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Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]

 R1A_CVHSA               Reviewed;        4382 AA.
P0C6U8; P59641;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
22-APR-2020, entry version 99.
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.-;
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=3.4.22.69;
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; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae;
Orthocoronavirinae; Betacoronavirus; Sarbecovirus.
NCBI_TaxID=694009;
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 OF PUBMED:12781537.
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 (NON-STRUCTURAL PROTEIN 8).
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 (NON-STRUCTURAL PROTEIN 3).
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 (NON-STRUCTURAL PROTEIN 3).
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 (NON-STRUCTURAL PROTEIN 2), AND INTERACTION WITH HOST PHB AND
PHB2.
PubMed=19640993; DOI=10.1128/jvi.00842-09;
Cornillez-Ty C.T., Liao L., Yates J.R., Kuhn P., Buchmeier M.J.;
"Severe acute respiratory syndrome coronavirus nonstructural protein 2
interacts with a host protein complex involved in mitochondrial biogenesis
and intracellular signaling.";
J. Virol. 83:10314-10318(2009).
[28]
FUNCTION (NON-STRUCTURAL PROTEIN 9).
PubMed=19153232; DOI=10.1128/jvi.01505-08;
Miknis Z.J., Donaldson E.F., Umland T.C., Rimmer R.A., Baric R.S.,
Schultz L.W.;
"Severe acute respiratory syndrome coronavirus nsp9 dimerization is
essential for efficient viral growth.";
J. Virol. 83:3007-3018(2009).
[29]
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).
[30]
FUNCTION (PROTEINASE 3CL-PRO).
PubMed=16226257; DOI=10.1016/j.febslet.2005.09.075;
Lin C.W., Tsai F.J., Wan L., Lai C.C., Lin K.H., Hsieh T.H., Shiu S.Y.,
Li J.Y.;
"Binding interaction of SARS coronavirus 3CL(pro) protease with vacuolar-H+
ATPase G1 subunit.";
FEBS Lett. 579:6089-6094(2005).
[31]
HOMODIMERIZATION (3C-LIKE PROTEINASE).
PubMed=15507456; DOI=10.1074/jbc.m408211200;
Chen S., Chen L., Tan J., Chen J., Du L., Sun T., Shen J., Chen K.,
Jiang H., Shen X.;
"Severe acute respiratory syndrome coronavirus 3C-like proteinase N
terminus is indispensable for proteolytic activity but not for enzyme
dimerization. Biochemical and thermodynamic investigation in conjunction
with molecular dynamics simulations.";
J. Biol. Chem. 280:164-173(2005).
[32]
FUNCTION (NON-STRUCTURAL PROTEIN 1).
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).
[33]
FUNCTION (NON-STRUCTURAL PROTEIN 7), AND FUNCTION (NON-STRUCTURAL PROTEIN
8).
PubMed=22039154; DOI=10.1093/nar/gkr893;
te Velthuis A.J., van den Worm S.H., Snijder E.J.;
"The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA
polymerase capable of both de novo initiation and primer extension.";
Nucleic Acids Res. 40:1737-1747(2012).
[34]
FUNCTION (NON-STRUCTURAL PROTEIN 10), FUNCTION (GUANINE-N7
METHYLTRANSFERASE), AND INTERACTION OF NSP10 AND NSP14.
PubMed=22635272; DOI=10.1073/pnas.1201130109;
Bouvet M., Imbert I., Subissi L., Gluais L., Canard B., Decroly E.;
"RNA 3'-end mismatch excision by the severe acute respiratory syndrome
coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex.";
Proc. Natl. Acad. Sci. U.S.A. 109:9372-9377(2012).
[35]
FUNCTION (NON-STRUCTURAL PROTEIN 4), AND SUBCELLULAR LOCATION
(NON-STRUCTURAL PROTEIN 4).
PubMed=23943763; DOI=10.1128/mbio.00524-13;
Angelini M.M., Akhlaghpour M., Neuman B.W., Buchmeier M.J.;
"Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4,
and 6 induce double-membrane vesicles.";
MBio 4:0-0(2013).
[36]
FUNCTION (NON-STRUCTURAL PROTEIN 6).
PubMed=24991833; DOI=10.4161/auto.29309;
Cottam E.M., Whelband M.C., Wileman T.;
"Coronavirus NSP6 restricts autophagosome expansion.";
Autophagy 10:1426-1441(2014).
[37]
PROTEOLYTIC CLEAVAGE (REPLICASE POLYPROTEIN 1AB), MASS SPECTROMETRY
(NON-STRUCTURAL PROTEIN 8), MASS SPECTROMETRY (NON-STRUCTURAL PROTEIN 9),
AND MASS SPECTROMETRY (NON-STRUCTURAL PROTEIN 10).
PubMed=32083638; DOI=10.1042/bcj20200029;
Krichel B., Falke S., Hilgenfeld R., Redecke L., Uetrecht C.;
"Processing of the SARS-CoV pp1a/ab nsp7-10 region.";
Biochem. J. 477:1009-1019(2020).
[38]
REVIEW.
PubMed=24410069; DOI=10.1089/dna.2013.2304;
Angelini M.M., Neuman B.W., Buchmeier M.J.;
"Untangling membrane rearrangement in the nidovirales.";
DNA Cell Biol. 33:122-127(2014).
[39]
FUNCTION (NON-STRUCTURAL PROTEIN 3).
PubMed=24622840; DOI=10.1007/s13238-014-0026-3;
Chen X., Yang X., Zheng Y., Yang Y., Xing Y., Chen Z.;
"SARS coronavirus papain-like protease inhibits the type I interferon
signaling pathway through interaction with the STING-TRAF3-TBK1 complex.";
Protein Cell 5:369-381(2014).
[40]
INTERACTION WITH NUP93 (HOST TRANSLATION INHIBITOR NSP1), AND FUNCTION
(HOST TRANSLATION INHIBITOR NSP1).
PubMed=30943371; DOI=10.1139/bcb-2018-0394;
Gomez G.N., Abrar F., Dodhia M.P., Gonzalez F.G., Nag A.;
"SARS coronavirus protein nsp1 disrupts localization of Nup93 from the
nuclear pore complex.";
Biochem. Cell Biol. 97:758-766(2019).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
[48]
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).
[49]
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).
[50]
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).
[51]
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: [Replicase polyprotein 1a]: Multifunctional protein involved
in the transcription and replication of viral RNAs. Contains the
proteinases responsible for the cleavages of the polyprotein.
-!- FUNCTION: [Non-structural protein 1]: Inhibits host translation by
interacting with the 40S ribosomal subunit. 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 (PubMed:23035226). May disrupt nuclear pore function by
binding and displacing host NUP93 (PubMed:30943371).
{ECO:0000269|PubMed:23035226, ECO:0000269|PubMed:30943371}.
-!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
of host cell survival signaling pathway by interacting with host PHB
and PHB2. Indeed, these two proteins play a role in maintaining the
functional integrity of the mitochondria and protecting cells from
various stresses. {ECO:0000269|PubMed:19640993}.
-!- FUNCTION: [Non-structural protein 3]: Responsible for the cleavages
located at the N-terminus of the 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 (PubMed:17692280). Plays a role in host membrane
rearrangement that leads to creation of cytoplasmic double-membrane
vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6
together are sufficient to form DMV (PubMed:24410069). Antagonizes
innate immune induction of type I interferon by blocking the
phosphorylation, dimerization and subsequent nuclear translocation of
host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-
kappa-B signaling. {ECO:0000269|PubMed:17692280,
ECO:0000269|PubMed:19369340, ECO:0000269|PubMed:24622840,
ECO:0000303|PubMed:24410069}.
-!- FUNCTION: [Non-structural protein 4]: Plays a role in host membrane
rearrangement that leads to creation of cytoplasmic double-membrane
vesicles (DMV) necessary for viral replication. Alone appears incapable
to induce membrane curvature, but together with nsp3 is able to induce
paired membranes. Nsp3, nsp4 and nsp6 together are sufficient to form
DMV. {ECO:0000269|PubMed:23943763, ECO:0000303|PubMed:24410069}.
-!- FUNCTION: [3C-like proteinase]: Cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-
phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host
vacuoles intracellular pH. {ECO:0000255|PROSITE-ProRule:PRU00772,
ECO:0000269|PubMed:16226257, ECO:0000269|PubMed:16271890}.
-!- FUNCTION: [Non-structural protein 6]: Plays a role in host membrane
rearrangement that leads to creation of cytoplasmic double-membrane
vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6
together are sufficient to form DMV (PubMed:24410069). Plays a role in
the initial induction of autophagosomes from host reticulum
endoplasmic. Later, limits the expansion of these phagosomes that are
no longer able to deliver viral components to lysosomes
(PubMed:24991833). {ECO:0000269|PubMed:24991833,
ECO:0000303|PubMed:24410069}.
-!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
subunits of each) that may participate in viral replication by acting
as a primase. Alternatively, may synthesize substantially longer
products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}.
-!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
subunits of each) that may participate in viral replication by acting
as a primase. Alternatively, may synthesize substantially longer
products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}.
-!- FUNCTION: [Non-structural protein 9]: May participate in viral
replication by acting as a ssRNA-binding protein.
{ECO:0000269|PubMed:19153232}.
-!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
2'-O-methyltransferase activities. Therefore plays an essential role in
viral mRNAs cap methylation. {ECO:0000269|PubMed:22635272}.
-!- CATALYTIC ACTIVITY: [Non-structural protein 3]:
Reaction=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).; EC=3.4.19.12;
-!- CATALYTIC ACTIVITY: [3C-like proteinase]:
Reaction=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.; EC=3.4.22.69;
-!- SUBUNIT: Eight copies of nsp7 and eight copies of nsp8 assemble to form
a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer.
-!- INTERACTION:
PRO_0000338265; PRO_0000037310 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25492625, EBI-25474098;
-!- 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;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X7-1; Sequence=External;
-!- 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}.
-!- MASS SPECTROMETRY: [Non-structural protein 8]: Mass=21871;
Method=Electrospray; Evidence={ECO:0000269|PubMed:32083638};
-!- MASS SPECTROMETRY: [Non-structural protein 9]: Mass=12403;
Method=Electrospray; Evidence={ECO:0000269|PubMed:32083638};
-!- MASS SPECTROMETRY: [Non-structural protein 10]: Mass=14974;
Method=Electrospray; Evidence={ECO:0000269|PubMed:32083638};
-!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
conventional translation.
-!- 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.
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.
PDB; 5Y3E; X-ray; 1.65 A; A=1541-1854.
PDB; 5Y3Q; X-ray; 1.65 A; A=1541-1854.
PDB; 6NUR; EM; 3.10 A; B/D=3920-4117.
PDB; 6NUS; EM; 3.50 A; B=3920-4117.
PDB; 6Y7M; X-ray; 1.90 A; AAA=3241-3546.
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; -.
PDBsum; 5Y3E; -.
PDBsum; 5Y3Q; -.
PDBsum; 6NUR; -.
PDBsum; 6NUS; -.
PDBsum; 6Y7M; -.
SMR; P0C6U8; -.
DIP; DIP-48580N; -.
IntAct; P0C6U8; 3.
BindingDB; P0C6U8; -.
ChEMBL; CHEMBL3927; -.
DrugBank; DB07620; 2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE.
DrugBank; DB08732; NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE.
DrugBank; DB07743; S-[5-(TRIFLUOROMETHYL)-4H-1,2,4-TRIAZOL-3-YL] 5-(PHENYLETHYNYL)FURAN-2-CARBOTHIOATE.
MEROPS; C16.009; -.
PRIDE; P0C6U8; -.
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: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; 1.10.150.420; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.30.30.590; -; 1.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 2.40.10.290; -; 1.
Gene3D; 3.10.20.350; -; 1.
Gene3D; 3.40.220.20; -; 1.
Gene3D; 3.40.50.11020; -; 1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR042570; NAR_sf.
InterPro; IPR021590; NSP1.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR038030; NSP1_sf.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR038400; Nsp3_coronavir_sf.
InterPro; IPR022733; Nsp3_PL2pro.
InterPro; IPR038166; Nsp3_PL2pro_sf.
InterPro; IPR038123; NSP4_C_sf.
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; IPR038083; R1a/1ab.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR024358; SARS-CoV_Nsp3_N.
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; SSF159936; SSF159936; 1.
SUPFAM; SSF160099; SSF160099; 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;
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
/note="Replicase polyprotein 1a"
/id="PRO_0000338254"
CHAIN 1..180
/note="Non-structural protein 1"
/evidence="ECO:0000250"
/id="PRO_0000338255"
CHAIN 181..818
/note="Non-structural protein 2"
/evidence="ECO:0000250"
/id="PRO_0000338256"
CHAIN 819..2740
/note="Non-structural protein 3"
/evidence="ECO:0000250"
/id="PRO_0000338257"
CHAIN 2741..3240
/note="Non-structural protein 4"
/evidence="ECO:0000255"
/id="PRO_0000338258"
CHAIN 3241..3546
/note="3C-like proteinase"
/evidence="ECO:0000250"
/id="PRO_0000338259"
CHAIN 3547..3836
/note="Non-structural protein 6"
/evidence="ECO:0000250"
/id="PRO_0000338260"
CHAIN 3837..3919
/note="Non-structural protein 7"
/evidence="ECO:0000250"
/id="PRO_0000338261"
CHAIN 3920..4117
/note="Non-structural protein 8"
/evidence="ECO:0000250"
/id="PRO_0000338262"
CHAIN 4118..4230
/note="Non-structural protein 9"
/evidence="ECO:0000250"
/id="PRO_0000338263"
CHAIN 4231..4369
/note="Non-structural protein 10"
/evidence="ECO:0000250"
/id="PRO_0000338264"
CHAIN 4370..4382
/note="Non-structural protein 11"
/evidence="ECO:0000255"
/id="PRO_0000338265"
TOPO_DOM 1..2202
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 2203..2223
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2224..2303
/note="Lumenal"
/evidence="ECO:0000305"
TRANSMEM 2304..2324
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2325..2350
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 2351..2371
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2372..2754
/note="Lumenal"
/evidence="ECO:0000305"
TRANSMEM 2755..2775
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2776..2991
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 2992..3012
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3013..3021
/note="Lumenal"
/evidence="ECO:0000305"
TRANSMEM 3022..3042
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3043..3053
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 3054..3074
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3075..3076
/note="Lumenal"
/evidence="ECO:0000305"
TRANSMEM 3077..3097
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3098..3104
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 3105..3125
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3126..3141
/note="Lumenal"
/evidence="ECO:0000305"
TRANSMEM 3142..3162
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3163..3563
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 3564..3584
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3585
/note="Lumenal"
/evidence="ECO:0000305"
TRANSMEM 3586..3606
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3607..3611
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 3612..3632
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3633..3657
/note="Lumenal"
/evidence="ECO:0000305"
TRANSMEM 3658..3678
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3679..3684
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 3685..3704
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3705..3727
/note="Lumenal"
/evidence="ECO:0000305"
TRANSMEM 3728..3748
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3749..3755
/note="Cytoplasmic"
/evidence="ECO:0000305"
TRANSMEM 3756..3776
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 3777..4382
/note="Lumenal"
/evidence="ECO:0000305"
DOMAIN 1003..1169
/note="Macro"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
DOMAIN 1611..1875
/note="Peptidase C16"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
DOMAIN 3241..3546
/note="Peptidase C30"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
ZN_FING 1729..1766
/note="C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ZN_FING 4304..4320
ZN_FING 4347..4360
REGION 2092..2371
/note="HD1"
REGION 2755..3162
/note="HD2"
REGION 3564..3776
/note="HD3"
COMPBIAS 930..1001
/note="Glu-rich"
COMPBIAS 2210..2213
/note="Poly-Leu"
COMPBIAS 3766..3769
/note="Poly-Cys"
ACT_SITE 1651
/note="For PL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ACT_SITE 1812
/note="For PL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ACT_SITE 3281
/note="For 3CL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
ACT_SITE 3385
/note="For 3CL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
METAL 4304
/note="Zinc"
METAL 4307
/note="Zinc"
METAL 4313
/note="Zinc"
METAL 4320
/note="Zinc"
METAL 4347
/note="Zinc"
METAL 4350
/note="Zinc"
METAL 4358
/note="Zinc"
SITE 180..181
/note="Cleavage"
/evidence="ECO:0000250"
SITE 818..819
/note="Cleavage; by PL-PRO"
/evidence="ECO:0000250"
SITE 2740..2741
/note="Cleavage; by PL-PRO"
/evidence="ECO:0000250"
SITE 3240..3241
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3546..3547
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3836..3837
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3919..3920
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4117..4118
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4230..4231
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4369..4370
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
VARIANT 82
/note="G -> C (in strain: Isolate GD01)"
VARIANT 130
/note="G -> R (in strain: Isolate GD01)"
VARIANT 138
/note="I -> T (in strain: Isolate SZ16)"
VARIANT 181
/note="A -> V (in strain: Isolate Shanghai LY)"
VARIANT 225
/note="K -> Q (in strain: Isolate GD01)"
VARIANT 249
/note="Y -> C (in strain: Isolate Shanghai LY)"
VARIANT 306
/note="V -> F (in strain: Isolate BJ04)"
VARIANT 549
/note="A -> S (in strain: Isolate SZ3)"
VARIANT 765
/note="A -> T (in strain: Isolate FRA and Isolate
Frankfurt-1)"
VARIANT 852
/note="K -> R (in strain: Isolate SZ16)"
VARIANT 1004
/note="N -> H (in strain: Isolate BJ03)"
VARIANT 1021
/note="V -> A (in strain: Isolate SZ3 and Isolate SZ16)"
VARIANT 1023
/note="I -> T (in strain: Isolate Shanghai QXC1)"
VARIANT 1121
/note="I -> T (in strain: Isolate GD01, Isolate SZ3 and
Isolate SZ16)"
VARIANT 1136
/note="P -> L (in strain: Isolate SZ3 and Isolate SZ16)"
VARIANT 1257
/note="K -> E (in strain: Isolate Shanghai QXC1)"
VARIANT 1319
/note="K -> R (in strain: Isolate GD01)"
VARIANT 1329
/note="F -> S (in strain: Isolate GD01)"
VARIANT 1361
/note="T -> A (in strain: Isolate Shanghai QXC1)"
VARIANT 1385
/note="I -> V (in strain: Isolate Shanghai QXC1)"
VARIANT 1538
/note="S -> T (in strain: Isolate GD01)"
VARIANT 1563
/note="M -> K (in strain: Isolate BJ02)"
VARIANT 1663
/note="L -> I (in strain: Isolate SZ3 and Isolate SZ16)"
VARIANT 1762
/note="I -> L (in strain: Isolate BJ03)"
VARIANT 1776..1777
/note="QQ -> PP (in strain: Isolate BJ03)"
VARIANT 1790
/note="E -> G (in strain: Isolate Shanghai QXC1)"
VARIANT 1806
/note="G -> V (in strain: Isolate BJ02)"
VARIANT 1962
/note="L -> I (in strain: Isolate BJ04)"
VARIANT 2116
/note="L -> F (in strain: Isolate GD01, Isolate SZ3 and
Isolate SZ16)"
VARIANT 2222
/note="C -> Y (in strain: Isolate GD01, Isolate SZ3 and
Isolate SZ16)"
VARIANT 2269
/note="L -> S (in strain: Isolate SZ3 and Isolate SZ16)"
VARIANT 2326
/note="V -> A (in strain: Isolate Shanghai QXC1)"
VARIANT 2392..2394
/note="RNR -> CNH (in strain: Isolate Shanghai QXC1)"
VARIANT 2480
/note="L -> P (in strain: Isolate Shanghai QXC1)"
VARIANT 2552
/note="A -> V (in strain: Isolate Urbani and Isolate Taiwan
TC2)"
VARIANT 2556
/note="D -> N (in strain: Isolate HKU-39849)"
VARIANT 2564
/note="S -> P (in strain: Isolate GD01)"
VARIANT 2648
/note="N -> Y (in strain: Isolate Shanghai QXC1)"
VARIANT 2708
/note="S -> T (in strain: Isolate HKU-39849)"
VARIANT 2718
/note="R -> T (in strain: Isolate HKU-39849)"
VARIANT 2746
/note="C -> W (in strain: Isolate SZ3 and Isolate SZ16)"
VARIANT 2770
/note="V -> L (in strain: Isolate BJ01 and Isolate BJ02)"
VARIANT 2944
/note="T -> I (in strain: Isolate SIN2500, Isolate GD01 and
Isolate GZ50)"
VARIANT 2971
/note="V -> A (in strain: Isolate GD01 and Isolate SZ16)"
VARIANT 3020
/note="V -> A (in strain: Isolate Shanghai QXC1)"
VARIANT 3047
/note="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
/note="V -> A (in strain: Isolate CUHK-W1, Isolate SZ3,
Isolate SZ16 and Isolate GD01)"
VARIANT 3197
/note="A -> V (in strain: Isolate BJ01, Isolate BJ02,
Isolate BJ03, Isolate BJ04 and Isolate Shanghai QXC1)"
VARIANT 3429
/note="Q -> P (in strain: Isolate BJ02)"
VARIANT 3488
/note="D -> E (in strain: Isolate BJ04)"
VARIANT 3717
/note="V -> A (in strain: Isolate Shanghai QXC1)"
VARIANT 3818
/note="N -> T (in strain: Isolate BJ04)"
VARIANT 3903
/note="D -> N (in strain: Isolate BJ03)"
VARIANT 3904
/note="I -> F (in strain: Isolate BJ02)"
VARIANT 3911
/note="M -> V (in strain: Isolate Shanghai QXC1)"
VARIANT 4001
/note="K -> Q (in strain: Isolate Shanghai LY)"
VARIANT 4003
/note="T -> A (in strain: Isolate Shanghai LY)"
VARIANT 4085
/note="I -> H (in strain: Isolate ZJ01)"
VARIANT 4114
/note="V -> A (in strain: Isolate Shanghai QXC1)"
VARIANT 4202
/note="V -> M (in strain: Isolate Shanghai QXC1)"
VARIANT 4240
/note="N -> H (in strain: Isolate ZJ01)"
VARIANT 4296
/note="E -> G (in strain: Isolate Shanghai QXC1)"
VARIANT 4377..4378
/note="LN -> FK (in strain: Isolate Shanghai QXC1)"
STRAND 1208..1211
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1214..1216
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1219..1222
/evidence="ECO:0000244|PDB:2W2G"
TURN 1223..1225
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1229..1233
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1235..1237
/evidence="ECO:0000244|PDB:2WCT"
HELIX 1241..1244
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1253..1255
/evidence="ECO:0000244|PDB:2W2G"
TURN 1256..1258
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1266..1269
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1272..1276
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1280..1282
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1286..1293
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1298..1303
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1309..1312
/evidence="ECO:0000244|PDB:2WCT"
HELIX 1315..1324
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1325..1331
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1343..1345
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1351..1361
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1364..1368
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1372..1381
/evidence="ECO:0000244|PDB:2W2G"
TURN 1382..1384
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1389..1401
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1403..1405
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1407..1417
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1421..1423
/evidence="ECO:0000244|PDB:2W2G"
TURN 1429..1431
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1435..1442
/evidence="ECO:0000244|PDB:2W2G"
STRAND 1449..1452
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1456..1467
/evidence="ECO:0000244|PDB:2W2G"
HELIX 1473..1484
/evidence="ECO:0000244|PDB:2KAF"
STRAND 1485..1487
/evidence="ECO:0000244|PDB:2KQW"
STRAND 1500..1506
/evidence="ECO:0000244|PDB:2KAF"
STRAND 1509..1513
/evidence="ECO:0000244|PDB:2KAF"
STRAND 1515..1518
/evidence="ECO:0000244|PDB:2KAF"
STRAND 1521..1523
/evidence="ECO:0000244|PDB:2KAF"
STRAND 1526..1528
/evidence="ECO:0000244|PDB:2KQW"
HELIX 1530..1537
/evidence="ECO:0000244|PDB:2KAF"
STRAND 1544..1555
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1557..1562
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1563..1565
/evidence="ECO:0000244|PDB:4OVZ"
HELIX 1567..1570
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1571..1576
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1581..1583
/evidence="ECO:0000244|PDB:4OW0"
HELIX 1588..1590
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1594..1597
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1602..1612
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1619..1630
/evidence="ECO:0000244|PDB:4M0W"
TURN 1648..1650
/evidence="ECO:0000244|PDB:2FE8"
HELIX 1651..1660
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1667..1669
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1670..1680
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1685..1695
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1705..1713
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1722..1729
/evidence="ECO:0000244|PDB:4M0W"
TURN 1730..1732
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1733..1740
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1741..1744
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1746..1749
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1753..1758
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1760..1763
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1767..1794
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1799..1806
/evidence="ECO:0000244|PDB:4M0W"
HELIX 1808..1810
/evidence="ECO:0000244|PDB:2FE8"
STRAND 1811..1826
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1829..1846
/evidence="ECO:0000244|PDB:4M0W"
STRAND 1848..1851
/evidence="ECO:0000244|PDB:4M0W"
HELIX 3251..3254
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3257..3262
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3265..3272
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3275..3279
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3280..3283
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3286..3288
/evidence="ECO:0000244|PDB:2ZU5"
STRAND 3289..3291
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3294..3299
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3303..3305
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3306..3310
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3313..3315
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3317..3323
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3326..3333
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3340..3343
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3351..3358
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3361..3369
/evidence="ECO:0000244|PDB:3TNT"
TURN 3380..3383
/evidence="ECO:0000244|PDB:3F9F"
STRAND 3388..3393
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3396..3406
/evidence="ECO:0000244|PDB:3TNT"
TURN 3408..3410
/evidence="ECO:0000244|PDB:3F9E"
STRAND 3412..3415
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3417..3419
/evidence="ECO:0000244|PDB:3F9G"
STRAND 3421..3424
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3427..3430
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3441..3453
/evidence="ECO:0000244|PDB:3TNT"
TURN 3458..3460
/evidence="ECO:0000244|PDB:3IWM"
HELIX 3467..3476
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3484..3489
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3491..3497
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3501..3514
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3521..3523
/evidence="ECO:0000244|PDB:3F9E"
STRAND 3524..3526
/evidence="ECO:0000244|PDB:3TNT"
HELIX 3533..3539
/evidence="ECO:0000244|PDB:3TNT"
STRAND 3541..3543
/evidence="ECO:0000244|PDB:2LIZ"
HELIX 3838..3855
/evidence="ECO:0000244|PDB:5F22"
HELIX 3858..3860
/evidence="ECO:0000244|PDB:5F22"
HELIX 3862..3877
/evidence="ECO:0000244|PDB:5F22"
HELIX 3881..3896
/evidence="ECO:0000244|PDB:5F22"
HELIX 3904..3913
/evidence="ECO:0000244|PDB:5F22"
HELIX 3997..4017
/evidence="ECO:0000244|PDB:5F22"
HELIX 4020..4030
/evidence="ECO:0000244|PDB:5F22"
STRAND 4035..4037
/evidence="ECO:0000244|PDB:5F22"
HELIX 4040..4043
/evidence="ECO:0000244|PDB:6NUR"
STRAND 4046..4051
/evidence="ECO:0000244|PDB:5F22"
HELIX 4054..4060
/evidence="ECO:0000244|PDB:5F22"
STRAND 4065..4068
/evidence="ECO:0000244|PDB:5F22"
STRAND 4071..4079
/evidence="ECO:0000244|PDB:5F22"
HELIX 4088..4090
/evidence="ECO:0000244|PDB:5F22"
TURN 4093..4095
/evidence="ECO:0000244|PDB:5F22"
HELIX 4096..4098
/evidence="ECO:0000244|PDB:5F22"
STRAND 4103..4109
/evidence="ECO:0000244|PDB:5F22"
STRAND 4127..4136
/evidence="ECO:0000244|PDB:3EE7"
TURN 4137..4139
/evidence="ECO:0000244|PDB:3EE7"
STRAND 4142..4150
/evidence="ECO:0000244|PDB:3EE7"
TURN 4152..4154
/evidence="ECO:0000244|PDB:1QZ8"
STRAND 4157..4164
/evidence="ECO:0000244|PDB:3EE7"
STRAND 4170..4173
/evidence="ECO:0000244|PDB:3EE7"
STRAND 4176..4179
/evidence="ECO:0000244|PDB:1QZ8"
STRAND 4180..4186
/evidence="ECO:0000244|PDB:3EE7"
STRAND 4190..4194
/evidence="ECO:0000244|PDB:3EE7"
STRAND 4201..4208
/evidence="ECO:0000244|PDB:3EE7"
HELIX 4213..4224
/evidence="ECO:0000244|PDB:3EE7"
HELIX 4240..4248
/evidence="ECO:0000244|PDB:2FYG"
STRAND 4250..4252
/evidence="ECO:0000244|PDB:2FYG"
HELIX 4253..4262
/evidence="ECO:0000244|PDB:2FYG"
STRAND 4273..4275
/evidence="ECO:0000244|PDB:2G9T"
STRAND 4284..4288
/evidence="ECO:0000244|PDB:2FYG"
STRAND 4295..4299
/evidence="ECO:0000244|PDB:2FYG"
HELIX 4301..4303
/evidence="ECO:0000244|PDB:2FYG"
HELIX 4305..4309
/evidence="ECO:0000244|PDB:2FYG"
STRAND 4316..4318
/evidence="ECO:0000244|PDB:2GA6"
TURN 4321..4324
/evidence="ECO:0000244|PDB:2GA6"
STRAND 4325..4330
/evidence="ECO:0000244|PDB:2FYG"
HELIX 4331..4333
/evidence="ECO:0000244|PDB:2FYG"
HELIX 4337..4343
/evidence="ECO:0000244|PDB:2FYG"
TURN 4348..4350
/evidence="ECO:0000244|PDB:2FYG"
TURN 4354..4356
/evidence="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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