ID   R1A_CVHSA               Reviewed;        4382 AA.
AC   P0C6U8; P59641;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   17-JUN-2020, entry version 100.
DE   RecName: Full=Replicase polyprotein 1a;
DE            Short=pp1a;
DE   AltName: Full=ORF1a polyprotein;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=nsp1;
DE     AltName: Full=Leader protein;
DE   Contains:
DE     RecName: Full=Non-structural protein 2;
DE              Short=nsp2;
DE     AltName: Full=p65 homolog;
DE   Contains:
DE     RecName: Full=Non-structural protein 3;
DE              Short=nsp3;
DE              EC=3.4.19.12;
DE              EC=3.4.22.-;
DE     AltName: Full=PL2-PRO;
DE     AltName: Full=Papain-like proteinase;
DE              Short=PL-PRO;
DE   Contains:
DE     RecName: Full=Non-structural protein 4;
DE              Short=nsp4;
DE   Contains:
DE     RecName: Full=3C-like proteinase;
DE              Short=3CL-PRO;
DE              Short=3CLp;
DE              EC=3.4.22.69;
DE     AltName: Full=SARS coronavirus main proteinase;
DE     AltName: Full=nsp5;
DE   Contains:
DE     RecName: Full=Non-structural protein 6;
DE              Short=nsp6;
DE   Contains:
DE     RecName: Full=Non-structural protein 7;
DE              Short=nsp7;
DE   Contains:
DE     RecName: Full=Non-structural protein 8;
DE              Short=nsp8;
DE   Contains:
DE     RecName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE   Contains:
DE     RecName: Full=Non-structural protein 10;
DE              Short=nsp10;
DE     AltName: Full=Growth factor-like peptide;
DE              Short=GFL;
DE   Contains:
DE     RecName: Full=Non-structural protein 11;
DE              Short=nsp11;
GN   ORFNames=1a;
OS   Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome
OS   coronavirus).
OC   Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae;
OC   Orthocoronavirinae; Betacoronavirus; Sarbecovirus.
OX   NCBI_TaxID=694009;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9675; Paguma larvata (Masked palm civet).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Urbani;
RX   PubMed=12730500; DOI=10.1126/science.1085952;
RA   Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R.,
RA   Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H., Tong S.,
RA   Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D., Erdman D.D.,
RA   Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E., Sanchez A., Liffick S.,
RA   Holloway B., Limor J., McCaustland K., Olsen-Rasmussen M., Fouchier R.,
RA   Guenther S., Osterhaus A.D.M.E., Drosten C., Pallansch M.A., Anderson L.J.,
RA   Bellini W.J.;
RT   "Characterization of a novel coronavirus associated with severe acute
RT   respiratory syndrome.";
RL   Science 300:1394-1399(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Tor2;
RX   PubMed=12730501; DOI=10.1126/science.1085953;
RA   Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A.,
RA   Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y.,
RA   Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L., Leach S.R.,
RA   Mayo M., McDonald H., Montgomery S.B., Pandoh P.K., Petrescu A.S.,
RA   Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E., Stott J.M.,
RA   Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N., Bernard K.,
RA   Booth T.F., Bowness D., Czub M., Drebot M., Fernando L., Flick R.,
RA   Garbutt M., Gray M., Grolla A., Jones S., Feldmann H., Meyers A.,
RA   Kabani A., Li Y., Normand S., Stroher U., Tipples G.A., Tyler S.,
RA   Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M., Petric M.,
RA   Skowronski D.M., Upton C., Roper R.L.;
RT   "The genome sequence of the SARS-associated coronavirus.";
RL   Science 300:1399-1404(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1;
RX   PubMed=12853594; DOI=10.1056/nejm200307103490216;
RA   Tsui S.K.W., Chim S.S.C., Lo Y.M.D.;
RT   "Coronavirus genomic-sequence variations and the epidemiology of the severe
RT   acute respiratory syndrome.";
RL   N. Engl. J. Med. 349:187-188(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate GZ50, Isolate SZ16, and Isolate SZ3;
RX   PubMed=12958366; DOI=10.1126/science.1087139;
RA   Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L., Luo S.W.,
RA   Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L., Chan K.W., Lim W.,
RA   Shortridge K.F., Yuen K.Y., Peiris J.S.M., Poon L.L.M.;
RT   "Isolation and characterization of viruses related to the SARS coronavirus
RT   from animals in southern China.";
RL   Science 302:276-278(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate HKU-39849;
RX   PubMed=12876307; DOI=10.1177/15353702-0322807-13;
RA   Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C.,
RA   Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B.,
RA   Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.;
RT   "The complete genome sequence of severe acute respiratory syndrome
RT   coronavirus strain HKU-39849 (HK-39).";
RL   Exp. Biol. Med. 228:866-873(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Sin2500, Isolate Sin2677, Isolate Sin2679, Isolate Sin2748,
RC   and Isolate sin2774;
RX   PubMed=12781537; DOI=10.1016/s0140-6736(03)13414-9;
RA   Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
RA   Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
RA   Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.;
RT   "Comparative full-length genome sequence analysis of 14 SARS coronavirus
RT   isolates and common mutations associated with putative origins of
RT   infection.";
RL   Lancet 361:1779-1785(2003).
RN   [7]
RP   ERRATUM OF PUBMED:12781537.
RA   Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
RA   Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
RA   Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.;
RL   Lancet 361:1832-1832(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate ZJ01;
RX   PubMed=14527350;
RA   Li L., Wang Z., Lu Y., Bao Q., Chen S., Wu N., Cheng S., Weng J., Zhang Y.,
RA   Yan J., Mei L., Wang X., Zhu H., Yu Y., Zhang M., Li M., Yao J., Lu Q.,
RA   Yao P., Bo X., Wo J., Wang S., Hu S.;
RT   "Severe acute respiratory syndrome-associated coronavirus genotype and its
RT   characterization.";
RL   Chin. Med. J. 116:1288-1292(2003).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and
RC   Isolate GD01;
RA   Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W., Jiang T.,
RA   Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y., Li X., Lu F.,
RA   Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L., Deng Y., Dong W.,
RA   Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H., Li S., Li S., Li W.,
RA   Li W., Lin W., Liu J., Liu Z., Lu H., Ni P., Qi Q., Sun Y., Tang L.,
RA   Tong Z., Wang J., Wang X., Wu Q., Xi Y., Xu Z., Yang L., Ye C., Ye J.,
RA   Zhang B., Zhang F., Zhang J., Zhang X., Zhou J., Yang H.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate TW1;
RA   Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.;
RT   "The complete genome of SARS coronavirus clone TW1.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate FRA;
RX   PubMed=14645828; DOI=10.1126/science.302.5650.1504b;
RA   Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K., Censini S.,
RA   Guidotti S., Masignani V., Scarselli M., Mora M., Donati C., Han J.H.,
RA   Song H.C., Abrignani S., Covacci A., Rappuoli R.;
RT   "Phylogeny of the SARS coronavirus.";
RL   Science 302:1504-1505(2003).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Frankfurt-1;
RA   Thiel V., Hertzig T., Putics A., Ivanov K.A., Schelle B., Bayer S.,
RA   Scheiner B., Weinand H., Weissbrich B., Ziebuhr J.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate TWC;
RA   Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee S.C., Lin Y.-C.,
RA   Hsu C.-K., Chen H.-Y., Chang J.G., Chen P.-J., Su I.-J.;
RT   "Genomic sequence of SARS isolate from the first fatal case in Taiwan.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Shanghai QXC1;
RA   Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RT   "Analysis of SARS coronavirus genome in Shanghai isolates.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate HSR 1;
RA   Canducci F., Clementi M., Poli G., Vicenzi E.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [16]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3;
RA   Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L., Shih M.-C.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [17]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and Isolate TWY;
RA   Shu H.Y., Wu K.M., Tsai S.F.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [18]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate AS;
RA   Balotta C., Corvasce S., Violin M., Galli M., Moroni M., Vigevani G.M.,
RA   Ruan Y.J., Salemi M.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [19]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate ZJ01;
RA   Wang Z., Cheng S., Zhang Y.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [20]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-507 AND 1655-4382.
RC   STRAIN=Isolate Shanghai LY;
RA   Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [21]
RP   PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX   PubMed=12917450; DOI=10.1099/vir.0.19424-0;
RA   Thiel V., Ivanov K.A., Putics A., Hertzig T., Schelle B., Bayer S.,
RA   Weissbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E.,
RA   Ziebuhr J.;
RT   "Mechanisms and enzymes involved in SARS coronavirus genome expression.";
RL   J. Gen. Virol. 84:2305-2315(2003).
RN   [22]
RP   PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX   PubMed=15331731; DOI=10.1128/jvi.78.18.9977-9986.2004;
RA   Prentice E., McAuliffe J., Lu X., Subbarao K., Denison M.R.;
RT   "Identification and characterization of severe acute respiratory syndrome
RT   coronavirus replicase proteins.";
RL   J. Virol. 78:9977-9986(2004).
RN   [23]
RP   PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC   STRAIN=Isolate Urbani;
RX   PubMed=15564471; DOI=10.1128/jvi.78.24.13600-13612.2004;
RA   Harcourt B.H., Jukneliene D., Kanjanahaluethai A., Bechill J.,
RA   Severson K.M., Smith C.M., Rota P.A., Baker S.C.;
RT   "Identification of severe acute respiratory syndrome coronavirus replicase
RT   products and characterization of papain-like protease activity.";
RL   J. Virol. 78:13600-13612(2004).
RN   [24]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 8).
RX   PubMed=17024178; DOI=10.1038/sj.emboj.7601368;
RA   Imbert I., Guillemot J.-C., Bourhis J.-M., Bussetta C., Coutard B.,
RA   Egloff M.-P., Ferron F., Gorbalenya A.E., Canard B.;
RT   "A second, non-canonical RNA-dependent RNA polymerase in SARS
RT   coronavirus.";
RL   EMBO J. 25:4933-4942(2006).
RN   [25]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 3).
RX   PubMed=17692280; DOI=10.1016/j.abb.2007.07.006;
RA   Lindner H.A., Lytvyn V., Qi H., Lachance P., Ziomek E., Menard R.;
RT   "Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus
RT   papain-like protease.";
RL   Arch. Biochem. Biophys. 466:8-14(2007).
RN   [26]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 3).
RX   PubMed=19369340; DOI=10.1128/jvi.02220-08;
RA   Frieman M., Ratia K., Johnston R.E., Mesecar A.D., Baric R.S.;
RT   "Severe acute respiratory syndrome coronavirus papain-like protease
RT   ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and
RT   NF-kappaB signaling.";
RL   J. Virol. 83:6689-6705(2009).
RN   [27]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 2), AND INTERACTION WITH HOST PHB AND
RP   PHB2.
RX   PubMed=19640993; DOI=10.1128/jvi.00842-09;
RA   Cornillez-Ty C.T., Liao L., Yates J.R., Kuhn P., Buchmeier M.J.;
RT   "Severe acute respiratory syndrome coronavirus nonstructural protein 2
RT   interacts with a host protein complex involved in mitochondrial biogenesis
RT   and intracellular signaling.";
RL   J. Virol. 83:10314-10318(2009).
RN   [28]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 9).
RX   PubMed=19153232; DOI=10.1128/jvi.01505-08;
RA   Miknis Z.J., Donaldson E.F., Umland T.C., Rimmer R.A., Baric R.S.,
RA   Schultz L.W.;
RT   "Severe acute respiratory syndrome coronavirus nsp9 dimerization is
RT   essential for efficient viral growth.";
RL   J. Virol. 83:3007-3018(2009).
RN   [29]
RP   FUNCTION OF NSP1.
RX   PubMed=22174690; DOI=10.1371/journal.ppat.1002433;
RA   Huang C., Lokugamage K.G., Rozovics J.M., Narayanan K., Semler B.L.,
RA   Makino S.;
RT   "SARS coronavirus nsp1 protein induces template-dependent endonucleolytic
RT   cleavage of mRNAs: viral mRNAs are resistant to nsp1-induced RNA
RT   cleavage.";
RL   PLoS Pathog. 7:E1002433-E1002433(2011).
RN   [30]
RP   FUNCTION (PROTEINASE 3CL-PRO).
RX   PubMed=16226257; DOI=10.1016/j.febslet.2005.09.075;
RA   Lin C.W., Tsai F.J., Wan L., Lai C.C., Lin K.H., Hsieh T.H., Shiu S.Y.,
RA   Li J.Y.;
RT   "Binding interaction of SARS coronavirus 3CL(pro) protease with vacuolar-H+
RT   ATPase G1 subunit.";
RL   FEBS Lett. 579:6089-6094(2005).
RN   [31]
RP   HOMODIMERIZATION (3C-LIKE PROTEINASE).
RX   PubMed=15507456; DOI=10.1074/jbc.m408211200;
RA   Chen S., Chen L., Tan J., Chen J., Du L., Sun T., Shen J., Chen K.,
RA   Jiang H., Shen X.;
RT   "Severe acute respiratory syndrome coronavirus 3C-like proteinase N
RT   terminus is indispensable for proteolytic activity but not for enzyme
RT   dimerization. Biochemical and thermodynamic investigation in conjunction
RT   with molecular dynamics simulations.";
RL   J. Biol. Chem. 280:164-173(2005).
RN   [32]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=23035226; DOI=10.1128/jvi.01958-12;
RA   Lokugamage K.G., Narayanan K., Huang C., Makino S.;
RT   "Severe acute respiratory syndrome coronavirus protein nsp1 is a novel
RT   eukaryotic translation inhibitor that represses multiple steps of
RT   translation initiation.";
RL   J. Virol. 86:13598-13608(2012).
RN   [33]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 7), AND FUNCTION (NON-STRUCTURAL PROTEIN
RP   8).
RX   PubMed=22039154; DOI=10.1093/nar/gkr893;
RA   te Velthuis A.J., van den Worm S.H., Snijder E.J.;
RT   "The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA
RT   polymerase capable of both de novo initiation and primer extension.";
RL   Nucleic Acids Res. 40:1737-1747(2012).
RN   [34]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 10), FUNCTION (GUANINE-N7
RP   METHYLTRANSFERASE), AND INTERACTION OF NSP10 AND NSP14.
RX   PubMed=22635272; DOI=10.1073/pnas.1201130109;
RA   Bouvet M., Imbert I., Subissi L., Gluais L., Canard B., Decroly E.;
RT   "RNA 3'-end mismatch excision by the severe acute respiratory syndrome
RT   coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:9372-9377(2012).
RN   [35]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4), AND SUBCELLULAR LOCATION
RP   (NON-STRUCTURAL PROTEIN 4).
RX   PubMed=23943763; DOI=10.1128/mbio.00524-13;
RA   Angelini M.M., Akhlaghpour M., Neuman B.W., Buchmeier M.J.;
RT   "Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4,
RT   and 6 induce double-membrane vesicles.";
RL   MBio 4:0-0(2013).
RN   [36]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 6).
RX   PubMed=24991833; DOI=10.4161/auto.29309;
RA   Cottam E.M., Whelband M.C., Wileman T.;
RT   "Coronavirus NSP6 restricts autophagosome expansion.";
RL   Autophagy 10:1426-1441(2014).
RN   [37]
RP   PROTEOLYTIC CLEAVAGE (REPLICASE POLYPROTEIN 1AB), MASS SPECTROMETRY
RP   (NON-STRUCTURAL PROTEIN 8), MASS SPECTROMETRY (NON-STRUCTURAL PROTEIN 9),
RP   AND MASS SPECTROMETRY (NON-STRUCTURAL PROTEIN 10).
RX   PubMed=32083638; DOI=10.1042/bcj20200029;
RA   Krichel B., Falke S., Hilgenfeld R., Redecke L., Uetrecht C.;
RT   "Processing of the SARS-CoV pp1a/ab nsp7-10 region.";
RL   Biochem. J. 477:1009-1019(2020).
RN   [38]
RP   REVIEW.
RX   PubMed=24410069; DOI=10.1089/dna.2013.2304;
RA   Angelini M.M., Neuman B.W., Buchmeier M.J.;
RT   "Untangling membrane rearrangement in the nidovirales.";
RL   DNA Cell Biol. 33:122-127(2014).
RN   [39]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 3).
RX   PubMed=24622840; DOI=10.1007/s13238-014-0026-3;
RA   Chen X., Yang X., Zheng Y., Yang Y., Xing Y., Chen Z.;
RT   "SARS coronavirus papain-like protease inhibits the type I interferon
RT   signaling pathway through interaction with the STING-TRAF3-TBK1 complex.";
RL   Protein Cell 5:369-381(2014).
RN   [40]
RP   INTERACTION WITH NUP93 (HOST TRANSLATION INHIBITOR NSP1), AND FUNCTION
RP   (HOST TRANSLATION INHIBITOR NSP1).
RX   PubMed=30943371; DOI=10.1139/bcb-2018-0394;
RA   Gomez G.N., Abrar F., Dodhia M.P., Gonzalez F.G., Nag A.;
RT   "SARS coronavirus protein nsp1 disrupts localization of Nup93 from the
RT   nuclear pore complex.";
RL   Biochem. Cell Biol. 97:758-766(2019).
RN   [41]
RP   3D-STRUCTURE MODELING OF 3241-3540, AND CHARACTERIZATION.
RX   PubMed=12746549; DOI=10.1126/science.1085658;
RA   Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.;
RT   "Coronavirus main proteinase (3CLpro) structure: basis for design of anti-
RT   SARS drugs.";
RL   Science 300:1763-1767(2003).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4118-4230 (NSP9).
RC   STRAIN=Isolate Frankfurt-1;
RX   PubMed=12925794; DOI=10.1107/s0907444903016779;
RA   Campanacci V., Egloff M.-P., Longhi S., Ferron F., Rancurel C.,
RA   Salomoni A., Durousseau C., Tocque F., Bremond N., Dobbe J.C.,
RA   Snijder E.J., Canard B., Cambillau C.;
RT   "Structural genomics of the SARS coronavirus: cloning, expression,
RT   crystallization and preliminary crystallographic study of the Nsp9
RT   protein.";
RL   Acta Crystallogr. D 59:1628-1631(2003).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 4118-4230.
RX   PubMed=15007178; DOI=10.1073/pnas.0307877101;
RA   Egloff M.-P., Ferron F., Campanacci V., Longhi S., Rancurel C.,
RA   Dutartre H., Snijder E.J., Gorbalenya A.E., Cambillau C., Canard B.;
RT   "The severe acute respiratory syndrome-coronavirus replicative protein nsp9
RT   is a single-stranded RNA-binding subunit unique in the RNA virus world.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:3792-3796(2004).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230.
RX   PubMed=14962394; DOI=10.1016/j.str.2004.01.016;
RA   Sutton G., Fry E., Carter L., Sainsbury S., Walter T., Nettleship J.,
RA   Berrow N., Owens R., Gilbert R., Davidson A., Siddell S., Poon L.L.M.,
RA   Diprose J., Alderton D., Walsh M., Grimes J.M., Stuart D.I.;
RT   "The nsp9 replicase protein of SARS-coronavirus, structure and functional
RT   insights.";
RL   Structure 12:341-353(2004).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 3837-4117 AND 3920-4117, AND
RP   INTERACTION OF NSP7 WITH NSP8.
RX   PubMed=16228002; DOI=10.1038/nsmb999;
RA   Zhai Y., Sun F., Li X., Pang H., Xu X., Bartlam M., Rao Z.;
RT   "Insights into SARS-CoV transcription and replication from the structure of
RT   the nsp7-nsp8 hexadecamer.";
RL   Nat. Struct. Mol. Biol. 12:980-986(2005).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1002-1176.
RX   PubMed=16271890; DOI=10.1016/j.str.2005.07.022;
RA   Saikatendu K.S., Joseph J.S., Subramanian V., Clayton T., Griffith M.,
RA   Moy K., Velasquez J., Neuman B.W., Buchmeier M.J., Stevens R.C., Kuhn P.;
RT   "Structural basis of severe acute respiratory syndrome coronavirus ADP-
RT   ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.";
RL   Structure 13:1665-1675(2005).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1541-1854.
RX   PubMed=16581910; DOI=10.1073/pnas.0510851103;
RA   Ratia K., Saikatendu K.S., Santarsiero B.D., Barretto N., Baker S.C.,
RA   Stevens R.C., Mesecar A.D.;
RT   "Severe acute respiratory syndrome coronavirus papain-like protease:
RT   structure of a viral deubiquitinating enzyme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5717-5722(2006).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4240-4362.
RC   STRAIN=Isolate Tor2;
RX   PubMed=16873246; DOI=10.1128/jvi.00467-06;
RA   Joseph J.S., Saikatendu K.S., Subramanian V., Neuman B.W., Brooun A.,
RA   Griffith M., Moy K., Yadav M.K., Velasquez J., Buchmeier M.J.,
RA   Stevens R.C., Kuhn P.;
RT   "Crystal structure of nonstructural protein 10 from the severe acute
RT   respiratory syndrome coronavirus reveals a novel fold with two zinc-binding
RT   motifs.";
RL   J. Virol. 80:7894-7901(2006).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4231-4378.
RX   PubMed=16873247; DOI=10.1128/jvi.00483-06;
RA   Su D., Lou Z., Sun F., Zhai Y., Yang H., Zhang R., Joachimiak A.,
RA   Zhang X.C., Bartlam M., Rao Z.;
RT   "Dodecamer structure of severe acute respiratory syndrome coronavirus
RT   nonstructural protein nsp10.";
RL   J. Virol. 80:7902-7908(2006).
RN   [50]
RP   STRUCTURE BY NMR OF 13-127.
RX   PubMed=17202208; DOI=10.1128/jvi.01939-06;
RA   Almeida M.S., Johnson M.A., Herrmann T., Geralt M., Wuthrich K.;
RT   "Novel beta-barrel fold in the nuclear magnetic resonance structure of the
RT   replicase nonstructural protein 1 from the severe acute respiratory
RT   syndrome coronavirus.";
RL   J. Virol. 81:3151-3161(2007).
RN   [51]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3241-3546.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of Sars coronavirus main proteinase(3CLPRO).";
RL   Submitted (JUL-2007) to the PDB data bank.
CC   -!- FUNCTION: [Replicase polyprotein 1a]: Multifunctional protein involved
CC       in the transcription and replication of viral RNAs. Contains the
CC       proteinases responsible for the cleavages of the polyprotein.
CC   -!- FUNCTION: [Non-structural protein 1]: Inhibits host translation by
CC       interacting with the 40S ribosomal subunit. The nsp1-40S ribosome
CC       complex further induces an endonucleolytic cleavage near the 5'UTR of
CC       host mRNAs, targeting them for degradation. Viral mRNAs are not
CC       susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the
CC       presence of a 5'-end leader sequence and are therefore protected from
CC       degradation. By suppressing host gene expression, nsp1 facilitates
CC       efficient viral gene expression in infected cells and evasion from host
CC       immune response (PubMed:23035226). May disrupt nuclear pore function by
CC       binding and displacing host NUP93 (PubMed:30943371).
CC       {ECO:0000269|PubMed:23035226, ECO:0000269|PubMed:30943371}.
CC   -!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
CC       of host cell survival signaling pathway by interacting with host PHB
CC       and PHB2. Indeed, these two proteins play a role in maintaining the
CC       functional integrity of the mitochondria and protecting cells from
CC       various stresses. {ECO:0000269|PubMed:19640993}.
CC   -!- FUNCTION: [Non-structural protein 3]: Responsible for the cleavages
CC       located at the N-terminus of the replicase polyprotein. In addition,
CC       PL-PRO possesses a deubiquitinating/deISGylating activity and processes
CC       both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular
CC       substrates (PubMed:17692280). Plays a role in host membrane
CC       rearrangement that leads to creation of cytoplasmic double-membrane
CC       vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6
CC       together are sufficient to form DMV (PubMed:24410069). Antagonizes
CC       innate immune induction of type I interferon by blocking the
CC       phosphorylation, dimerization and subsequent nuclear translocation of
CC       host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-
CC       kappa-B signaling. {ECO:0000269|PubMed:17692280,
CC       ECO:0000269|PubMed:19369340, ECO:0000269|PubMed:24622840,
CC       ECO:0000303|PubMed:24410069}.
CC   -!- FUNCTION: [Non-structural protein 4]: Plays a role in host membrane
CC       rearrangement that leads to creation of cytoplasmic double-membrane
CC       vesicles (DMV) necessary for viral replication. Alone appears incapable
CC       to induce membrane curvature, but together with nsp3 is able to induce
CC       paired membranes. Nsp3, nsp4 and nsp6 together are sufficient to form
CC       DMV. {ECO:0000269|PubMed:23943763, ECO:0000303|PubMed:24410069}.
CC   -!- FUNCTION: [3C-like proteinase]: Cleaves the C-terminus of replicase
CC       polyprotein at 11 sites. Recognizes substrates containing the core
CC       sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-
CC       phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host
CC       vacuoles intracellular pH. {ECO:0000255|PROSITE-ProRule:PRU00772,
CC       ECO:0000269|PubMed:16226257, ECO:0000269|PubMed:16271890}.
CC   -!- FUNCTION: [Non-structural protein 6]: Plays a role in host membrane
CC       rearrangement that leads to creation of cytoplasmic double-membrane
CC       vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6
CC       together are sufficient to form DMV (PubMed:24410069). Plays a role in
CC       the initial induction of autophagosomes from host reticulum
CC       endoplasmic. Later, limits the expansion of these phagosomes that are
CC       no longer able to deliver viral components to lysosomes
CC       (PubMed:24991833). {ECO:0000269|PubMed:24991833,
CC       ECO:0000303|PubMed:24410069}.
CC   -!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
CC       subunits of each) that may participate in viral replication by acting
CC       as a primase. Alternatively, may synthesize substantially longer
CC       products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}.
CC   -!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
CC       subunits of each) that may participate in viral replication by acting
CC       as a primase. Alternatively, may synthesize substantially longer
CC       products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}.
CC   -!- FUNCTION: [Non-structural protein 9]: May participate in viral
CC       replication by acting as a ssRNA-binding protein.
CC       {ECO:0000269|PubMed:19153232}.
CC   -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC       transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
CC       2'-O-methyltransferase activities. Therefore plays an essential role in
CC       viral mRNAs cap methylation. {ECO:0000269|PubMed:22635272}.
CC   -!- CATALYTIC ACTIVITY: [Non-structural protein 3]:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
CC   -!- CATALYTIC ACTIVITY: [3C-like proteinase]:
CC       Reaction=TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides
CC         corresponding to the two self-cleavage sites of the SARS 3C-like
CC         proteinase are the two most reactive peptide substrates. The enzyme
CC         exhibits a strong preference for substrates containing Gln at P1
CC         position and Leu at P2 position.; EC=3.4.22.69;
CC   -!- SUBUNIT: Eight copies of nsp7 and eight copies of nsp8 assemble to form
CC       a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer.
CC   -!- INTERACTION:
CC       PRO_0000338265; PRO_0000037310 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25492625, EBI-25474098;
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6U8-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6X7-1; Sequence=External;
CC   -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC       association of the replication complex and thereby alter the
CC       architecture of the host cell membrane.
CC   -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC       mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC       processed (By similarity). {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: [Non-structural protein 8]: Mass=21871;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:32083638};
CC   -!- MASS SPECTROMETRY: [Non-structural protein 9]: Mass=12403;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:32083638};
CC   -!- MASS SPECTROMETRY: [Non-structural protein 10]: Mass=14974;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:32083638};
CC   -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
CC       conventional translation.
CC   -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Isolates SZ3 and SZ16 have been isolated from Paguma larvata
CC       and are described as SARS-like in literature. {ECO:0000305}.
DR   EMBL; AY278741; AAP13439.1; -; Genomic_RNA.
DR   EMBL; AY274119; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY278554; AAP13575.1; -; Genomic_RNA.
DR   EMBL; AY282752; AAP30712.1; -; Genomic_RNA.
DR   EMBL; AY304495; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY304486; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY304488; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283795; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283796; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283797; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283798; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY286320; AAR16181.1; -; Genomic_RNA.
DR   EMBL; AY278488; AAP30029.1; -; Genomic_RNA.
DR   EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY278489; AAP51226.1; -; Genomic_RNA.
DR   EMBL; AY291451; AAP37016.1; -; Genomic_RNA.
DR   EMBL; AY310120; AAP50484.1; -; Genomic_RNA.
DR   EMBL; AY291315; AAP33695.1; -; Genomic_RNA.
DR   EMBL; AY323977; AAP72974.2; -; Genomic_RNA.
DR   EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY338174; AAQ01595.1; -; Genomic_RNA.
DR   EMBL; AY338175; AAQ01607.1; -; Genomic_RNA.
DR   EMBL; AY348314; AAP97880.1; -; Genomic_RNA.
DR   EMBL; AP006557; BAC81347.1; -; Genomic_RNA.
DR   EMBL; AP006558; BAC81361.1; -; Genomic_RNA.
DR   EMBL; AP006559; BAC81375.1; -; Genomic_RNA.
DR   EMBL; AP006560; BAC81389.1; -; Genomic_RNA.
DR   EMBL; AP006561; BAC81403.1; -; Genomic_RNA.
DR   EMBL; AY427439; AAQ94059.1; -; Genomic_RNA.
DR   EMBL; AY322205; AAP82966.1; -; Genomic_RNA.
DR   EMBL; AY322206; AAP82976.1; -; Genomic_RNA.
DR   EMBL; AY463059; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   PDB; 1P76; Model; -; A=3241-3541, B=4225-4231.
DR   PDB; 1P9T; Model; -; A=3241-3544.
DR   PDB; 1PA5; Model; -; A=3241-3546.
DR   PDB; 1PUK; Model; -; A=3241-3550.
DR   PDB; 1Q1X; Model; -; A=3241-3542.
DR   PDB; 1Q2W; X-ray; 1.86 A; A/B=3241-3544.
DR   PDB; 1QZ8; X-ray; 2.70 A; A/B=4118-4230.
DR   PDB; 1UJ1; X-ray; 1.90 A; A/B=3241-3546.
DR   PDB; 1UK2; X-ray; 2.20 A; A/B=3241-3546.
DR   PDB; 1UK3; X-ray; 2.40 A; A/B=3241-3546.
DR   PDB; 1UK4; X-ray; 2.50 A; A/B=3241-3546.
DR   PDB; 1UW7; X-ray; 2.80 A; A=4118-4230.
DR   PDB; 1WOF; X-ray; 2.00 A; A/B=3241-3546.
DR   PDB; 1YSY; NMR; -; A=3837-3919.
DR   PDB; 1Z1I; X-ray; 2.80 A; A=3241-3546.
DR   PDB; 1Z1J; X-ray; 2.80 A; A/B=3241-3546.
DR   PDB; 2A5A; X-ray; 2.08 A; A=3241-3546.
DR   PDB; 2A5I; X-ray; 1.88 A; A=3241-3546.
DR   PDB; 2A5K; X-ray; 2.30 A; A/B=3241-3546.
DR   PDB; 2ACF; X-ray; 1.40 A; A/B/C/D=1002-1176.
DR   PDB; 2AHM; X-ray; 2.40 A; A/B/C/D=3837-3919, E/F/G/H=3920-4117.
DR   PDB; 2AJ5; Model; -; A=3241-3546.
DR   PDB; 2ALV; X-ray; 1.90 A; A=3241-3543.
DR   PDB; 2AMD; X-ray; 1.85 A; A/B=3241-3546.
DR   PDB; 2AMQ; X-ray; 2.30 A; A/B=3241-3546.
DR   PDB; 2BX3; X-ray; 2.00 A; A=3241-3546.
DR   PDB; 2BX4; X-ray; 2.79 A; A=3241-3546.
DR   PDB; 2C3S; X-ray; 1.90 A; A=3241-3546.
DR   PDB; 2D2D; X-ray; 2.70 A; A/B=3241-3546.
DR   PDB; 2DUC; X-ray; 1.70 A; A/B=3241-3546.
DR   PDB; 2FAV; X-ray; 1.80 A; A/B/C=1000-1173.
DR   PDB; 2FE8; X-ray; 1.85 A; A/B/C=1541-1854.
DR   PDB; 2FYG; X-ray; 1.80 A; A=4240-4362.
DR   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.
DR   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.
DR   PDB; 2GDT; NMR; -; A=13-127.
DR   PDB; 2GRI; NMR; -; A=819-930.
DR   PDB; 2GT7; X-ray; 1.82 A; A/B=3241-3546.
DR   PDB; 2GT8; X-ray; 2.00 A; A=3241-3546.
DR   PDB; 2GTB; X-ray; 2.00 A; A=3241-3546.
DR   PDB; 2GX4; X-ray; 1.93 A; A=3241-3546.
DR   PDB; 2GZ7; X-ray; 1.86 A; A=3241-3546.
DR   PDB; 2GZ8; X-ray; 1.97 A; A=3241-3546.
DR   PDB; 2GZ9; X-ray; 2.17 A; A=3241-3546.
DR   PDB; 2H2Z; X-ray; 1.60 A; A=3241-3546.
DR   PDB; 2HOB; X-ray; 1.95 A; A=3241-3546.
DR   PDB; 2HSX; NMR; -; A=13-127.
DR   PDB; 2IDY; NMR; -; A=819-930.
DR   PDB; 2KAF; NMR; -; A=1473-1538.
DR   PDB; 2KQV; NMR; -; A=1345-1538.
DR   PDB; 2KQW; NMR; -; A=1345-1538.
DR   PDB; 2KYS; NMR; -; A=3837-3919.
DR   PDB; 2LIZ; NMR; -; A=3427-3546.
DR   PDB; 2OP9; X-ray; 1.80 A; A/B=3241-3541.
DR   PDB; 2PWX; X-ray; 2.50 A; A=3241-3546.
DR   PDB; 2W2G; X-ray; 2.22 A; A/B=1207-1470.
DR   PDB; 2WCT; X-ray; 2.79 A; A/B/C/D=1207-1470.
DR   PDB; 2Z3C; X-ray; 1.79 A; A=3241-3546.
DR   PDB; 2Z3D; X-ray; 2.10 A; A=3241-3546.
DR   PDB; 2Z3E; X-ray; 2.32 A; A=3241-3546.
DR   PDB; 2ZU4; X-ray; 1.93 A; A=3241-3546.
DR   PDB; 2ZU5; X-ray; 1.65 A; A=3241-3546.
DR   PDB; 3ATW; X-ray; 2.36 A; A/B=3241-3546.
DR   PDB; 3AVZ; X-ray; 2.46 A; A=3241-3546.
DR   PDB; 3AW0; X-ray; 2.30 A; A=3241-3546.
DR   PDB; 3AW1; X-ray; 2.00 A; A/B=3241-3546.
DR   PDB; 3E91; X-ray; 2.55 A; A/B=3241-3546.
DR   PDB; 3EA7; X-ray; 2.65 A; A/B=3241-3546.
DR   PDB; 3EA8; X-ray; 2.25 A; A=3241-3546.
DR   PDB; 3EA9; X-ray; 2.40 A; A=3241-3546.
DR   PDB; 3EAJ; X-ray; 2.70 A; A/B=3241-3546.
DR   PDB; 3EE7; X-ray; 2.60 A; A/B/C/D=4118-4230.
DR   PDB; 3F9E; X-ray; 2.50 A; A=3241-3546.
DR   PDB; 3F9F; X-ray; 2.30 A; A/B=3241-3546.
DR   PDB; 3F9G; X-ray; 2.60 A; A/B=3241-3541.
DR   PDB; 3F9H; X-ray; 2.90 A; A/B=3241-3546.
DR   PDB; 3FZD; X-ray; 2.35 A; A=3241-3541.
DR   PDB; 3IWM; X-ray; 3.20 A; A/B/C/D=3241-3546.
DR   PDB; 3M3S; X-ray; 2.30 A; A/B=3241-3546.
DR   PDB; 3M3T; X-ray; 2.90 A; A=3241-3546.
DR   PDB; 3M3V; X-ray; 2.70 A; A/B=3241-3546.
DR   PDB; 3MJ5; X-ray; 2.63 A; A/B=1541-1855.
DR   PDB; 3R24; X-ray; 2.00 A; B=4240-4382.
DR   PDB; 3SN8; X-ray; 1.99 A; A=3241-3546.
DR   PDB; 3SNA; X-ray; 3.05 A; A=3241-3541.
DR   PDB; 3SNB; X-ray; 2.40 A; A=3241-3546.
DR   PDB; 3SNC; X-ray; 2.58 A; A=3241-3546.
DR   PDB; 3SND; X-ray; 1.89 A; A/B=3241-3546.
DR   PDB; 3SNE; X-ray; 2.60 A; A=3241-3546.
DR   PDB; 3SZN; X-ray; 1.69 A; A=3241-3546.
DR   PDB; 3TIT; X-ray; 1.99 A; A=3241-3546.
DR   PDB; 3TIU; X-ray; 2.08 A; A=3241-3546.
DR   PDB; 3TNS; X-ray; 1.99 A; A=3241-3546.
DR   PDB; 3TNT; X-ray; 1.59 A; A=3241-3546.
DR   PDB; 3V3M; X-ray; 1.96 A; A=3241-3546.
DR   PDB; 3VB3; X-ray; 2.20 A; A/B=3241-3546.
DR   PDB; 3VB4; X-ray; 2.20 A; A/B=3241-3546.
DR   PDB; 3VB5; X-ray; 1.95 A; A/B=3241-3546.
DR   PDB; 3VB6; X-ray; 2.50 A; A/B=3241-3546.
DR   PDB; 3VB7; X-ray; 1.95 A; A/B=3241-3546.
DR   PDB; 4HI3; X-ray; 2.09 A; A/B=3241-3546.
DR   PDB; 4M0W; X-ray; 1.40 A; A=1541-1858.
DR   PDB; 4MDS; X-ray; 1.60 A; A=3241-3542.
DR   PDB; 4MM3; X-ray; 2.75 A; B=1541-1855.
DR   PDB; 4OVZ; X-ray; 2.50 A; A/B=1541-1855.
DR   PDB; 4OW0; X-ray; 2.10 A; A/B=1541-1855.
DR   PDB; 5F22; X-ray; 2.15 A; A=3837-3919.
DR   PDB; 5Y3E; X-ray; 1.65 A; A=1541-1854.
DR   PDB; 5Y3Q; X-ray; 1.65 A; A=1541-1854.
DR   PDB; 6NUR; EM; 3.10 A; B/D=3920-4117.
DR   PDB; 6NUS; EM; 3.50 A; B=3920-4117.
DR   PDB; 6Y7M; X-ray; 1.90 A; AAA=3241-3546.
DR   PDBsum; 1P76; -.
DR   PDBsum; 1P9T; -.
DR   PDBsum; 1PA5; -.
DR   PDBsum; 1PUK; -.
DR   PDBsum; 1Q1X; -.
DR   PDBsum; 1Q2W; -.
DR   PDBsum; 1QZ8; -.
DR   PDBsum; 1UJ1; -.
DR   PDBsum; 1UK2; -.
DR   PDBsum; 1UK3; -.
DR   PDBsum; 1UK4; -.
DR   PDBsum; 1UW7; -.
DR   PDBsum; 1WOF; -.
DR   PDBsum; 1YSY; -.
DR   PDBsum; 1Z1I; -.
DR   PDBsum; 1Z1J; -.
DR   PDBsum; 2A5A; -.
DR   PDBsum; 2A5I; -.
DR   PDBsum; 2A5K; -.
DR   PDBsum; 2ACF; -.
DR   PDBsum; 2AHM; -.
DR   PDBsum; 2AJ5; -.
DR   PDBsum; 2ALV; -.
DR   PDBsum; 2AMD; -.
DR   PDBsum; 2AMQ; -.
DR   PDBsum; 2BX3; -.
DR   PDBsum; 2BX4; -.
DR   PDBsum; 2C3S; -.
DR   PDBsum; 2D2D; -.
DR   PDBsum; 2DUC; -.
DR   PDBsum; 2FAV; -.
DR   PDBsum; 2FE8; -.
DR   PDBsum; 2FYG; -.
DR   PDBsum; 2G9T; -.
DR   PDBsum; 2GA6; -.
DR   PDBsum; 2GDT; -.
DR   PDBsum; 2GRI; -.
DR   PDBsum; 2GT7; -.
DR   PDBsum; 2GT8; -.
DR   PDBsum; 2GTB; -.
DR   PDBsum; 2GX4; -.
DR   PDBsum; 2GZ7; -.
DR   PDBsum; 2GZ8; -.
DR   PDBsum; 2GZ9; -.
DR   PDBsum; 2H2Z; -.
DR   PDBsum; 2HOB; -.
DR   PDBsum; 2HSX; -.
DR   PDBsum; 2IDY; -.
DR   PDBsum; 2KAF; -.
DR   PDBsum; 2KQV; -.
DR   PDBsum; 2KQW; -.
DR   PDBsum; 2KYS; -.
DR   PDBsum; 2LIZ; -.
DR   PDBsum; 2OP9; -.
DR   PDBsum; 2PWX; -.
DR   PDBsum; 2W2G; -.
DR   PDBsum; 2WCT; -.
DR   PDBsum; 2Z3C; -.
DR   PDBsum; 2Z3D; -.
DR   PDBsum; 2Z3E; -.
DR   PDBsum; 2ZU4; -.
DR   PDBsum; 2ZU5; -.
DR   PDBsum; 3ATW; -.
DR   PDBsum; 3AVZ; -.
DR   PDBsum; 3AW0; -.
DR   PDBsum; 3AW1; -.
DR   PDBsum; 3E91; -.
DR   PDBsum; 3EA7; -.
DR   PDBsum; 3EA8; -.
DR   PDBsum; 3EA9; -.
DR   PDBsum; 3EAJ; -.
DR   PDBsum; 3EE7; -.
DR   PDBsum; 3F9E; -.
DR   PDBsum; 3F9F; -.
DR   PDBsum; 3F9G; -.
DR   PDBsum; 3F9H; -.
DR   PDBsum; 3FZD; -.
DR   PDBsum; 3IWM; -.
DR   PDBsum; 3M3S; -.
DR   PDBsum; 3M3T; -.
DR   PDBsum; 3M3V; -.
DR   PDBsum; 3MJ5; -.
DR   PDBsum; 3R24; -.
DR   PDBsum; 3SN8; -.
DR   PDBsum; 3SNA; -.
DR   PDBsum; 3SNB; -.
DR   PDBsum; 3SNC; -.
DR   PDBsum; 3SND; -.
DR   PDBsum; 3SNE; -.
DR   PDBsum; 3SZN; -.
DR   PDBsum; 3TIT; -.
DR   PDBsum; 3TIU; -.
DR   PDBsum; 3TNS; -.
DR   PDBsum; 3TNT; -.
DR   PDBsum; 3V3M; -.
DR   PDBsum; 3VB3; -.
DR   PDBsum; 3VB4; -.
DR   PDBsum; 3VB5; -.
DR   PDBsum; 3VB6; -.
DR   PDBsum; 3VB7; -.
DR   PDBsum; 4HI3; -.
DR   PDBsum; 4M0W; -.
DR   PDBsum; 4MDS; -.
DR   PDBsum; 4MM3; -.
DR   PDBsum; 4OVZ; -.
DR   PDBsum; 4OW0; -.
DR   PDBsum; 5F22; -.
DR   PDBsum; 5Y3E; -.
DR   PDBsum; 5Y3Q; -.
DR   PDBsum; 6NUR; -.
DR   PDBsum; 6NUS; -.
DR   PDBsum; 6Y7M; -.
DR   SMR; P0C6U8; -.
DR   DIP; DIP-48580N; -.
DR   IntAct; P0C6U8; 3.
DR   BindingDB; P0C6U8; -.
DR   ChEMBL; CHEMBL3927; -.
DR   DrugBank; DB07620; 2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE.
DR   DrugBank; DB08732; NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE.
DR   DrugBank; DB07743; S-[5-(TRIFLUOROMETHYL)-4H-1,2,4-TRIAZOL-3-YL] 5-(PHENYLETHYNYL)FURAN-2-CARBOTHIOATE.
DR   MEROPS; C16.009; -.
DR   PRIDE; P0C6U8; -.
DR   BRENDA; 3.4.22.69; 7599.
DR   EvolutionaryTrace; P0C6U8; -.
DR   Proteomes; UP000000354; Genome.
DR   Proteomes; UP000103670; Genome.
DR   Proteomes; UP000109640; Genome.
DR   Proteomes; UP000116947; Genome.
DR   Proteomes; UP000121636; Genome.
DR   Proteomes; UP000131569; Genome.
DR   Proteomes; UP000131955; Genome.
DR   Proteomes; UP000137377; Genome.
DR   Proteomes; UP000138690; Genome.
DR   Proteomes; UP000143093; Genome.
DR   Proteomes; UP000145651; Genome.
DR   Proteomes; UP000146108; Genome.
DR   Proteomes; UP000146181; Genome.
DR   Proteomes; UP000146296; Genome.
DR   Proteomes; UP000148194; Genome.
DR   Proteomes; UP000153467; Genome.
DR   Proteomes; UP000160648; Genome.
DR   Proteomes; UP000164441; Genome.
DR   Proteomes; UP000172416; Genome.
DR   GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR   GO; GO:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   Gene3D; 1.10.150.420; -; 1.
DR   Gene3D; 1.10.8.1190; -; 1.
DR   Gene3D; 1.10.8.370; -; 1.
DR   Gene3D; 2.30.30.590; -; 1.
DR   Gene3D; 2.40.10.250; -; 1.
DR   Gene3D; 2.40.10.290; -; 1.
DR   Gene3D; 3.10.20.350; -; 1.
DR   Gene3D; 3.10.20.540; -; 1.
DR   Gene3D; 3.40.220.20; -; 1.
DR   Gene3D; 3.40.50.11020; -; 1.
DR   InterPro; IPR032505; Corona_NSP4_C.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR032592; NAR_dom.
DR   InterPro; IPR042570; NAR_sf.
DR   InterPro; IPR021590; NSP1.
DR   InterPro; IPR036333; NSP10_sf.
DR   InterPro; IPR038030; NSP1_sf.
DR   InterPro; IPR024375; Nsp3_coronavir.
DR   InterPro; IPR038400; Nsp3_coronavir_sf.
DR   InterPro; IPR022733; Nsp3_PL2pro.
DR   InterPro; IPR038166; Nsp3_PL2pro_sf.
DR   InterPro; IPR038123; NSP4_C_sf.
DR   InterPro; IPR014828; NSP7.
DR   InterPro; IPR037204; NSP7_sf.
DR   InterPro; IPR014829; NSP8.
DR   InterPro; IPR037230; NSP8_sf.
DR   InterPro; IPR014822; NSP9.
DR   InterPro; IPR036499; NSP9_sf.
DR   InterPro; IPR008740; Peptidase_C30.
DR   InterPro; IPR013016; Peptidase_C30/C16.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR038083; R1a/1ab.
DR   InterPro; IPR043177; R1a/1ab_N.
DR   InterPro; IPR043178; R1a/1ab_thumb.
DR   InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
DR   InterPro; IPR024358; SARS-CoV_Nsp3_N.
DR   InterPro; IPR014827; Viral_protease.
DR   Pfam; PF16348; Corona_NSP4_C; 1.
DR   Pfam; PF12379; DUF3655; 1.
DR   Pfam; PF01661; Macro; 1.
DR   Pfam; PF16251; NAR; 1.
DR   Pfam; PF11501; Nsp1; 1.
DR   Pfam; PF09401; NSP10; 1.
DR   Pfam; PF12124; Nsp3_PL2pro; 1.
DR   Pfam; PF08716; nsp7; 1.
DR   Pfam; PF08717; nsp8; 1.
DR   Pfam; PF08710; nsp9; 1.
DR   Pfam; PF05409; Peptidase_C30; 1.
DR   Pfam; PF11633; SUD-M; 1.
DR   Pfam; PF08715; Viral_protease; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF101816; SSF101816; 1.
DR   SUPFAM; SSF140367; SSF140367; 1.
DR   SUPFAM; SSF143076; SSF143076; 1.
DR   SUPFAM; SSF144246; SSF144246; 1.
DR   SUPFAM; SSF159936; SSF159936; 1.
DR   SUPFAM; SSF160099; SSF160099; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS51442; M_PRO; 1.
DR   PROSITE; PS51154; MACRO; 1.
DR   PROSITE; PS51124; PEPTIDASE_C16; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus;
KW   Decay of host mRNAs by virus; Endonuclease;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW   Host gene expression shutoff by virus; Host membrane;
KW   Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host ISG15 by virus;
KW   Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
KW   Modulation of host ubiquitin pathway by viral deubiquitinase;
KW   Modulation of host ubiquitin pathway by virus; Nuclease; Protease;
KW   Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
KW   Thiol protease; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..4382
FT                   /note="Replicase polyprotein 1a"
FT                   /id="PRO_0000338254"
FT   CHAIN           1..180
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338255"
FT   CHAIN           181..818
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338256"
FT   CHAIN           819..2740
FT                   /note="Non-structural protein 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338257"
FT   CHAIN           2741..3240
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338258"
FT   CHAIN           3241..3546
FT                   /note="3C-like proteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338259"
FT   CHAIN           3547..3836
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338260"
FT   CHAIN           3837..3919
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338261"
FT   CHAIN           3920..4117
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338262"
FT   CHAIN           4118..4230
FT                   /note="Non-structural protein 9"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338263"
FT   CHAIN           4231..4369
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338264"
FT   CHAIN           4370..4382
FT                   /note="Non-structural protein 11"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338265"
FT   TOPO_DOM        1..2202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2203..2223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2224..2303
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2304..2324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2325..2350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2351..2371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2372..2754
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2755..2775
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2776..2991
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2992..3012
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3013..3021
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3022..3042
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3043..3053
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3054..3074
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3075..3076
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3077..3097
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3098..3104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3105..3125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3126..3141
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3142..3162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3163..3563
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3564..3584
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3585
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3586..3606
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3607..3611
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3612..3632
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3633..3657
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3658..3678
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3679..3684
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3685..3704
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3705..3727
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3728..3748
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3749..3755
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3756..3776
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3777..4382
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          1003..1169
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1611..1875
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          3241..3546
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ZN_FING         1729..1766
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4304..4320
FT   ZN_FING         4347..4360
FT   REGION          2092..2371
FT                   /note="HD1"
FT   REGION          2755..3162
FT                   /note="HD2"
FT   REGION          3564..3776
FT                   /note="HD3"
FT   COMPBIAS        930..1001
FT                   /note="Glu-rich"
FT   COMPBIAS        2210..2213
FT                   /note="Poly-Leu"
FT   COMPBIAS        3766..3769
FT                   /note="Poly-Cys"
FT   ACT_SITE        1651
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1812
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3281
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3385
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   METAL           4304
FT                   /note="Zinc"
FT   METAL           4307
FT                   /note="Zinc"
FT   METAL           4313
FT                   /note="Zinc"
FT   METAL           4320
FT                   /note="Zinc"
FT   METAL           4347
FT                   /note="Zinc"
FT   METAL           4350
FT                   /note="Zinc"
FT   METAL           4358
FT                   /note="Zinc"
FT   SITE            180..181
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   SITE            818..819
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            2740..2741
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3240..3241
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3546..3547
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3836..3837
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3919..3920
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4117..4118
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4230..4231
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4369..4370
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   VARIANT         82
FT                   /note="G -> C (in strain: Isolate GD01)"
FT   VARIANT         130
FT                   /note="G -> R (in strain: Isolate GD01)"
FT   VARIANT         138
FT                   /note="I -> T (in strain: Isolate SZ16)"
FT   VARIANT         181
FT                   /note="A -> V (in strain: Isolate Shanghai LY)"
FT   VARIANT         225
FT                   /note="K -> Q (in strain: Isolate GD01)"
FT   VARIANT         249
FT                   /note="Y -> C (in strain: Isolate Shanghai LY)"
FT   VARIANT         306
FT                   /note="V -> F (in strain: Isolate BJ04)"
FT   VARIANT         549
FT                   /note="A -> S (in strain: Isolate SZ3)"
FT   VARIANT         765
FT                   /note="A -> T (in strain: Isolate FRA and Isolate
FT                   Frankfurt-1)"
FT   VARIANT         852
FT                   /note="K -> R (in strain: Isolate SZ16)"
FT   VARIANT         1004
FT                   /note="N -> H (in strain: Isolate BJ03)"
FT   VARIANT         1021
FT                   /note="V -> A (in strain: Isolate SZ3 and Isolate SZ16)"
FT   VARIANT         1023
FT                   /note="I -> T (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         1121
FT                   /note="I -> T (in strain: Isolate GD01, Isolate SZ3 and
FT                   Isolate SZ16)"
FT   VARIANT         1136
FT                   /note="P -> L (in strain: Isolate SZ3 and Isolate SZ16)"
FT   VARIANT         1257
FT                   /note="K -> E (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         1319
FT                   /note="K -> R (in strain: Isolate GD01)"
FT   VARIANT         1329
FT                   /note="F -> S (in strain: Isolate GD01)"
FT   VARIANT         1361
FT                   /note="T -> A (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         1385
FT                   /note="I -> V (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         1538
FT                   /note="S -> T (in strain: Isolate GD01)"
FT   VARIANT         1563
FT                   /note="M -> K (in strain: Isolate BJ02)"
FT   VARIANT         1663
FT                   /note="L -> I (in strain: Isolate SZ3 and Isolate SZ16)"
FT   VARIANT         1762
FT                   /note="I -> L (in strain: Isolate BJ03)"
FT   VARIANT         1776..1777
FT                   /note="QQ -> PP (in strain: Isolate BJ03)"
FT   VARIANT         1790
FT                   /note="E -> G (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         1806
FT                   /note="G -> V (in strain: Isolate BJ02)"
FT   VARIANT         1962
FT                   /note="L -> I (in strain: Isolate BJ04)"
FT   VARIANT         2116
FT                   /note="L -> F (in strain: Isolate GD01, Isolate SZ3 and
FT                   Isolate SZ16)"
FT   VARIANT         2222
FT                   /note="C -> Y (in strain: Isolate GD01, Isolate SZ3 and
FT                   Isolate SZ16)"
FT   VARIANT         2269
FT                   /note="L -> S (in strain: Isolate SZ3 and Isolate SZ16)"
FT   VARIANT         2326
FT                   /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         2392..2394
FT                   /note="RNR -> CNH (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         2480
FT                   /note="L -> P (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         2552
FT                   /note="A -> V (in strain: Isolate Urbani and Isolate Taiwan
FT                   TC2)"
FT   VARIANT         2556
FT                   /note="D -> N (in strain: Isolate HKU-39849)"
FT   VARIANT         2564
FT                   /note="S -> P (in strain: Isolate GD01)"
FT   VARIANT         2648
FT                   /note="N -> Y (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         2708
FT                   /note="S -> T (in strain: Isolate HKU-39849)"
FT   VARIANT         2718
FT                   /note="R -> T (in strain: Isolate HKU-39849)"
FT   VARIANT         2746
FT                   /note="C -> W (in strain: Isolate SZ3 and Isolate SZ16)"
FT   VARIANT         2770
FT                   /note="V -> L (in strain: Isolate BJ01 and Isolate BJ02)"
FT   VARIANT         2944
FT                   /note="T -> I (in strain: Isolate SIN2500, Isolate GD01 and
FT                   Isolate GZ50)"
FT   VARIANT         2971
FT                   /note="V -> A (in strain: Isolate GD01 and Isolate SZ16)"
FT   VARIANT         3020
FT                   /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         3047
FT                   /note="V -> A (in strain: Isolate CUHK-W1, Isolate GD01,
FT                   Isolate SZ3, Isolate SZ16, Isolate BJ01, Isolate BJ02,
FT                   Isolate BJ03 and Isolate Shanghai QXC1)"
FT   VARIANT         3072
FT                   /note="V -> A (in strain: Isolate CUHK-W1, Isolate SZ3,
FT                   Isolate SZ16 and Isolate GD01)"
FT   VARIANT         3197
FT                   /note="A -> V (in strain: Isolate BJ01, Isolate BJ02,
FT                   Isolate BJ03, Isolate BJ04 and Isolate Shanghai QXC1)"
FT   VARIANT         3429
FT                   /note="Q -> P (in strain: Isolate BJ02)"
FT   VARIANT         3488
FT                   /note="D -> E (in strain: Isolate BJ04)"
FT   VARIANT         3717
FT                   /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         3818
FT                   /note="N -> T (in strain: Isolate BJ04)"
FT   VARIANT         3903
FT                   /note="D -> N (in strain: Isolate BJ03)"
FT   VARIANT         3904
FT                   /note="I -> F (in strain: Isolate BJ02)"
FT   VARIANT         3911
FT                   /note="M -> V (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         4001
FT                   /note="K -> Q (in strain: Isolate Shanghai LY)"
FT   VARIANT         4003
FT                   /note="T -> A (in strain: Isolate Shanghai LY)"
FT   VARIANT         4085
FT                   /note="I -> H (in strain: Isolate ZJ01)"
FT   VARIANT         4114
FT                   /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         4202
FT                   /note="V -> M (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         4240
FT                   /note="N -> H (in strain: Isolate ZJ01)"
FT   VARIANT         4296
FT                   /note="E -> G (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         4377..4378
FT                   /note="LN -> FK (in strain: Isolate Shanghai QXC1)"
FT   STRAND          1208..1211
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1214..1216
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1219..1222
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   TURN            1223..1225
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1229..1233
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1235..1237
FT                   /evidence="ECO:0000244|PDB:2WCT"
FT   HELIX           1241..1244
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1253..1255
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   TURN            1256..1258
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1266..1269
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1272..1276
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1280..1282
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1286..1293
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1298..1303
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1309..1312
FT                   /evidence="ECO:0000244|PDB:2WCT"
FT   HELIX           1315..1324
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1325..1331
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1343..1345
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1351..1361
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1364..1368
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1372..1381
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   TURN            1382..1384
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1389..1401
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1403..1405
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1407..1417
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1421..1423
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   TURN            1429..1431
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1435..1442
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   STRAND          1449..1452
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1456..1467
FT                   /evidence="ECO:0000244|PDB:2W2G"
FT   HELIX           1473..1484
FT                   /evidence="ECO:0000244|PDB:2KAF"
FT   STRAND          1485..1487
FT                   /evidence="ECO:0000244|PDB:2KQW"
FT   STRAND          1500..1506
FT                   /evidence="ECO:0000244|PDB:2KAF"
FT   STRAND          1509..1513
FT                   /evidence="ECO:0000244|PDB:2KAF"
FT   STRAND          1515..1518
FT                   /evidence="ECO:0000244|PDB:2KAF"
FT   STRAND          1521..1523
FT                   /evidence="ECO:0000244|PDB:2KAF"
FT   STRAND          1526..1528
FT                   /evidence="ECO:0000244|PDB:2KQW"
FT   HELIX           1530..1537
FT                   /evidence="ECO:0000244|PDB:2KAF"
FT   STRAND          1544..1555
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1557..1562
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1563..1565
FT                   /evidence="ECO:0000244|PDB:4OVZ"
FT   HELIX           1567..1570
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1571..1576
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1581..1583
FT                   /evidence="ECO:0000244|PDB:4OW0"
FT   HELIX           1588..1590
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1594..1597
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1602..1612
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1619..1630
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   TURN            1648..1650
FT                   /evidence="ECO:0000244|PDB:2FE8"
FT   HELIX           1651..1660
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1667..1669
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1670..1680
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1685..1695
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1705..1713
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1722..1729
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   TURN            1730..1732
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1733..1740
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1741..1744
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1746..1749
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1753..1758
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1760..1763
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1767..1794
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1799..1806
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           1808..1810
FT                   /evidence="ECO:0000244|PDB:2FE8"
FT   STRAND          1811..1826
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1829..1846
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   STRAND          1848..1851
FT                   /evidence="ECO:0000244|PDB:4M0W"
FT   HELIX           3251..3254
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3257..3262
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3265..3272
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3275..3279
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3280..3283
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3286..3288
FT                   /evidence="ECO:0000244|PDB:2ZU5"
FT   STRAND          3289..3291
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3294..3299
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3303..3305
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3306..3310
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3313..3315
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3317..3323
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3326..3333
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3340..3343
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3351..3358
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3361..3369
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   TURN            3380..3383
FT                   /evidence="ECO:0000244|PDB:3F9F"
FT   STRAND          3388..3393
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3396..3406
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   TURN            3408..3410
FT                   /evidence="ECO:0000244|PDB:3F9E"
FT   STRAND          3412..3415
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3417..3419
FT                   /evidence="ECO:0000244|PDB:3F9G"
FT   STRAND          3421..3424
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3427..3430
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3441..3453
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   TURN            3458..3460
FT                   /evidence="ECO:0000244|PDB:3IWM"
FT   HELIX           3467..3476
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3484..3489
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3491..3497
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3501..3514
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3521..3523
FT                   /evidence="ECO:0000244|PDB:3F9E"
FT   STRAND          3524..3526
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   HELIX           3533..3539
FT                   /evidence="ECO:0000244|PDB:3TNT"
FT   STRAND          3541..3543
FT                   /evidence="ECO:0000244|PDB:2LIZ"
FT   HELIX           3838..3855
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           3858..3860
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           3862..3877
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           3881..3896
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           3904..3913
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           3997..4017
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           4020..4030
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   STRAND          4035..4037
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           4040..4043
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4046..4051
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           4054..4060
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   STRAND          4065..4068
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   STRAND          4071..4079
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           4088..4090
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   TURN            4093..4095
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   HELIX           4096..4098
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   STRAND          4103..4109
FT                   /evidence="ECO:0000244|PDB:5F22"
FT   STRAND          4127..4136
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   TURN            4137..4139
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   STRAND          4142..4150
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   TURN            4152..4154
FT                   /evidence="ECO:0000244|PDB:1QZ8"
FT   STRAND          4157..4164
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   STRAND          4170..4173
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   STRAND          4176..4179
FT                   /evidence="ECO:0000244|PDB:1QZ8"
FT   STRAND          4180..4186
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   STRAND          4190..4194
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   STRAND          4201..4208
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   HELIX           4213..4224
FT                   /evidence="ECO:0000244|PDB:3EE7"
FT   HELIX           4240..4248
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   STRAND          4250..4252
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   HELIX           4253..4262
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   STRAND          4273..4275
FT                   /evidence="ECO:0000244|PDB:2G9T"
FT   STRAND          4284..4288
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   STRAND          4295..4299
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   HELIX           4301..4303
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   HELIX           4305..4309
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   STRAND          4316..4318
FT                   /evidence="ECO:0000244|PDB:2GA6"
FT   TURN            4321..4324
FT                   /evidence="ECO:0000244|PDB:2GA6"
FT   STRAND          4325..4330
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   HELIX           4331..4333
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   HELIX           4337..4343
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   TURN            4348..4350
FT                   /evidence="ECO:0000244|PDB:2FYG"
FT   TURN            4354..4356
FT                   /evidence="ECO:0000244|PDB:2FYG"
SQ   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
//