; C16.009; -.
PRIDE; P0C6U8; -.
GeneID; 1489680; -.
OrthoDB; VOG09000000; -.
BRENDA; 3.4.22.69; 7599.
EvolutionaryTrace; P0C6U8; -.
Proteomes; UP000000354; Genome.
Proteomes; UP000103670; Genome.
Proteomes; UP000109640; Genome.
Proteomes; UP000116947; Genome.
Proteomes; UP000121636; Genome.
Proteomes; UP000131569; Genome.
Proteomes; UP000131955; Genome.
Proteomes; UP000137377; Genome.
Proteomes; UP000138690; Genome.
Proteomes; UP000143093; Genome.
Proteomes; UP000145651; Genome.
Proteomes; UP000146108; Genome.
Proteomes; UP000146181; Genome.
Proteomes; UP000146296; Genome.
Proteomes; UP000148194; Genome.
Proteomes; UP000153467; Genome.
Proteomes; UP000160648; Genome.
Proteomes; UP000164441; Genome.
Proteomes; UP000172416; Genome.
GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
GO; GO:0033644; C:host cell membrane; 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase 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:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
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:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR021590; NSP1.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR024358; SARS-CoV_Nsp3_N.
InterPro; IPR022733; SARS_polyprot_cleavage.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF12379; DUF3655; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF11501; Nsp1; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF12124; Nsp3_PL2pro; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF11633; SUD-M; 1.
Pfam; PF08715; Viral_protease; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus;
Complete proteome; Decay of host mRNAs by virus; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Host cytoplasm;
Host gene expression shutoff by virus; Host membrane;
Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host IRF3 by virus; Inhibition of host ISG15 by virus;
Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Nuclease; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
Thiol protease; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 4382 Replicase polyprotein 1a.
/FTId=PRO_0000338254.
CHAIN 1 180 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338255.
CHAIN 181 818 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338256.
CHAIN 819 2740 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338257.
CHAIN 2741 3240 Non-structural protein 4. {ECO:0000255}.
/FTId=PRO_0000338258.
CHAIN 3241 3546 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338259.
CHAIN 3547 3836 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338260.
CHAIN 3837 3919 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338261.
CHAIN 3920 4117 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338262.
CHAIN 4118 4230 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338263.
CHAIN 4231 4369 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338264.
CHAIN 4370 4382 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338265.
TRANSMEM 2092 2112 Helical. {ECO:0000255}.
TRANSMEM 2203 2223 Helical. {ECO:0000255}.
TRANSMEM 2304 2324 Helical. {ECO:0000255}.
TRANSMEM 2326 2346 Helical. {ECO:0000255}.
TRANSMEM 2351 2371 Helical. {ECO:0000255}.
TRANSMEM 2755 2775 Helical. {ECO:0000255}.
TRANSMEM 2830 2850 Helical. {ECO:0000255}.
TRANSMEM 2879 2899 Helical. {ECO:0000255}.
TRANSMEM 2992 3012 Helical. {ECO:0000255}.
TRANSMEM 3022 3042 Helical. {ECO:0000255}.
TRANSMEM 3054 3074 Helical. {ECO:0000255}.
TRANSMEM 3077 3097 Helical. {ECO:0000255}.
TRANSMEM 3105 3125 Helical. {ECO:0000255}.
TRANSMEM 3142 3162 Helical. {ECO:0000255}.
TRANSMEM 3564 3584 Helical. {ECO:0000255}.
TRANSMEM 3586 3606 Helical. {ECO:0000255}.
TRANSMEM 3612 3632 Helical. {ECO:0000255}.
TRANSMEM 3658 3678 Helical. {ECO:0000255}.
TRANSMEM 3707 3727 Helical. {ECO:0000255}.
TRANSMEM 3728 3748 Helical. {ECO:0000255}.
TRANSMEM 3756 3776 Helical. {ECO:0000255}.
DOMAIN 1003 1169 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1611 1875 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3241 3546 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1729 1766 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4304 4320
ZN_FING 4347 4360
REGION 2092 2371 HD1.
REGION 2755 3162 HD2.
REGION 3564 3776 HD3.
COMPBIAS 930 1001 Glu-rich.
COMPBIAS 2210 2213 Poly-Leu.
COMPBIAS 3766 3769 Poly-Cys.
ACT_SITE 1651 1651 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1812 1812 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3281 3281 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3385 3385 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 4304 4304 Zinc.
METAL 4307 4307 Zinc.
METAL 4313 4313 Zinc.
METAL 4320 4320 Zinc.
METAL 4347 4347 Zinc.
METAL 4350 4350 Zinc.
METAL 4358 4358 Zinc.
SITE 180 181 Cleavage. {ECO:0000250}.
SITE 818 819 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 2740 2741 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3240 3241 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3546 3547 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3836 3837 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3919 3920 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4117 4118 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4230 4231 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4369 4370 Cleavage; by 3CL-PRO. {ECO:0000250}.
VARIANT 82 82 G -> C (in strain: Isolate GD01).
VARIANT 130 130 G -> R (in strain: Isolate GD01).
VARIANT 138 138 I -> T (in strain: Isolate SZ16).
VARIANT 181 181 A -> V (in strain: Isolate Shanghai LY).
VARIANT 225 225 K -> Q (in strain: Isolate GD01).
VARIANT 249 249 Y -> C (in strain: Isolate Shanghai LY).
VARIANT 306 306 V -> F (in strain: Isolate BJ04).
VARIANT 549 549 A -> S (in strain: Isolate SZ3).
VARIANT 765 765 A -> T (in strain: Isolate FRA and
Isolate Frankfurt-1).
VARIANT 852 852 K -> R (in strain: Isolate SZ16).
VARIANT 1004 1004 N -> H (in strain: Isolate BJ03).
VARIANT 1021 1021 V -> A (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 1023 1023 I -> T (in strain: Isolate Shanghai
QXC1).
VARIANT 1121 1121 I -> T (in strain: Isolate GD01, Isolate
SZ3 and Isolate SZ16).
VARIANT 1136 1136 P -> L (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 1257 1257 K -> E (in strain: Isolate Shanghai
QXC1).
VARIANT 1319 1319 K -> R (in strain: Isolate GD01).
VARIANT 1329 1329 F -> S (in strain: Isolate GD01).
VARIANT 1361 1361 T -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 1385 1385 I -> V (in strain: Isolate Shanghai
QXC1).
VARIANT 1538 1538 S -> T (in strain: Isolate GD01).
VARIANT 1563 1563 M -> K (in strain: Isolate BJ02).
VARIANT 1663 1663 L -> I (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 1762 1762 I -> L (in strain: Isolate BJ03).
VARIANT 1776 1777 QQ -> PP (in strain: Isolate BJ03).
VARIANT 1790 1790 E -> G (in strain: Isolate Shanghai
QXC1).
VARIANT 1806 1806 G -> V (in strain: Isolate BJ02).
VARIANT 1962 1962 L -> I (in strain: Isolate BJ04).
VARIANT 2116 2116 L -> F (in strain: Isolate GD01, Isolate
SZ3 and Isolate SZ16).
VARIANT 2222 2222 C -> Y (in strain: Isolate GD01, Isolate
SZ3 and Isolate SZ16).
VARIANT 2269 2269 L -> S (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 2326 2326 V -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 2392 2394 RNR -> CNH (in strain: Isolate Shanghai
QXC1).
VARIANT 2480 2480 L -> P (in strain: Isolate Shanghai
QXC1).
VARIANT 2552 2552 A -> V (in strain: Isolate Urbani and
Isolate Taiwan TC2).
VARIANT 2556 2556 D -> N (in strain: Isolate HKU-39849).
VARIANT 2564 2564 S -> P (in strain: Isolate GD01).
VARIANT 2648 2648 N -> Y (in strain: Isolate Shanghai
QXC1).
VARIANT 2708 2708 S -> T (in strain: Isolate HKU-39849).
VARIANT 2718 2718 R -> T (in strain: Isolate HKU-39849).
VARIANT 2746 2746 C -> W (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 2770 2770 V -> L (in strain: Isolate BJ01 and
Isolate BJ02).
VARIANT 2944 2944 T -> I (in strain: Isolate SIN2500,
Isolate GD01 and Isolate GZ50).
VARIANT 2971 2971 V -> A (in strain: Isolate GD01 and
Isolate SZ16).
VARIANT 3020 3020 V -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 3047 3047 V -> A (in strain: Isolate CUHK-W1,
Isolate GD01, Isolate SZ3, Isolate SZ16,
Isolate BJ01, Isolate BJ02, Isolate BJ03
and Isolate Shanghai QXC1).
VARIANT 3072 3072 V -> A (in strain: Isolate CUHK-W1,
Isolate SZ3, Isolate SZ16 and Isolate
GD01).
VARIANT 3197 3197 A -> V (in strain: Isolate BJ01, Isolate
BJ02, Isolate BJ03, Isolate BJ04 and
Isolate Shanghai QXC1).
VARIANT 3429 3429 Q -> P (in strain: Isolate BJ02).
VARIANT 3488 3488 D -> E (in strain: Isolate BJ04).
VARIANT 3717 3717 V -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 3818 3818 N -> T (in strain: Isolate BJ04).
VARIANT 3903 3903 D -> N (in strain: Isolate BJ03).
VARIANT 3904 3904 I -> F (in strain: Isolate BJ02).
VARIANT 3911 3911 M -> V (in strain: Isolate Shanghai
QXC1).
VARIANT 4001 4001 K -> Q (in strain: Isolate Shanghai LY).
VARIANT 4003 4003 T -> A (in strain: Isolate Shanghai LY).
VARIANT 4085 4085 I -> H (in strain: Isolate ZJ01).
VARIANT 4114 4114 V -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 4202 4202 V -> M (in strain: Isolate Shanghai
QXC1).
VARIANT 4240 4240 N -> H (in strain: Isolate ZJ01).
VARIANT 4296 4296 E -> G (in strain: Isolate Shanghai
QXC1).
VARIANT 4377 4378 LN -> FK (in strain: Isolate Shanghai
QXC1).
STRAND 1208 1211 {ECO:0000244|PDB:2W2G}.
STRAND 1214 1216 {ECO:0000244|PDB:2W2G}.
HELIX 1219 1222 {ECO:0000244|PDB:2W2G}.
TURN 1223 1225 {ECO:0000244|PDB:2W2G}.
STRAND 1229 1233 {ECO:0000244|PDB:2W2G}.
STRAND 1235 1237 {ECO:0000244|PDB:2WCT}.
HELIX 1241 1244 {ECO:0000244|PDB:2W2G}.
HELIX 1253 1255 {ECO:0000244|PDB:2W2G}.
TURN 1256 1258 {ECO:0000244|PDB:2W2G}.
STRAND 1266 1269 {ECO:0000244|PDB:2W2G}.
STRAND 1272 1276 {ECO:0000244|PDB:2W2G}.
HELIX 1280 1282 {ECO:0000244|PDB:2W2G}.
HELIX 1286 1293 {ECO:0000244|PDB:2W2G}.
STRAND 1298 1303 {ECO:0000244|PDB:2W2G}.
STRAND 1309 1312 {ECO:0000244|PDB:2WCT}.
HELIX 1315 1324 {ECO:0000244|PDB:2W2G}.
STRAND 1325 1331 {ECO:0000244|PDB:2W2G}.
HELIX 1343 1345 {ECO:0000244|PDB:2W2G}.
HELIX 1351 1361 {ECO:0000244|PDB:2W2G}.
STRAND 1364 1368 {ECO:0000244|PDB:2W2G}.
HELIX 1372 1381 {ECO:0000244|PDB:2W2G}.
TURN 1382 1384 {ECO:0000244|PDB:2W2G}.
STRAND 1389 1401 {ECO:0000244|PDB:2W2G}.
STRAND 1403 1405 {ECO:0000244|PDB:2W2G}.
HELIX 1407 1417 {ECO:0000244|PDB:2W2G}.
STRAND 1421 1423 {ECO:0000244|PDB:2W2G}.
TURN 1429 1431 {ECO:0000244|PDB:2W2G}.
HELIX 1435 1442 {ECO:0000244|PDB:2W2G}.
STRAND 1449 1452 {ECO:0000244|PDB:2W2G}.
HELIX 1456 1467 {ECO:0000244|PDB:2W2G}.
HELIX 1473 1484 {ECO:0000244|PDB:2KAF}.
STRAND 1485 1487 {ECO:0000244|PDB:2KQW}.
STRAND 1500 1506 {ECO:0000244|PDB:2KAF}.
STRAND 1509 1513 {ECO:0000244|PDB:2KAF}.
STRAND 1515 1518 {ECO:0000244|PDB:2KAF}.
STRAND 1521 1523 {ECO:0000244|PDB:2KAF}.
STRAND 1526 1528 {ECO:0000244|PDB:2KQW}.
HELIX 1530 1537 {ECO:0000244|PDB:2KAF}.
STRAND 1544 1555 {ECO:0000244|PDB:4M0W}.
STRAND 1557 1562 {ECO:0000244|PDB:4M0W}.
STRAND 1563 1565 {ECO:0000244|PDB:4OVZ}.
HELIX 1567 1570 {ECO:0000244|PDB:4M0W}.
STRAND 1571 1576 {ECO:0000244|PDB:4M0W}.
HELIX 1581 1583 {ECO:0000244|PDB:4OW0}.
HELIX 1588 1590 {ECO:0000244|PDB:4M0W}.
STRAND 1594 1597 {ECO:0000244|PDB:4M0W}.
HELIX 1602 1612 {ECO:0000244|PDB:4M0W}.
HELIX 1619 1630 {ECO:0000244|PDB:4M0W}.
TURN 1648 1650 {ECO:0000244|PDB:2FE8}.
HELIX 1651 1660 {ECO:0000244|PDB:4M0W}.
STRAND 1667 1669 {ECO:0000244|PDB:4M0W}.
HELIX 1670 1680 {ECO:0000244|PDB:4M0W}.
HELIX 1685 1695 {ECO:0000244|PDB:4M0W}.
HELIX 1705 1713 {ECO:0000244|PDB:4M0W}.
STRAND 1722 1729 {ECO:0000244|PDB:4M0W}.
TURN 1730 1732 {ECO:0000244|PDB:4M0W}.
STRAND 1733 1740 {ECO:0000244|PDB:4M0W}.
HELIX 1741 1744 {ECO:0000244|PDB:4M0W}.
STRAND 1746 1749 {ECO:0000244|PDB:4M0W}.
HELIX 1753 1758 {ECO:0000244|PDB:4M0W}.
STRAND 1760 1763 {ECO:0000244|PDB:4M0W}.
STRAND 1767 1794 {ECO:0000244|PDB:4M0W}.
STRAND 1799 1806 {ECO:0000244|PDB:4M0W}.
HELIX 1808 1810 {ECO:0000244|PDB:2FE8}.
STRAND 1811 1826 {ECO:0000244|PDB:4M0W}.
STRAND 1829 1846 {ECO:0000244|PDB:4M0W}.
STRAND 1848 1851 {ECO:0000244|PDB:4M0W}.
HELIX 3251 3254 {ECO:0000244|PDB:3TNT}.
STRAND 3257 3262 {ECO:0000244|PDB:3TNT}.
STRAND 3265 3272 {ECO:0000244|PDB:3TNT}.
STRAND 3275 3279 {ECO:0000244|PDB:3TNT}.
HELIX 3280 3283 {ECO:0000244|PDB:3TNT}.
HELIX 3286 3288 {ECO:0000244|PDB:2ZU5}.
STRAND 3289 3291 {ECO:0000244|PDB:3TNT}.
HELIX 3294 3299 {ECO:0000244|PDB:3TNT}.
HELIX 3303 3305 {ECO:0000244|PDB:3TNT}.
STRAND 3306 3310 {ECO:0000244|PDB:3TNT}.
STRAND 3313 3315 {ECO:0000244|PDB:3TNT}.
STRAND 3317 3323 {ECO:0000244|PDB:3TNT}.
STRAND 3326 3333 {ECO:0000244|PDB:3TNT}.
STRAND 3340 3343 {ECO:0000244|PDB:3TNT}.
STRAND 3351 3358 {ECO:0000244|PDB:3TNT}.
STRAND 3361 3369 {ECO:0000244|PDB:3TNT}.
TURN 3380 3383 {ECO:0000244|PDB:3F9F}.
STRAND 3388 3393 {ECO:0000244|PDB:3TNT}.
STRAND 3396 3406 {ECO:0000244|PDB:3TNT}.
TURN 3408 3410 {ECO:0000244|PDB:3F9E}.
STRAND 3412 3415 {ECO:0000244|PDB:3TNT}.
STRAND 3417 3419 {ECO:0000244|PDB:3F9G}.
STRAND 3421 3424 {ECO:0000244|PDB:3TNT}.
STRAND 3427 3430 {ECO:0000244|PDB:3TNT}.
HELIX 3441 3453 {ECO:0000244|PDB:3TNT}.
TURN 3458 3460 {ECO:0000244|PDB:3IWM}.
HELIX 3467 3476 {ECO:0000244|PDB:3TNT}.
HELIX 3484 3489 {ECO:0000244|PDB:3TNT}.
HELIX 3491 3497 {ECO:0000244|PDB:3TNT}.
HELIX 3501 3514 {ECO:0000244|PDB:3TNT}.
STRAND 3521 3523 {ECO:0000244|PDB:3F9E}.
STRAND 3524 3526 {ECO:0000244|PDB:3TNT}.
HELIX 3533 3539 {ECO:0000244|PDB:3TNT}.
STRAND 3541 3543 {ECO:0000244|PDB:2LIZ}.
HELIX 3838 3855 {ECO:0000244|PDB:5F22}.
HELIX 3858 3860 {ECO:0000244|PDB:5F22}.
HELIX 3862 3877 {ECO:0000244|PDB:5F22}.
HELIX 3881 3896 {ECO:0000244|PDB:5F22}.
HELIX 3904 3913 {ECO:0000244|PDB:5F22}.
HELIX 3997 4017 {ECO:0000244|PDB:5F22}.
HELIX 4020 4030 {ECO:0000244|PDB:5F22}.
STRAND 4035 4037 {ECO:0000244|PDB:5F22}.
STRAND 4046 4051 {ECO:0000244|PDB:5F22}.
HELIX 4054 4060 {ECO:0000244|PDB:5F22}.
STRAND 4065 4068 {ECO:0000244|PDB:5F22}.
STRAND 4071 4079 {ECO:0000244|PDB:5F22}.
HELIX 4088 4090 {ECO:0000244|PDB:5F22}.
TURN 4093 4095 {ECO:0000244|PDB:5F22}.
HELIX 4096 4098 {ECO:0000244|PDB:5F22}.
STRAND 4103 4109 {ECO:0000244|PDB:5F22}.
STRAND 4127 4136 {ECO:0000244|PDB:3EE7}.
TURN 4137 4139 {ECO:0000244|PDB:3EE7}.
STRAND 4142 4150 {ECO:0000244|PDB:3EE7}.
TURN 4152 4154 {ECO:0000244|PDB:1QZ8}.
STRAND 4157 4164 {ECO:0000244|PDB:3EE7}.
STRAND 4170 4173 {ECO:0000244|PDB:3EE7}.
STRAND 4176 4179 {ECO:0000244|PDB:1QZ8}.
STRAND 4180 4186 {ECO:0000244|PDB:3EE7}.
STRAND 4190 4194 {ECO:0000244|PDB:3EE7}.
STRAND 4201 4208 {ECO:0000244|PDB:3EE7}.
HELIX 4213 4224 {ECO:0000244|PDB:3EE7}.
HELIX 4240 4248 {ECO:0000244|PDB:2FYG}.
STRAND 4250 4252 {ECO:0000244|PDB:2FYG}.
HELIX 4253 4262 {ECO:0000244|PDB:2FYG}.
STRAND 4273 4275 {ECO:0000244|PDB:2G9T}.
STRAND 4284 4288 {ECO:0000244|PDB:2FYG}.
STRAND 4295 4299 {ECO:0000244|PDB:2FYG}.
HELIX 4301 4303 {ECO:0000244|PDB:2FYG}.
HELIX 4305 4309 {ECO:0000244|PDB:2FYG}.
STRAND 4316 4318 {ECO:0000244|PDB:2GA6}.
TURN 4321 4324 {ECO:0000244|PDB:2GA6}.
STRAND 4325 4330 {ECO:0000244|PDB:2FYG}.
HELIX 4331 4333 {ECO:0000244|PDB:2FYG}.
HELIX 4337 4343 {ECO:0000244|PDB:2FYG}.
TURN 4348 4350 {ECO:0000244|PDB:2FYG}.
TURN 4354 4356 {ECO:0000244|PDB:2FYG}.
SEQUENCE 4382 AA; 486373 MW; E1F65D5FD5DFF828 CRC64;
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT CGLVELEKGV
LPQLEQPYVF IKRSDALSTN HGHKVVELVA EMDGIQYGRS GITLGVLVPH VGETPIAYRN
VLLRKNGNKG AGGHSYGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGAL RELTRELNGG
AVTRYVDNNF CGPDGYPLDC IKDFLARAGK SMCTLSEQLD YIESKRGVYC CRDHEHEIAW
FTERSDKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVASPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEHCGTENLV IEGPTTCGYL
PTNAVVKMPC PACQDPEIGP EHSVADYHNH SNIETRLRKG GRTRCFGGCV FAYVGCYNKR
AYWVPRASAD IGSGHTGITG DNVETLNEDL LEILSRERVN INIVGDFHLN EEVAIILASF
SASTSAFIDT IKSLDYKSFK TIVESCGNYK VTKGKPVKGA WNIGQQRSVL TPLCGFPSQA
AGVIRSIFAR TLDAANHSIP DLQRAAVTIL DGISEQSLRL VDAMVYTSDL LTNSVIIMAY
VTGGLVQQTS QWLSNLLGTT VEKLRPIFEW IEAKLSAGVE FLKDAWEILK FLITGVFDIV
KGQIQVASDN IKDCVKCFID VVNKALEMCI DQVTIAGAKL RSLNLGEVFI AQSKGLYRQC
IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV LTSEEVVLKN GELEALETPV DSFTNGAIVG
TPVCVNGLML LEIKDKEQYC ALSPGLLATN NVFRLKGGAP IKGVTFGEDT VWEVQGYKNV
RITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
WSVATFYLFD DAGEENFSSR MYCSFYPPDE EEEDDAECEE EEIDETCEHE YGTEDDYQGL
PLEFGASAET VRVEEEEEED WLDDTTEQSE IEPEPEPTPE EPVNQFTGYL KLTDNVAIKC
VDIVKEAQSA NPMVIVNAAN IHLKHGGGVA GALNKATNGA MQKESDDYIK LNGPLTVGGS
CLLSGHNLAK KCLHVVGPNL NAGEDIQLLK AAYENFNSQD ILLAPLLSAG IFGAKPLQSL
QVCVQTVRTQ VYIAVNDKAL YEQVVMDYLD NLKPRVEAPK QEEPPNTEDS KTEEKSVVQK
PVDVKPKIKA CIDEVTTTLE ETKFLTNKLL LFADINGKLY HDSQNMLRGE DMSFLEKDAP
YMVGDVITSG DITCVVIPSK KAGGTTEMLS RALKKVPVDE YITTYPGQGC AGYTLEEAKT
ALKKCKSAFY VLPSEAPNAK EEILGTVSWN LREMLAHAEE TRKLMPICMD VRAIMATIQR
KYKGIKIQEG IVDYGVRFFF YTSKEPVASI ITKLNSLNEP LVTMPIGYVT HGFNLEEAAR
CMRSLKAPAV VSVSSPDAVT TYNGYLTSSS KTSEEHFVET VSLAGSYRDW SYSGQRTELG
VEFLKRGDKI VYHTLESPVE FHLDGEVLSL DKLKSLLSLR EVKTIKVFTT VDNTNLHTQL
VDMSMTYGQQ FGPTYLDGAD VTKIKPHVNH EGKTFFVLPS DDTLRSEAFE YYHTLDESFL
GRYMSALNHT KKWKFPQVGG LTSIKWADNN CYLSSVLLAL QQLEVKFNAP ALQEAYYRAR
AGDAANFCAL ILAYSNKTVG ELGDVRETMT HLLQHANLES AKRVLNVVCK HCGQKTTTLT
GVEAVMYMGT LSYDNLKTGV SIPCVCGRDA TQYLVQQESS FVMMSAPPAE YKLQQGTFLC
ANEYTGNYQC GHYTHITAKE TLYRIDGAHL TKMSEYKGPV TDVFYKETSY TTTIKPVSYK
LDGVTYTEIE PKLDGYYKKD NAYYTEQPID LVPTQPLPNA SFDNFKLTCS NTKFADDLNQ
MTGFTKPASR ELSVTFFPDL NGDVVAIDYR HYSASFKKGA KLLHKPIVWH INQATTKTTF
KPNTWCLRCL WSTKPVDTSN SFEVLAVEDT QGMDNLACES QQPTSEEVVE NPTIQKEVIE
CDVKTTEVVG NVILKPSDEG VKVTQELGHE DLMAAYVENT SITIKKPNEL SLALGLKTIA
THGIAAINSV PWSKILAYVK PFLGQAAITT SNCAKRLAQR VFNNYMPYVF TLLFQLCTFT
KSTNSRIRAS LPTTIAKNSV KSVAKLCLDA GINYVKSPKF SKLFTIAMWL LLLSICLGSL
ICVTAAFGVL LSNFGAPSYC NGVRELYLNS SNVTTMDFCE GSFPCSICLS GLDSLDSYPA
LETIQVTISS YKLDLTILGL AAEWVLAYML FTKFFYLLGL SAIMQVFFGY FASHFISNSW
LMWFIISIVQ MAPVSAMVRM YIFFASFYYI WKSYVHIMDG CTSSTCMMCY KRNRATRVEC
TTIVNGMKRS FYVYANGGRG FCKTHNWNCL NCDTFCTGST FISDEVARDL SLQFKRPINP
TDQSSYIVDS VAVKNGALHL YFDKAGQKTY ERHPLSHFVN LDNLRANNTK GSLPINVIVF
DGKSKCDESA SKSASVYYSQ LMCQPILLLD QALVSDVGDS TEVSVKMFDA YVDTFSATFS
VPMEKLKALV ATAHSELAKG VALDGVLSTF VSAARQGVVD TDVDTKDVIE CLKLSHHSDL
EVTGDSCNNF MLTYNKVENM TPRDLGACID CNARHINAQV AKSHNVSLIW NVKDYMSLSE
QLRKQIRSAA KKNNIPFRLT CATTRQVVNV ITTKISLKGG KIVSTCFKLM LKATLLCVLA
ALVCYIVMPV HTLSIHDGYT NEIIGYKAIQ DGVTRDIIST DDCFANKHAG FDAWFSQRGG
SYKNDKSCPV VAAIITREIG FIVPGLPGTV LRAINGDFLH FLPRVFSAVG NICYTPSKLI
EYSDFATSAC VLAAECTIFK DAMGKPVPYC YDTNLLEGSI SYSELRPDTR YVLMDGSIIQ
FPNTYLEGSV RVVTTFDAEY CRHGTCERSE VGICLSTSGR WVLNNEHYRA LSGVFCGVDA
MNLIANIFTP LVQPVGALDV SASVVAGGII AILVTCAAYY FMKFRRVFGE YNHVVAANAL
LFLMSFTILC LVPAYSFLPG VYSVFYLYLT FYFTNDVSFL AHLQWFAMFS PIVPFWITAI
YVFCISLKHC HWFFNNYLRK RVMFNGVTFS TFEEAALCTF LLNKEMYLKL RSETLLPLTQ
YNRYLALYNK YKYFSGALDT TSYREAACCH LAKALNDFSN SGADVLYQPP QTSITSAVLQ
SGFRKMAFPS GKVEGCMVQV TCGTTTLNGL WLDDTVYCPR HVICTAEDML NPNYEDLLIR
KSNHSFLVQA GNVQLRVIGH SMQNCLLRLK VDTSNPKTPK YKFVRIQPGQ TFSVLACYNG
SPSGVYQCAM RPNHTIKGSF LNGSCGSVGF NIDYDCVSFC YMHHMELPTG VHAGTDLEGK
FYGPFVDRQT AQAAGTDTTI TLNVLAWLYA AVINGDRWFL NRFTTTLNDF NLVAMKYNYE
PLTQDHVDIL GPLSAQTGIA VLDMCAALKE LLQNGMNGRT ILGSTILEDE FTPFDVVRQC
SGVTFQGKFK KIVKGTHHWM LLTFLTSLLI LVQSTQWSLF FFVYENAFLP FTLGIMAIAA
CAMLLVKHKH AFLCLFLLPS LATVAYFNMV YMPASWVMRI MTWLELADTS LSGYRLKDCV
MYASALVLLI LMTARTVYDD AARRVWTLMN VITLVYKVYY GNALDQAISM WALVISVTSN
YSGVVTTIMF LARAIVFVCV EYYPLLFITG NTLQCIMLVY CFLGYCCCCY FGLFCLLNRY
FRLTLGVYDY LVSTQEFRYM NSQGLLPPKS SIDAFKLNIK LLGIGGKPCI KVATVQSKMS
DVKCTSVVLL SVLQQLRVES SSKLWAQCVQ LHNDILLAKD TTEAFEKMVS LLSVLLSMQG
AVDINRLCEE MLDNRATLQA IASEFSSLPS YAAYATAQEA YEQAVANGDS EVVLKKLKKS
LNVAKSEFDR DAAMQRKLEK MADQAMTQMY KQARSEDKRA KVTSAMQTML FTMLRKLDND
ALNNIINNAR DGCVPLNIIP LTTAAKLMVV VPDYGTYKNT CDGNTFTYAS ALWEIQQVVD
ADSKIVQLSE INMDNSPNLA WPLIVTALRA NSAVKLQNNE LSPVALRQMS CAAGTTQTAC
TDDNALAYYN NSKGGRFVLA LLSDHQDLKW ARFPKSDGTG TIYTELEPPC RFVTDTPKGP
KVKYLYFIKG LNNLNRGMVL GSLAATVRLQ AGNATEVPAN STVLSFCAFA VDPAKAYKDY
LASGGQPITN CVKMLCTHTG TGQAITVTPE ANMDQESFGG ASCCLYCRCH IDHPNPKGFC
DLKGKYVQIP TTCANDPVGF TLRNTVCTVC GMWKGYGCSC DQLREPLMQS ADASTFLNGF
AV


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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