ID   R1AB_CVHSA              Reviewed;        7073 AA.
AC   P0C6X7; P59641; Q6WGN0; Q7T697; Q808C0; Q80BV7; Q80BV8; Q80E51;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   12-AUG-2020, entry version 112.
DE   RecName: Full=Replicase polyprotein 1ab;
DE            Short=pp1ab;
DE   AltName: Full=ORF1ab polyprotein;
DE   Contains:
DE     RecName: Full=Host translation inhibitor nsp1;
DE     AltName: Full=Leader protein;
DE     AltName: Full=Non-structural protein 1;
DE              Short=nsp1;
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=3.4.22.69;
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.-;
DE     AltName: Full=Main protease;
DE              Short=Mpro;
DE     AltName: Full=Non-structural protein 5;
DE              Short=nsp5;
DE     AltName: Full=SARS coronavirus main proteinase;
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=RNA-directed RNA polymerase;
DE              Short=Pol;
DE              Short=RdRp;
DE              EC=2.7.7.48;
DE     AltName: Full=Non-structural protein 12;
DE              Short=nsp12;
DE   Contains:
DE     RecName: Full=Helicase;
DE              Short=Hel;
DE              EC=3.6.4.12;
DE              EC=3.6.4.13;
DE     AltName: Full=Non-structural protein 13;
DE              Short=nsp13;
DE   Contains:
DE     RecName: Full=Proofreading exoribonuclease {ECO:0000303|PubMed:23966862, ECO:0000303|PubMed:29511076};
DE              Short=ExoN;
DE              EC=2.1.1.-;
DE              EC=3.1.13.-;
DE     AltName: Full=Guanine-N7 methyltransferase;
DE     AltName: Full=Non-structural protein 14;
DE              Short=nsp14;
DE   Contains:
DE     RecName: Full=Uridylate-specific endoribonuclease;
DE              EC=3.1.-.-;
DE     AltName: Full=NendoU;
DE     AltName: Full=Non-structural protein 15;
DE              Short=nsp15;
DE   Contains:
DE     RecName: Full=2'-O-methyltransferase;
DE              EC=2.1.1.-;
DE     AltName: Full=Non-structural protein 16;
DE              Short=nsp16;
GN   Name=rep; ORFNames=1a-1b;
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; 1655-5170 AND 6903-7073.
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   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4993-5127.
RC   STRAIN=Isolate Vietnam;
RA   Emery S., Erdman D.D., Peret T.C.T., Ksiazek T.G.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [22]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4993-5136.
RC   STRAIN=Isolate Taiwan;
RA   Lin J.-H., Chiu S.-C., Yang J.-Y., Wang S.-F., Chen H.-Y.;
RT   "Detection of a novel human coronavirus in a severe acute respiratory
RT   syndrome patient in Taiwan.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [23]
RP   FUNCTION (HELICASE).
RX   PubMed=12917423; DOI=10.1074/jbc.c300328200;
RA   Tanner J.A., Watt R.M., Chai Y.-B., Lu L.-Y., Lin M.C., Peiris J.S.,
RA   Poon L.L.M., Kung H.-F., Huang J.-D.;
RT   "The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase
RT   belongs to a distinct class of 5' to 3' viral helicases.";
RL   J. Biol. Chem. 278:39578-39582(2003).
RN   [24]
RP   PROTEOLYTIC PROCESSING (REPLICASE POLYPROTEIN 1AB).
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   [25]
RP   CATALYTIC ACTIVITY (3C-LIKE PROTEINASE), SUBUNIT (3C-LIKE PROTEINASE), AND
RP   BIOPHYSICOCHEMICAL PROPERTIES (3C-LIKE PROTEINASE).
RX   PubMed=14561748; DOI=10.1074/jbc.m310875200;
RA   Fan K., Wei P., Feng Q., Chen S., Huang C., Ma L., Lai B., Pei J., Liu Y.,
RA   Chen J., Lai L.;
RT   "Biosynthesis, purification, and substrate specificity of severe acute
RT   respiratory syndrome coronavirus 3C-like proteinase.";
RL   J. Biol. Chem. 279:1637-1642(2004).
RN   [26]
RP   PROTEOLYTIC PROCESSING (REPLICASE POLYPROTEIN 1AB).
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   [27]
RP   PROTEOLYTIC PROCESSING (REPLICASE POLYPROTEIN 1AB).
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   [28]
RP   FUNCTION (3C-LIKE PROTEINASE).
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   [29]
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   [30]
RP   FUNCTION (GUANINE-N7 METHYLTRANSFERASE).
RC   STRAIN=Isolate Frankfurt-1;
RX   PubMed=16549795; DOI=10.1073/pnas.0508200103;
RA   Minskaia E., Hertzig T., Gorbalenya A.E., Campanacci V., Cambillau C.,
RA   Canard B., Ziebuhr J.;
RT   "Discovery of an RNA virus 3'->5' exoribonuclease that is critically
RT   involved in coronavirus RNA synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5108-5113(2006).
RN   [31]
RP   CHARACTERIZATION (URIDYLATE-SPECIFIC ENDORIBONUCLEASE).
RX   PubMed=16882730; DOI=10.1073/pnas.0601708103;
RA   Ricagno S., Egloff M.-P., Ulferts R., Coutard B., Nurizzo D.,
RA   Campanacci V., Cambillau C., Ziebuhr J., Canard B.;
RT   "Crystal structure and mechanistic determinants of SARS coronavirus
RT   nonstructural protein 15 define an endoribonuclease family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11892-11897(2006).
RN   [32]
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   [33]
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   [34]
RP   SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4).
RX   PubMed=17855519; DOI=10.1128/jvi.01506-07;
RA   Oostra M., te Lintelo E.G., Deijs M., Verheije M.H., Rottier P.J.,
RA   de Haan C.A.;
RT   "Localization and membrane topology of coronavirus nonstructural protein 4:
RT   involvement of the early secretory pathway in replication.";
RL   J. Virol. 81:12323-12336(2007).
RN   [35]
RP   INTERACTION WITH ORF6 PROTEIN.
RX   PubMed=17532020; DOI=10.1016/j.virol.2007.04.029;
RA   Kumar P., Gunalan V., Liu B., Chow V.T., Druce J., Birch C., Catton M.,
RA   Fielding B.C., Tan Y.J., Lal S.K.;
RT   "The nonstructural protein 8 (nsp8) of the SARS coronavirus interacts with
RT   its ORF6 accessory protein.";
RL   Virology 366:293-303(2007).
RN   [36]
RP   FUNCTION (2'-O-METHYLTRANSFERASE).
RX   PubMed=18417574; DOI=10.1128/jvi.00407-08;
RA   Decroly E., Imbert I., Coutard B., Bouvet M., Selisko B., Alvarez K.,
RA   Gorbalenya A.E., Snijder E.J., Canard B.;
RT   "Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing
RT   (nucleoside-2'O)-methyltransferase activity.";
RL   J. Virol. 82:8071-8084(2008).
RN   [37]
RP   INTERACTION OF NSP10 WITH NSP14 AND NSP16.
RX   PubMed=18827877; DOI=10.1371/journal.pone.0003299;
RA   Pan J., Peng X., Gao Y., Li Z., Lu X., Chen Y., Ishaq M., Liu D.,
RA   Dediego M.L., Enjuanes L., Guo D.;
RT   "Genome-wide analysis of protein-protein interactions and involvement of
RT   viral proteins in SARS-CoV replication.";
RL   PLoS ONE 3:E3299-E3299(2008).
RN   [38]
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   [39]
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   [40]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 9), AND MUTAGENESIS OF GLY-4217 AND
RP   GLY-4221.
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   [41]
RP   INTERACTION (PROOFREADING EXORIBONUCLEASE) WITH HOST DDX1.
RX   PubMed=20573827; DOI=10.1128/jvi.00392-10;
RA   Xu L., Khadijah S., Fang S., Wang L., Tay F.P., Liu D.X.;
RT   "The cellular RNA helicase DDX1 interacts with coronavirus nonstructural
RT   protein 14 and enhances viral replication.";
RL   J. Virol. 84:8571-8583(2010).
RN   [42]
RP   FUNCTION (GUANINE-N7 METHYLTRANSFERASE), AND FUNCTION
RP   (2'-O-METHYLTRANSFERASE).
RX   PubMed=20421945; DOI=10.1371/journal.ppat.1000863;
RA   Bouvet M., Debarnot C., Imbert I., Selisko B., Snijder E.J., Canard B.,
RA   Decroly E.;
RT   "In vitro reconstitution of SARS-coronavirus mRNA cap methylation.";
RL   PLoS Pathog. 6:E1000863-E1000863(2010).
RN   [43]
RP   FUNCTION (HOST TRANSLATION INHIBITOR 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   [44]
RP   INTERACTION OF NSP4 WITH PL-PRO AND NSP6, AND SUBCELLULAR LOCATION
RP   (NON-STRUCTURAL PROTEIN 4).
RX   PubMed=21345958; DOI=10.1128/jvi.00042-11;
RA   Hagemeijer M.C., Ulasli M., Vonk A.M., Reggiori F., Rottier P.J.,
RA   de Haan C.A.;
RT   "Mobility and interactions of coronavirus nonstructural protein 4.";
RL   J. Virol. 85:4572-4577(2011).
RN   [45]
RP   FUNCTION (PROOFREADING EXORIBONUCLEASE).
RX   PubMed=21593585; DOI=10.4161/rna.8.2.15013;
RA   Denison M.R., Graham R.L., Donaldson E.F., Eckerle L.D., Baric R.S.;
RT   "Coronaviruses: an RNA proofreading machine regulates replication fidelity
RT   and diversity.";
RL   RNA Biol. 8:270-279(2011).
RN   [46]
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   [47]
RP   FUNCTION (HOST TRANSLATION INHIBITOR NSP1).
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   [48]
RP   FUNCTION (HELICASE).
RX   PubMed=22615777; DOI=10.1371/journal.pone.0036521;
RA   Adedeji A.O., Marchand B., Te Velthuis A.J., Snijder E.J., Weiss S.,
RA   Eoff R.L., Singh K., Sarafianos S.G.;
RT   "Mechanism of nucleic acid unwinding by SARS-CoV helicase.";
RL   PLoS ONE 7:E36521-E36521(2012).
RN   [49]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=22791111; DOI=10.1007/s00705-012-1404-x;
RA   Ahn D.G., Choi J.K., Taylor D.R., Oh J.W.;
RT   "Biochemical characterization of a recombinant SARS coronavirus nsp12 RNA-
RT   dependent RNA polymerase capable of copying viral RNA templates.";
RL   Arch. Virol. 157:2095-2104(2012).
RN   [50]
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   [51]
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   [52]
RP   FUNCTION (PROOFREADING EXORIBONUCLEASE).
RX   PubMed=23966862; DOI=10.1371/journal.ppat.1003565;
RA   Smith E.C., Blanc H., Surdel M.C., Vignuzzi M., Denison M.R.;
RT   "Coronaviruses lacking exoribonuclease activity are susceptible to lethal
RT   mutagenesis: evidence for proofreading and potential therapeutics.";
RL   PLoS Pathog. 9:e1003565-e1003565(2013).
RN   [53]
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   [54]
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   [55]
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   [56]
RP   FUNCTION (PROOFREADING EXORIBONUCLEASE), AND ACTIVITY REGULATION
RP   (PROOFREADING EXORIBONUCLEASE).
RX   PubMed=29511076; DOI=10.1128/mbio.00221-18;
RA   Agostini M.L., Andres E.L., Sims A.C., Graham R.L., Sheahan T.P., Lu X.,
RA   Smith E.C., Case J.B., Feng J.Y., Jordan R., Ray A.S., Cihlar T.,
RA   Siegel D., Mackman R.L., Clarke M.O., Baric R.S., Denison M.R.;
RT   "Coronavirus Susceptibility to the Antiviral Remdesivir (GS-5734) Is
RT   Mediated by the Viral Polymerase and the Proofreading Exoribonuclease.";
RL   MBio 9:0-0(2018).
RN   [57]
RP   INTERACTION WITH HOST 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   [58]
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   [59]
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   [60]
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   [61]
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   [62]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230, AND INTERACTION OF NSP8
RP   WITH NSP9.
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   [63]
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   [64]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1002-1176, AND FUNCTION (3C-LIKE
RP   PROTEINASE).
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   [65]
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   [66]
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   [67]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4231-4378, AND SUBUNIT
RP   (NON-STRUCTURAL PROTEIN 10).
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   [68]
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   [69]
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: [Isoform Replicase polyprotein 1ab]: Multifunctional protein
CC       involved in the transcription and replication of viral RNAs. Contains
CC       the proteinases responsible for the cleavages of the polyprotein.
CC   -!- FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation
CC       by 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:16271890,
CC       ECO:0000269|PubMed:17692280, ECO:0000269|PubMed:19369340,
CC       ECO:0000269|PubMed:24622840, 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}.
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   -!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
CC       and transcription of the viral RNA genome.
CC       {ECO:0000269|PubMed:22791111}.
CC   -!- FUNCTION: [Helicase]: Multi-functional protein with a zinc-binding
CC       domain in N-terminus displaying RNA and DNA duplex-unwinding activities
CC       with 5' to 3' polarity. Activity of helicase is dependent on magnesium.
CC       {ECO:0000269|PubMed:12917423, ECO:0000269|PubMed:22615777}.
CC   -!- FUNCTION: [Proofreading exoribonuclease]: Enzyme possessing two
CC       different activities: an exoribonuclease activity acting on both ssRNA
CC       and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase
CC       activity (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a
CC       proofreading exoribonuclease for RNA replication, thereby lowering The
CC       sensitivity of the virus to RNA mutagens (PubMed:23966862,
CC       PubMed:29511076, PubMed:21593585). {ECO:0000269|PubMed:16549795,
CC       ECO:0000269|PubMed:20421945, ECO:0000269|PubMed:21593585,
CC       ECO:0000269|PubMed:22635272, ECO:0000269|PubMed:23966862,
CC       ECO:0000269|PubMed:29511076}.
CC   -!- FUNCTION: [Uridylate-specific endoribonuclease]: Mn(2+)-dependent,
CC       uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to
CC       the cleaved bond.
CC   -!- FUNCTION: [2'-O-methyltransferase]: Methyltransferase that mediates
CC       mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
CC       mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16.
CC       Therefore plays an essential role in viral mRNAs cap methylation which
CC       is essential to evade immune system. {ECO:0000269|PubMed:18417574,
CC       ECO:0000269|PubMed:20421945, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539,
CC         ECO:0000269|PubMed:14561748};
CC   -!- CATALYTIC ACTIVITY: [Helicase]:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- CATALYTIC ACTIVITY: [Helicase]:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
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         Evidence={ECO:0000269|PubMed:14561748};
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; Evidence={ECO:0000269|PubMed:17692280};
CC   -!- ACTIVITY REGULATION: [Proofreading exoribonuclease]: Inhibited by
CC       Remdesivir (GS-5734). {ECO:0000269|PubMed:29511076}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.15 mM for peptide TSAVLQSGFRK-NH(2)
CC         {ECO:0000269|PubMed:14561748};
CC         KM=0.58 mM for peptide SGVTFQGKFKK {ECO:0000269|PubMed:14561748};
CC         KM=1.44 mM for peptide ATVRLQAGNAT {ECO:0000269|PubMed:14561748};
CC         Note=The kinetic parameters are studied for the 3C-like proteinase
CC         domain.;
CC       pH dependence:
CC         Optimum pH is 7.0 for 3C-like proteinase activity.
CC         {ECO:0000269|PubMed:14561748};
CC   -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC       {ECO:0000269|PubMed:19640993}.
CC   -!- SUBUNIT: [Non-structural protein 4]: Interacts with PL-PRO and nsp6.
CC       {ECO:0000269|PubMed:21345958}.
CC   -!- SUBUNIT: [3C-like proteinase]: Exists as monomer and homodimer. Only
CC       the homodimer shows catalytic activity. {ECO:0000269|PubMed:14561748,
CC       ECO:0000269|PubMed:15507456}.
CC   -!- SUBUNIT: [Non-structural protein 7]: Eight copies of nsp7 and eight
CC       copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC       ring structure. {ECO:0000269|PubMed:16228002}.
CC   -!- SUBUNIT: [Non-structural protein 8]: Interacts with ORF6 protein.
CC       {ECO:0000269|PubMed:17532020}.
CC   -!- SUBUNIT: [Non-structural protein 9]: Homodimerizes.
CC       {ECO:0000269|PubMed:19153232}.
CC   -!- SUBUNIT: [Non-structural protein 10]: Forms a dodecamer and interacts
CC       with nsp14 and nsp16; these interactions enhance nsp14 and nsp16
CC       enzymatic activities. {ECO:0000269|PubMed:16873247,
CC       ECO:0000269|PubMed:18827877, ECO:0000269|PubMed:22635272}.
CC   -!- SUBUNIT: [Proofreading exoribonuclease]: Interacts (via N-terminus)
CC       with DDX1. {ECO:0000269|PubMed:20573827}.
CC   -!- INTERACTION:
CC       P0C6X7; P0C6X7: rep; NbExp=2; IntAct=EBI-7843867, EBI-7843867;
CC       PRO_0000037309; P59637: E; NbExp=2; IntAct=EBI-25475797, EBI-25487741;
CC       PRO_0000037309; Q9UQN3: CHMP2B; Xeno; NbExp=2; IntAct=EBI-25475797, EBI-718324;
CC       PRO_0000037309; P62942: FKBP1A; Xeno; NbExp=4; IntAct=EBI-25475797, EBI-1027571;
CC       PRO_0000037309; Q9Y4W2: LAS1L; Xeno; NbExp=2; IntAct=EBI-25475797, EBI-1051591;
CC       PRO_0000037309; P62937: PPIA; Xeno; NbExp=4; IntAct=EBI-25475797, EBI-437708;
CC       PRO_0000037309; Q13427: PPIG; Xeno; NbExp=4; IntAct=EBI-25475797, EBI-396072;
CC       PRO_0000037309; O43447: PPIH; Xeno; NbExp=4; IntAct=EBI-25475797, EBI-1055615;
CC       PRO_0000037309; Q9UKA8: RCAN3; Xeno; NbExp=2; IntAct=EBI-25475797, EBI-9091952;
CC       PRO_0000037310; PRO_0000338265 [P0C6U8]: 1a; NbExp=2; IntAct=EBI-25474098, EBI-25492625;
CC       PRO_0000037310; P59632: 3a; NbExp=2; IntAct=EBI-25474098, EBI-15595051;
CC       PRO_0000037310; PRO_0000037310 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25474098, EBI-25474098;
CC       PRO_0000037310; PRO_0000037311 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25474098, EBI-25474079;
CC       PRO_0000037310; PRO_0000037315 [P0C6X7]: rep; NbExp=4; IntAct=EBI-25474098, EBI-25487941;
CC       PRO_0000037310; P05155: SERPING1; Xeno; NbExp=2; IntAct=EBI-25474098, EBI-1223454;
CC       PRO_0000037311; PRO_0000037312 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25474079, EBI-25487250;
CC       PRO_0000037311; PRO_0000037315 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25474079, EBI-25487941;
CC       PRO_0000037311; PRO_0000037318 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25474079, EBI-25487684;
CC       PRO_0000037311; Q14653: IRF3; Xeno; NbExp=4; IntAct=EBI-25474079, EBI-2650369;
CC       PRO_0000037311; Q9H000: MKRN2; Xeno; NbExp=2; IntAct=EBI-25474079, EBI-2341005;
CC       PRO_0000037311; Q13064: MKRN3; Xeno; NbExp=2; IntAct=EBI-25474079, EBI-2340269;
CC       PRO_0000037312; PRO_0000037315 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25487250, EBI-25487941;
CC       PRO_0000037312; P62942: FKBP1A; Xeno; NbExp=2; IntAct=EBI-25487250, EBI-1027571;
CC       PRO_0000037313; PRO_0000037310 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25487192, EBI-25474098;
CC       PRO_0000037314; PRO_0000037315 [P0C6X7]: rep; NbExp=4; IntAct=EBI-25487672, EBI-25487941;
CC       PRO_0000037314; O95865: DDAH2; Xeno; NbExp=2; IntAct=EBI-25487672, EBI-749139;
CC       PRO_0000037314; A9UHW6: MIF4GD; Xeno; NbExp=2; IntAct=EBI-25487672, EBI-373498;
CC       PRO_0000037315; P59637: E; NbExp=2; IntAct=EBI-25487941, EBI-25487741;
CC       PRO_0000037315; PRO_0000037315 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25487941, EBI-25487941;
CC       PRO_0000037315; Q9P0M6: MACROH2A2; Xeno; NbExp=2; IntAct=EBI-25487941, EBI-3922608;
CC       PRO_0000037315; P69849: NOMO3; Xeno; NbExp=2; IntAct=EBI-25487941, EBI-947048;
CC       PRO_0000037315; P54274: TERF1; Xeno; NbExp=2; IntAct=EBI-25487941, EBI-710997;
CC       PRO_0000037316; PRO_0000037309 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25475825, EBI-25475797;
CC       PRO_0000037316; PRO_0000037314 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25475825, EBI-25487672;
CC       PRO_0000037316; PRO_0000037315 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25475825, EBI-25487941;
CC       PRO_0000037316; PRO_0000037320 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25475825, EBI-25487328;
CC       PRO_0000037316; Q9UQN3: CHMP2B; Xeno; NbExp=2; IntAct=EBI-25475825, EBI-718324;
CC       PRO_0000037316; Q5SQN1: SNAP47; Xeno; NbExp=2; IntAct=EBI-25475825, EBI-10244848;
CC       PRO_0000037318; PRO_0000037315 [P0C6X7]: rep; NbExp=5; IntAct=EBI-25487684, EBI-25487941;
CC       PRO_0000037319; PRO_0000037311 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25487926, EBI-25474079;
CC       PRO_0000037319; PRO_0000037315 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25487926, EBI-25487941;
CC       PRO_0000037319; PRO_0000037318 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25487926, EBI-25487684;
CC       PRO_0000037319; O96017: CHEK2; Xeno; NbExp=2; IntAct=EBI-25487926, EBI-1180783;
CC       PRO_0000037319; Q8N488: RYBP; Xeno; NbExp=2; IntAct=EBI-25487926, EBI-752324;
CC       PRO_0000037320; P59636: 9b; NbExp=3; IntAct=EBI-25487328, EBI-9021274;
CC       PRO_0000037320; PRO_0000037311 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25487328, EBI-25474079;
CC       PRO_0000037320; PRO_0000037315 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25487328, EBI-25487941;
CC       PRO_0000037320; PRO_0000037317 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25487328, EBI-25487277;
CC       PRO_0000037320; PRO_0000037318 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25487328, EBI-25487684;
CC       PRO_0000037320; P05155: SERPING1; Xeno; NbExp=2; IntAct=EBI-25487328, EBI-1223454;
CC       PRO_0000037321; PRO_0000037315 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25487301, EBI-25487941;
CC       PRO_0000037322; PRO_0000037310 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25487235, EBI-25474098;
CC       PRO_0000037322; PRO_0000037311 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25487235, EBI-25474079;
CC       PRO_0000037322; P40337: VHL; Xeno; NbExp=7; IntAct=EBI-25487235, EBI-301246;
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane; Multi-
CC       pass membrane protein. Host cytoplasm {ECO:0000269|PubMed:23943763}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-
CC       pass membrane protein. Host cytoplasm. Note=Localizes in virally-
CC       induced cytoplasmic double-membrane vesicles.
CC       {ECO:0000269|PubMed:17855519, ECO:0000269|PubMed:21345958,
CC       ECO:0000269|PubMed:23943763}.
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:0000269|PubMed:17532020}. Note=nsp7, nsp8, nsp9
CC       and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
CC       in infection, they merge into confluent complexes (By similarity).
CC       {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   -!- SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi
CC       intermediate compartment {ECO:0000305}. Note=The helicase interacts
CC       with the N protein in membranous complexes and colocalizes with sites
CC       of synthesis of new viral RNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
CC       cytoplasm, host perinuclear region {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6X7-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6U8-1; 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 (PubMed:32083638). 3CL-PRO and PL-PRO proteinases are
CC       autocatalytically processed (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:32083638}.
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 1ab]: Produced by -1
CC       ribosomal frameshifting at the 1a-1b genes boundary.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP13440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAP41036.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAP82975.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAP97881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAQ01596.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAQ01608.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AY278741; AAP13442.1; -; Genomic_RNA.
DR   EMBL; AY278741; AAP13440.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; AY274119; AAP41036.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; AY278554; AAP13566.1; -; Genomic_RNA.
DR   EMBL; AY282752; AAP30711.1; -; 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; AAP49011.4; -; Genomic_RNA.
DR   EMBL; AY278488; AAP30028.1; -; Genomic_RNA.
DR   EMBL; AY278489; AAP51225.1; -; Genomic_RNA.
DR   EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY291451; AAP37015.1; -; Genomic_RNA.
DR   EMBL; AY310120; AAP50483.1; -; Genomic_RNA.
DR   EMBL; AY291315; AAP33696.1; -; Genomic_RNA.
DR   EMBL; AY323977; AAP72973.2; -; Genomic_RNA.
DR   EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY338174; AAQ01594.1; -; Genomic_RNA.
DR   EMBL; AY338174; AAQ01596.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; AY338175; AAQ01606.1; -; Genomic_RNA.
DR   EMBL; AY338175; AAQ01608.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; AY348314; AAP97879.1; -; Genomic_RNA.
DR   EMBL; AY348314; AAP97881.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; AP006557; BAC81346.1; -; Genomic_RNA.
DR   EMBL; AP006558; BAC81360.1; -; Genomic_RNA.
DR   EMBL; AP006559; BAC81374.1; -; Genomic_RNA.
DR   EMBL; AP006560; BAC81388.1; -; Genomic_RNA.
DR   EMBL; AP006561; BAC81402.1; -; Genomic_RNA.
DR   EMBL; AY427439; AAQ94058.1; -; Genomic_RNA.
DR   EMBL; AY322205; AAP82966.1; -; Genomic_RNA.
DR   EMBL; AY322206; AAP82975.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; AY322207; AAP82967.1; -; Genomic_RNA.
DR   EMBL; AY463059; AAP82978.2; -; Genomic_RNA.
DR   EMBL; AY269391; AAP04003.1; -; Genomic_RNA.
DR   EMBL; AY268049; AAP04587.1; -; Genomic_RNA.
DR   PDB; 1O5S; Model; -; A=4745-5301.
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; 1SXF; Model; -; A=4765-5244.
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; 2G1F; Model; -; A/B=5302-5877.
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=4231-4378.
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=4231-4378.
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; 2H85; X-ray; 2.60 A; A=6429-6774.
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; 2JZD; NMR; -; A=1345-1469.
DR   PDB; 2JZE; NMR; -; A=1345-1469.
DR   PDB; 2JZF; NMR; -; A=1331-1469.
DR   PDB; 2K87; NMR; -; A=1884-1998.
DR   PDB; 2OP9; X-ray; 1.80 A; A/B=3241-3541.
DR   PDB; 2OZK; X-ray; 2.90 A; A/B/C/D=6430-6775.
DR   PDB; 2PWX; X-ray; 2.50 A; A=3241-3546.
DR   PDB; 2Q6G; X-ray; 2.50 A; A/B=3241-3546.
DR   PDB; 2QC2; X-ray; 2.70 A; A/B=3241-3546.
DR   PDB; 2QCY; X-ray; 1.75 A; A=3241-3546.
DR   PDB; 2QIQ; X-ray; 1.90 A; A=3242-3541.
DR   PDB; 2RHB; X-ray; 2.80 A; A/B/C/D/E/F=6430-6775.
DR   PDB; 2RNK; NMR; -; A=1331-1469.
DR   PDB; 2V6N; X-ray; 1.98 A; A=3241-3546.
DR   PDB; 2VJ1; X-ray; 2.25 A; A/B=3242-3544.
DR   PDB; 2XYQ; X-ray; 2.00 A; A=6776-7065, B=4240-4361.
DR   PDB; 2XYR; X-ray; 2.50 A; A=6776-7067, B=4240-4361.
DR   PDB; 2XYV; X-ray; 2.06 A; A=6776-7067, B=4240-4361.
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; 2Z94; X-ray; 1.78 A; A=3241-3546.
DR   PDB; 2Z9G; X-ray; 1.86 A; A=3241-3546.
DR   PDB; 2Z9J; X-ray; 1.95 A; A/B=3241-3546.
DR   PDB; 2Z9K; X-ray; 1.85 A; A/B=3241-3546.
DR   PDB; 2Z9L; X-ray; 2.10 A; A/B=3241-3546.
DR   PDB; 3D62; X-ray; 2.70 A; A=3243-3541.
DR   PDB; 3E9S; X-ray; 2.50 A; A=1541-1855.
DR   PDB; 3EBN; X-ray; 2.40 A; A/B/C/D=3429-3546.
DR   PDB; 3R24; X-ray; 2.00 A; A=6776-7073, B=4240-4382.
DR   PDB; 4TWW; X-ray; 2.42 A; A/B=3241-3546.
DR   PDB; 4TWY; X-ray; 1.60 A; A=3241-3546.
DR   PDB; 4WY3; X-ray; 1.89 A; A=3241-3546.
DR   PDB; 4ZUH; X-ray; 2.39 A; C=3235-3245.
DR   PDB; 5B6O; X-ray; 2.20 A; A/B=3241-3556.
DR   PDB; 5C5N; X-ray; 1.69 A; A=3241-3546.
DR   PDB; 5C5O; X-ray; 1.50 A; A/B=3241-3546.
DR   PDB; 5C8S; X-ray; 3.33 A; A/C=4231-4369, B/D=5903-6429.
DR   PDB; 5C8T; X-ray; 3.20 A; A/C=4231-4369, B/D=5903-6429.
DR   PDB; 5C8U; X-ray; 3.40 A; A/C=4231-4369, B/D=5903-6429.
DR   PDB; 5E6J; X-ray; 2.85 A; A/D=1541-1856.
DR   PDB; 5F22; X-ray; 2.15 A; B=3989-4117.
DR   PDB; 5N19; X-ray; 1.62 A; A=3241-3546.
DR   PDB; 5N5O; X-ray; 2.00 A; A=3241-3546.
DR   PDB; 5NFY; X-ray; 3.38 A; M/N/O/P=4231-4361.
DR   PDB; 6JYT; X-ray; 2.80 A; A/B=5302-5902.
DR   PDB; 6NUR; EM; 3.10 A; A=4370-5300, C=3837-3919.
DR   PDB; 6NUS; EM; 3.50 A; A=4370-5300.
DR   PDBsum; 1O5S; -.
DR   PDBsum; 1P76; -.
DR   PDBsum; 1P9T; -.
DR   PDBsum; 1PA5; -.
DR   PDBsum; 1PUK; -.
DR   PDBsum; 1Q1X; -.
DR   PDBsum; 1Q2W; -.
DR   PDBsum; 1QZ8; -.
DR   PDBsum; 1SXF; -.
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; 2G1F; -.
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; 2H85; -.
DR   PDBsum; 2HOB; -.
DR   PDBsum; 2HSX; -.
DR   PDBsum; 2IDY; -.
DR   PDBsum; 2JZD; -.
DR   PDBsum; 2JZE; -.
DR   PDBsum; 2JZF; -.
DR   PDBsum; 2K87; -.
DR   PDBsum; 2OP9; -.
DR   PDBsum; 2OZK; -.
DR   PDBsum; 2PWX; -.
DR   PDBsum; 2Q6G; -.
DR   PDBsum; 2QC2; -.
DR   PDBsum; 2QCY; -.
DR   PDBsum; 2QIQ; -.
DR   PDBsum; 2RHB; -.
DR   PDBsum; 2RNK; -.
DR   PDBsum; 2V6N; -.
DR   PDBsum; 2VJ1; -.
DR   PDBsum; 2XYQ; -.
DR   PDBsum; 2XYR; -.
DR   PDBsum; 2XYV; -.
DR   PDBsum; 2Z3C; -.
DR   PDBsum; 2Z3D; -.
DR   PDBsum; 2Z3E; -.
DR   PDBsum; 2Z94; -.
DR   PDBsum; 2Z9G; -.
DR   PDBsum; 2Z9J; -.
DR   PDBsum; 2Z9K; -.
DR   PDBsum; 2Z9L; -.
DR   PDBsum; 3D62; -.
DR   PDBsum; 3E9S; -.
DR   PDBsum; 3EBN; -.
DR   PDBsum; 3R24; -.
DR   PDBsum; 4TWW; -.
DR   PDBsum; 4TWY; -.
DR   PDBsum; 4WY3; -.
DR   PDBsum; 4ZUH; -.
DR   PDBsum; 5B6O; -.
DR   PDBsum; 5C5N; -.
DR   PDBsum; 5C5O; -.
DR   PDBsum; 5C8S; -.
DR   PDBsum; 5C8T; -.
DR   PDBsum; 5C8U; -.
DR   PDBsum; 5E6J; -.
DR   PDBsum; 5F22; -.
DR   PDBsum; 5N19; -.
DR   PDBsum; 5N5O; -.
DR   PDBsum; 5NFY; -.
DR   PDBsum; 6JYT; -.
DR   PDBsum; 6NUR; -.
DR   PDBsum; 6NUS; -.
DR   SMR; P0C6X7; -.
DR   BioGRID; 4383938; 1.
DR   BioGRID; 4383939; 9.
DR   BioGRID; 4383940; 14.
DR   BioGRID; 4383941; 17.
DR   BioGRID; 4383942; 4.
DR   BioGRID; 4383943; 16.
DR   BioGRID; 4383944; 4.
DR   BioGRID; 4383945; 17.
DR   BioGRID; 4383946; 23.
DR   BioGRID; 4383947; 12.
DR   BioGRID; 4383948; 5.
DR   BioGRID; 4383949; 18.
DR   BioGRID; 4383950; 14.
DR   BioGRID; 4383951; 7.
DR   BioGRID; 4383952; 5.
DR   BioGRID; 4383953; 4.
DR   ComplexPortal; CPX-5706; SARS-CoV main protease complex.
DR   ComplexPortal; CPX-5707; SARS-CoV 3'-5' exoribonuclease proof-reading complex.
DR   ComplexPortal; CPX-5709; SARS-CoV NSP10-NSP16 2'-O-methyltransferase complex.
DR   ComplexPortal; CPX-5710; SARS-CoV primase complex.
DR   ComplexPortal; CPX-5711; SARS-CoV NSP15 complex.
DR   ComplexPortal; CPX-5717; SARS-CoV polymerase complex.
DR   ComplexPortal; CPX-5719; SARS-CoV NSP9 complex.
DR   ComplexPortal; CPX-5721; SARS-CoV NSP3-NSP4-NSP6 complex.
DR   IntAct; P0C6X7; 98.
DR   MINT; P0C6X7; -.
DR   BindingDB; P0C6X7; -.
DR   ChEMBL; CHEMBL5118; -.
DR   DrugBank; DB07620; 2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE.
DR   DrugBank; DB08748; 4-(Dimethylamino)benzoic acid.
DR   DrugBank; DB08656; 5-amino-2-methyl-N-[(1R)-1-naphthalen-1-ylethyl]benzamide.
DR   DrugBank; DB07293; benzyl (2-oxopropyl)carbamate.
DR   DrugBank; DB08732; NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE.
DR   DrugBank; DB14761; Remdesivir.
DR   DrugBank; DB07743; S-[5-(TRIFLUOROMETHYL)-4H-1,2,4-TRIAZOL-3-YL] 5-(PHENYLETHYNYL)FURAN-2-CARBOTHIOATE.
DR   DrugCentral; P0C6X7; -.
DR   PRIDE; P0C6X7; -.
DR   BRENDA; 2.7.7.48; 7599.
DR   BRENDA; 3.4.22.B14; 7599.
DR   BRENDA; 3.6.4.12; 7599.
DR   SABIO-RK; P0C6X7; -.
DR   EvolutionaryTrace; P0C6X7; -.
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:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
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:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
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:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0039519; P:modulation by virus of host autophagy; IDA:UniProtKB.
DR   GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR   GO; GO:2000158; P:positive regulation of ubiquitin-specific protease activity; IDA:UniProtKB.
DR   GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
DR   GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:UniProtKB.
DR   GO; GO:0039548; P:suppression by virus of host IRF3 activity; IDA:UniProtKB.
DR   GO; GO:0039579; P:suppression by virus of host ISG15 activity; IDA:UniProtKB.
DR   GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0039604; P:suppression by virus of host translation; IDA:UniProtKB.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0001172; P:transcription, RNA-templated; IDA:UniProtKB.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019083; P:viral transcription; IMP:CACAO.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 1.10.150.420; -; 1.
DR   Gene3D; 1.10.1840.10; -; 1.
DR   Gene3D; 1.10.8.1190; -; 1.
DR   Gene3D; 1.10.8.370; -; 1.
DR   Gene3D; 2.20.25.360; -; 1.
DR   Gene3D; 2.30.30.590; -; 1.
DR   Gene3D; 2.40.10.10; -; 2.
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; 3.40.220.10; -; 1.
DR   Gene3D; 3.40.220.20; -; 1.
DR   Gene3D; 3.40.220.30; -; 1.
DR   Gene3D; 3.40.50.11020; -; 1.
DR   Gene3D; 3.40.50.11580; -; 1.
DR   Gene3D; 3.90.70.90; -; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR027352; CV_ZBD.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR041679; DNA2/NAM7-like_AAA.
DR   InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR   InterPro; IPR037227; EndoU-like.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR042570; NAR_sf.
DR   InterPro; IPR036333; NSP10_sf_CoV.
DR   InterPro; IPR009466; NSP11_CoV.
DR   InterPro; IPR043174; NSP15_middle_sf.
DR   InterPro; IPR042515; NSP15_N_CoV.
DR   InterPro; IPR009461; NSP16_CoV-like.
DR   InterPro; IPR021590; NSP1_bCoV.
DR   InterPro; IPR038030; NSP1_sf_bCoV.
DR   InterPro; IPR024375; NSP3_bCoV.
DR   InterPro; IPR024358; NSP3_N_bCoV.
DR   InterPro; IPR032592; NSP3_NAR_bCoV.
DR   InterPro; IPR038166; NSP3_PL2pro_sf_CoV.
DR   InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR   InterPro; IPR043478; NSP3_SUD-N_bCoV.
DR   InterPro; IPR038083; NSP3A-like.
DR   InterPro; IPR032505; NSP4_C_CoV.
DR   InterPro; IPR038123; NSP4_C_sf_CoV.
DR   InterPro; IPR014828; NSP7_CoV.
DR   InterPro; IPR037204; NSP7_sf_CoV.
DR   InterPro; IPR014829; NSP8_CoV-like.
DR   InterPro; IPR037230; NSP8_sf_CoV.
DR   InterPro; IPR014822; NSP9_CoV.
DR   InterPro; IPR036499; NSP9_sf_CoV.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013016; Peptidase_C16_CoV.
DR   InterPro; IPR008740; Peptidase_C30_CoV.
DR   InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR043177; PLpro_N_sf_CoV.
DR   InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR   InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR009469; RNA_pol_N_coronovir.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF16348; Corona_NSP4_C; 1.
DR   Pfam; PF06478; Corona_RPol_N; 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; PF06471; NSP11; 1.
DR   Pfam; PF06460; NSP16; 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; SSF142877; SSF142877; 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   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51653; CV_ZBD; 1.
DR   PROSITE; PS51442; M_PRO; 1.
DR   PROSITE; PS51154; MACRO; 1.
DR   PROSITE; PS51124; PEPTIDASE_C16; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Decay of host mRNAs by virus; Endonuclease;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
KW   Host cytoplasm; 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 ISG15 by virus; Inhibition of host NF-kappa-B by virus;
KW   Membrane; Metal-binding; Methyltransferase;
KW   Modulation of host ubiquitin pathway by viral deubiquitinase;
KW   Modulation of host ubiquitin pathway by virus; Nuclease;
KW   Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW   Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW   Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..180
FT                   /note="Host translation inhibitor nsp1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037309"
FT   CHAIN           181..818
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037310"
FT   CHAIN           819..2740
FT                   /note="Non-structural protein 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037311"
FT   CHAIN           2741..3240
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283841"
FT   CHAIN           3241..3546
FT                   /note="3C-like proteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037312"
FT   CHAIN           3547..3836
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037313"
FT   CHAIN           3837..3919
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037314"
FT   CHAIN           3920..4117
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037315"
FT   CHAIN           4118..4230
FT                   /note="Non-structural protein 9"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037316"
FT   CHAIN           4231..4369
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037317"
FT   CHAIN           4370..5301
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037318"
FT   CHAIN           5302..5902
FT                   /note="Helicase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037319"
FT   CHAIN           5903..6429
FT                   /note="Proofreading exoribonuclease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037320"
FT   CHAIN           6430..6775
FT                   /note="Uridylate-specific endoribonuclease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037321"
FT   CHAIN           6776..7073
FT                   /note="2'-O-methyltransferase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037322"
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..7073
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   DOMAIN          4981..5143
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          5302..5385
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   DOMAIN          5558..5739
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          5740..5909
FT                   /note="(+)RNA virus helicase C-terminal"
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   NP_BIND         5583..5590
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
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   METAL           5306
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5309
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5317
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5320
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5327
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5330
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5334
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5340
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5351
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5356
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5373
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   METAL           5376
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
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:0000269|PubMed:32083638"
FT   SITE            3919..3920
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000269|PubMed:32083638"
FT   SITE            4117..4118
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000269|PubMed:32083638"
FT   SITE            4230..4231
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000269|PubMed:32083638"
FT   SITE            4369..4370
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            5301..5302
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            5902..5903
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6429..6430
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6775..6776
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   VARIANT         4411
FT                   /note="V -> S (in strain: Isolate HKU-39849)"
FT   VARIANT         4459
FT                   /note="V -> I (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         4592
FT                   /note="V -> E (in strain: Isolate ZJ01)"
FT   VARIANT         4910
FT                   /note="Q -> L (in strain: Isolate ZJ01)"
FT   VARIANT         5112
FT                   /note="D -> G (in strain: Isolate SZ3)"
FT   VARIANT         5131
FT                   /note="A -> G (in strain: Isolate Taiwan)"
FT   VARIANT         5134..5135
FT                   /note="CY -> VL (in strain: Isolate Taiwan)"
FT   VARIANT         5623
FT                   /note="L -> S (in strain: Isolate GD01)"
FT   VARIANT         5720
FT                   /note="P -> S (in strain: Isolate GZ50 and Isolate
FT                   SIN2500)"
FT   VARIANT         5744
FT                   /note="R -> C (in strain: Isolate ZJ01)"
FT   VARIANT         5767
FT                   /note="D -> E (in strain: Isolate CUHK-W1, Isolate BJ01,
FT                   Isolate BJ02, Isolate BJ03, Isolate BJ04, Isolate SIN2500,
FT                   Isolate GD01, Isolate GZ50, Isolate SZ3, Isolate SZ16 and
FT                   Isolate Shanghai QXC1)"
FT   VARIANT         6274
FT                   /note="T -> I (in strain: Isolate FRA, Isolate Frankfurt-1
FT                   Isolate SIN2677, Isolate SIN2679 and Isolate SIN2748)"
FT   VARIANT         6474
FT                   /note="N -> S (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         6700
FT                   /note="M -> I (in strain: Isolate BJ03)"
FT   VARIANT         6721
FT                   /note="C -> R (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         6729
FT                   /note="D -> N (in strain: Isolate GD01)"
FT   VARIANT         6840
FT                   /note="M -> L (in strain: Isolate BJ02)"
FT   VARIANT         6862
FT                   /note="Q -> P (in strain: Isolate BJ04)"
FT   VARIANT         6877
FT                   /note="D -> E (in strain: Isolate GD01)"
FT   VARIANT         6910
FT                   /note="R -> K (in strain: Isolate SZ3 and Isolate SZ16)"
FT   VARIANT         6937
FT                   /note="A -> P (in strain: Isolate BJ03)"
FT   VARIANT         6992
FT                   /note="E -> D (in strain: Isolate BJ04)"
FT   VARIANT         7008
FT                   /note="N -> K (in strain: Isolate GD01)"
FT   VARIANT         7024
FT                   /note="K -> Q (in strain: Isolate BJ04)"
FT   MUTAGEN         4217
FT                   /note="G->E: Complete loss of nsp9 dimerization."
FT                   /evidence="ECO:0000269|PubMed:19153232"
FT   MUTAGEN         4221
FT                   /note="G->E: Complete loss of nsp9 dimerization."
FT                   /evidence="ECO:0000269|PubMed:19153232"
FT   STRAND          14..20
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   TURN            23..25
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   HELIX           35..48
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   STRAND          51..54
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   HELIX           61..63
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   STRAND          68..72
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   STRAND          87..93
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   TURN            95..98
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   STRAND          99..102
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   STRAND          105..109
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   STRAND          116..123
FT                   /evidence="ECO:0000244|PDB:2GDT"
FT   STRAND          827..829
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   TURN            831..833
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   STRAND          839..841
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   STRAND          848..851
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   TURN            852..856
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   STRAND          860..862
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   TURN            869..871
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   HELIX           872..882
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   HELIX           888..894
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   HELIX           898..901
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   STRAND          907..909
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   STRAND          911..915
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   STRAND          918..920
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   STRAND          922..926
FT                   /evidence="ECO:0000244|PDB:2GRI"
FT   STRAND          1013..1021
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1023..1030
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   STRAND          1033..1038
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1048..1056
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   TURN            1057..1059
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1060..1072
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   STRAND          1080..1084
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   TURN            1086..1088
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   STRAND          1090..1095
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1100..1102
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1108..1114
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1115..1118
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   STRAND          1119..1124
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1130..1132
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1136..1146
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   STRAND          1149..1156
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   HELIX           1158..1168
FT                   /evidence="ECO:0000244|PDB:2ACF"
FT   STRAND          1345..1347
FT                   /evidence="ECO:0000244|PDB:2JZF"
FT   HELIX           1351..1361
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   STRAND          1364..1368
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   HELIX           1372..1381
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   STRAND          1389..1401
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   HELIX           1407..1417
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   STRAND          1421..1424
FT                   /evidence="ECO:0000244|PDB:2JZF"
FT   STRAND          1426..1428
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   HELIX           1429..1431
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   HELIX           1435..1442
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   STRAND          1449..1452
FT                   /evidence="ECO:0000244|PDB:2JZF"
FT   HELIX           1457..1467
FT                   /evidence="ECO:0000244|PDB:2JZD"
FT   STRAND          1544..1555
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1557..1562
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1567..1571
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1572..1576
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1582..1584
FT                   /evidence="ECO:0000244|PDB:5E6J"
FT   HELIX           1588..1590
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1594..1597
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1602..1612
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1619..1630
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1639..1642
FT                   /evidence="ECO:0000244|PDB:5E6J"
FT   TURN            1648..1650
FT                   /evidence="ECO:0000244|PDB:5E6J"
FT   HELIX           1651..1661
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1667..1669
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1670..1680
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1685..1694
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1705..1713
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1722..1728
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1730..1732
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1734..1740
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1742..1745
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1746..1749
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1753..1758
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1760..1763
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1765..1785
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1790..1793
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   HELIX           1795..1797
FT                   /evidence="ECO:0000244|PDB:5E6J"
FT   STRAND          1799..1807
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1810..1826
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1829..1834
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1836..1846
FT                   /evidence="ECO:0000244|PDB:3E9S"
FT   STRAND          1904..1911
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   HELIX           1912..1921
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   STRAND          1929..1936
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   STRAND          1942..1948
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   HELIX           1949..1951
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   HELIX           1954..1956
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   STRAND          1963..1966
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   STRAND          1969..1971
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   HELIX           1977..1990
FT                   /evidence="ECO:0000244|PDB:2K87"
FT   HELIX           3251..3254
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3257..3262
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3265..3272
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3275..3279
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3280..3283
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3286..3290
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3294..3299
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3303..3305
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3307..3310
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3313..3315
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3317..3323
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3326..3333
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3340..3343
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3351..3358
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3361..3369
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3379..3381
FT                   /evidence="ECO:0000244|PDB:2QCY"
FT   STRAND          3388..3393
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3396..3406
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   TURN            3408..3410
FT                   /evidence="ECO:0000244|PDB:1UJ1"
FT   STRAND          3412..3415
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3421..3424
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3427..3430
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3441..3453
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   TURN            3458..3460
FT                   /evidence="ECO:0000244|PDB:3EBN"
FT   HELIX           3467..3476
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3477..3479
FT                   /evidence="ECO:0000244|PDB:1Z1J"
FT   HELIX           3484..3489
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3491..3497
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3501..3514
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   STRAND          3516..3518
FT                   /evidence="ECO:0000244|PDB:2BX3"
FT   STRAND          3521..3523
FT                   /evidence="ECO:0000244|PDB:1UK4"
FT   STRAND          3524..3526
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   HELIX           3533..3539
FT                   /evidence="ECO:0000244|PDB:5C5O"
FT   TURN            3540..3542
FT                   /evidence="ECO:0000244|PDB:2QC2"
FT   HELIX           3837..3855
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           3858..3860
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           3862..3876
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   STRAND          3878..3880
FT                   /evidence="ECO:0000244|PDB:1YSY"
FT   HELIX           3881..3905
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           3906..3909
FT                   /evidence="ECO:0000244|PDB:1YSY"
FT   TURN            3910..3912
FT                   /evidence="ECO:0000244|PDB:1YSY"
FT   HELIX           3913..3916
FT                   /evidence="ECO:0000244|PDB:1YSY"
FT   HELIX           3922..3924
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           3929..3946
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           3951..3956
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   TURN            3959..3963
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   TURN            3970..3972
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           3973..3987
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           3996..4017
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           4020..4030
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   STRAND          4034..4037
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   STRAND          4046..4051
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           4054..4060
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   STRAND          4065..4068
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   STRAND          4071..4079
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           4088..4090
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   TURN            4093..4095
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   HELIX           4096..4098
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   STRAND          4103..4109
FT                   /evidence="ECO:0000244|PDB:2AHM"
FT   STRAND          4120..4125
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4127..4131
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4134..4137
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4145..4150
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4153..4155
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4157..4164
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4170..4174
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4181..4186
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4191..4194
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   STRAND          4201..4208
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   HELIX           4213..4222
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   HELIX           4224..4227
FT                   /evidence="ECO:0000244|PDB:1UW7"
FT   HELIX           4238..4240
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           4243..4248
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          4250..4252
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           4253..4262
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          4284..4288
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          4295..4300
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           4301..4303
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           4305..4308
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          4314..4318
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          4325..4330
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           4331..4333
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           4337..4343
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   TURN            4348..4350
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          4351..4353
FT                   /evidence="ECO:0000244|PDB:5NFY"
FT   TURN            4354..4357
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          4490..4492
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4493..4501
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4505..4507
FT                   /evidence="ECO:0000244|PDB:6NUS"
FT   HELIX           4509..4517
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4523..4527
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            4529..4532
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4534..4537
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4540..4544
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4545..4547
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4548..4567
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4570..4573
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4576..4578
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4600..4602
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4604..4616
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            4617..4620
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4621..4624
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4645..4655
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4667..4669
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4671..4673
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4674..4686
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4687..4689
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4692..4694
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4695..4704
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4707..4717
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            4718..4720
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4721..4724
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4731..4734
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4737..4744
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4748..4751
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4754..4759
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4766..4770
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4786..4793
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            4794..4798
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4818..4822
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4823..4827
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4835..4847
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            4848..4851
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4859..4861
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4875..4877
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4881..4885
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4890..4899
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            4900..4902
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4908..4913
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4918..4920
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4925..4928
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4931..4949
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4953..4956
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            4963..4965
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4966..4975
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          4979..4985
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4991..4994
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           4997..5007
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5008..5010
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5012..5014
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5017..5031
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5035..5038
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5041..5044
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5053..5055
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5056..5077
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5081..5083
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5087..5097
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            5098..5100
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5108..5121
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5122..5127
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5130..5136
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5137..5140
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            5141..5143
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5148..5158
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5165..5167
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5169..5171
FT                   /evidence="ECO:0000244|PDB:6NUS"
FT   STRAND          5184..5190
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5192..5200
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5203..5211
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   STRAND          5217..5219
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5221..5234
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5236..5240
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5244..5263
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5278..5282
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   HELIX           5283..5285
FT                   /evidence="ECO:0000244|PDB:6NUR"
FT   TURN            5307..5309
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5312..5314
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5316..5320
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5328..5335
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5343..5349
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5361..5363
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5368..5372
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5374..5376
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5382..5386
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5393..5397
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5404..5412
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5418..5426
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5429..5446
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5447..5449
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5453..5457
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5461..5468
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5483..5488
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5493..5503
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5509..5516
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5525..5528
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5561..5566
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5567..5570
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5572..5575
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5576..5581
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5589..5599
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5605..5610
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5612..5616
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5617..5622
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5623..5626
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5630..5633
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5640..5642
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5647..5649
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5655..5660
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5661..5663
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5666..5668
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5670..5674
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5677..5679
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5682..5691
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5695..5700
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5720..5722
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5725..5730
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5743..5745
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5747..5750
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5751..5754
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5756..5759
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5791..5793
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5794..5796
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5797..5800
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5815..5818
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5819..5827
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5834..5836
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5843..5848
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   TURN            5854..5856
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5859..5866
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5873..5876
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   HELIX           5882..5884
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5893..5895
FT                   /evidence="ECO:0000244|PDB:6JYT"
FT   STRAND          5922..5924
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          5928..5931
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           5933..5935
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          5955..5957
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           5978..5983
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          5986..5997
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6000..6002
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6006..6016
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6018..6020
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6024..6028
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6033..6037
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6046..6053
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6054..6057
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6061..6076
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   TURN            6077..6079
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6084..6089
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6091..6100
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6112..6115
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6118..6120
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   TURN            6121..6124
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6125..6127
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   TURN            6129..6131
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6137..6140
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6142..6145
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6146..6149
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6155..6162
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6164..6166
FT                   /evidence="ECO:0000244|PDB:5C8U"
FT   HELIX           6172..6188
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6204..6226
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6229..6235
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6242..6245
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6247..6256
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6263..6267
FT                   /evidence="ECO:0000244|PDB:5C8S"
FT   HELIX           6272..6275
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   TURN            6276..6278
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6281..6288
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6296..6303
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6312..6314
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6320..6322
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6324..6326
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6328..6330
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6335..6338
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6341..6343
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6373..6376
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6381..6383
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6387..6405
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   STRAND          6408..6412
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6419..6425
FT                   /evidence="ECO:0000244|PDB:5C8T"
FT   HELIX           6431..6441
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6453..6456
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6459..6464
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6467..6473
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6476..6478
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   HELIX           6480..6488
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6493..6495
FT                   /evidence="ECO:0000244|PDB:2OZK"
FT   HELIX           6498..6503
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6508..6513
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   TURN            6517..6520
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6521..6530
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   TURN            6532..6534
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6535..6539
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   HELIX           6543..6545
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6550..6553
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   HELIX           6559..6565
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6567..6575
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6589..6591
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6594..6596
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6599..6601
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6606..6611
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6614..6616
FT                   /evidence="ECO:0000244|PDB:2RHB"
FT   HELIX           6629..6631
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   HELIX           6637..6644
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   HELIX           6647..6653
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   HELIX           6661..6664
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6670..6673
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6677..6679
FT                   /evidence="ECO:0000244|PDB:2OZK"
FT   HELIX           6680..6689
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6692..6698
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6703..6711
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   TURN            6712..6714
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6717..6724
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   HELIX           6728..6736
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6741..6751
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6754..6763
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   STRAND          6766..6772
FT                   /evidence="ECO:0000244|PDB:2H85"
FT   HELIX           6777..6780
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6781..6785
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           6788..6791
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           6817..6829
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6841..6846
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           6855..6863
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6869..6876
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6881..6888
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           6890..6892
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6893..6897
FT                   /evidence="ECO:0000244|PDB:3R24"
FT   STRAND          6899..6904
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           6924..6935
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6936..6946
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6948..6950
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           6953..6959
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6962..6970
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           6971..6973
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          6979..6986
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           6996..7009
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           7017..7020
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          7033..7035
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           7039..7041
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   HELIX           7044..7051
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          7055..7057
FT                   /evidence="ECO:0000244|PDB:2XYQ"
FT   STRAND          7065..7067
FT                   /evidence="ECO:0000244|PDB:3R24"
SQ   SEQUENCE   7073 AA;  790248 MW;  E6504CAFDC36BC09 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 ADASTFLNRV
     CGVSAARLTP CGTGTSTDVV YRAFDIYNEK VAGFAKFLKT NCCRFQEKDE EGNLLDSYFV
     VKRHTMSNYQ HEETIYNLVK DCPAVAVHDF FKFRVDGDMV PHISRQRLTK YTMADLVYAL
     RHFDEGNCDT LKEILVTYNC CDDDYFNKKD WYDFVENPDI LRVYANLGER VRQSLLKTVQ
     FCDAMRDAGI VGVLTLDNQD LNGNWYDFGD FVQVAPGCGV PIVDSYYSLL MPILTLTRAL
     AAESHMDADL AKPLIKWDLL KYDFTEERLC LFDRYFKYWD QTYHPNCINC LDDRCILHCA
     NFNVLFSTVF PPTSFGPLVR KIFVDGVPFV VSTGYHFREL GVVHNQDVNL HSSRLSFKEL
     LVYAADPAMH AASGNLLLDK RTTCFSVAAL TNNVAFQTVK PGNFNKDFYD FAVSKGFFKE
     GSSVELKHFF FAQDGNAAIS DYDYYRYNLP TMCDIRQLLF VVEVVDKYFD CYDGGCINAN
     QVIVNNLDKS AGFPFNKWGK ARLYYDSMSY EDQDALFAYT KRNVIPTITQ MNLKYAISAK
     NRARTVAGVS ICSTMTNRQF HQKLLKSIAA TRGATVVIGT SKFYGGWHNM LKTVYSDVET
     PHLMGWDYPK CDRAMPNMLR IMASLVLARK HNTCCNLSHR FYRLANECAQ VLSEMVMCGG
     SLYVKPGGTS SGDATTAYAN SVFNICQAVT ANVNALLSTD GNKIADKYVR NLQHRLYECL
     YRNRDVDHEF VDEFYAYLRK HFSMMILSDD AVVCYNSNYA AQGLVASIKN FKAVLYYQNN
     VFMSEAKCWT ETDLTKGPHE FCSQHTMLVK QGDDYVYLPY PDPSRILGAG CFVDDIVKTD
     GTLMIERFVS LAIDAYPLTK HPNQEYADVF HLYLQYIRKL HDELTGHMLD MYSVMLTNDN
     TSRYWEPEFY EAMYTPHTVL QAVGACVLCN SQTSLRCGAC IRRPFLCCKC CYDHVISTSH
     KLVLSVNPYV CNAPGCDVTD VTQLYLGGMS YYCKSHKPPI SFPLCANGQV FGLYKNTCVG
     SDNVTDFNAI ATCDWTNAGD YILANTCTER LKLFAAETLK ATEETFKLSY GIATVREVLS
     DRELHLSWEV GKPRPPLNRN YVFTGYRVTK NSKVQIGEYT FEKGDYGDAV VYRGTTTYKL
     NVGDYFVLTS HTVMPLSAPT LVPQEHYVRI TGLYPTLNIS DEFSSNVANY QKVGMQKYST
     LQGPPGTGKS HFAIGLALYY PSARIVYTAC SHAAVDALCE KALKYLPIDK CSRIIPARAR
     VECFDKFKVN STLEQYVFCT VNALPETTAD IVVFDEISMA TNYDLSVVNA RLRAKHYVYI
     GDPAQLPAPR TLLTKGTLEP EYFNSVCRLM KTIGPDMFLG TCRRCPAEIV DTVSALVYDN
     KLKAHKDKSA QCFKMFYKGV ITHDVSSAIN RPQIGVVREF LTRNPAWRKA VFISPYNSQN
     AVASKILGLP TQTVDSSQGS EYDYVIFTQT TETAHSCNVN RFNVAITRAK IGILCIMSDR
     DLYDKLQFTS LEIPRRNVAT LQAENVTGLF KDCSKIITGL HPTQAPTHLS VDIKFKTEGL
     CVDIPGIPKD MTYRRLISMM GFKMNYQVNG YPNMFITREE AIRHVRAWIG FDVEGCHATR
     DAVGTNLPLQ LGFSTGVNLV AVPTGYVDTE NNTEFTRVNA KPPPGDQFKH LIPLMYKGLP
     WNVVRIKIVQ MLSDTLKGLS DRVVFVLWAH GFELTSMKYF VKIGPERTCC LCDKRATCFS
     TSSDTYACWN HSVGFDYVYN PFMIDVQQWG FTGNLQSNHD QHCQVHGNAH VASCDAIMTR
     CLAVHECFVK RVDWSVEYPI IGDELRVNSA CRKVQHMVVK SALLADKFPV LHDIGNPKAI
     KCVPQAEVEW KFYDAQPCSD KAYKIEELFY SYATHHDKFT DGVCLFWNCN VDRYPANAIV
     CRFDTRVLSN LNLPGCDGGS LYVNKHAFHT PAFDKSAFTN LKQLPFFYYS DSPCESHGKQ
     VVSDIDYVPL KSATCITRCN LGGAVCRHHA NEYRQYLDAY NMMISAGFSL WIYKQFDTYN
     LWNTFTRLQS LENVAYNVVN KGHFDGHAGE APVSIINNAV YTKVDGIDVE IFENKTTLPV
     NVAFELWAKR NIKPVPEIKI LNNLGVDIAA NTVIWDYKRE APAHVSTIGV CTMTDIAKKP
     TESACSSLTV LFDGRVEGQV DLFRNARNGV LITEGSVKGL TPSKGPAQAS VNGVTLIGES
     VKTQFNYFKK VDGIIQQLPE TYFTQSRDLE DFKPRSQMET DFLELAMDEF IQRYKLEGYA
     FEHIVYGDFS HGQLGGLHLM IGLAKRSQDS PLKLEDFIPM DSTVKNYFIT DAQTGSSKCV
     CSVIDLLLDD FVEIIKSQDL SVISKVVKVT IDYAEISFML WCKDGHVETF YPKLQASQAW
     QPGVAMPNLY KMQRMLLEKC DLQNYGENAV IPKGIMMNVA KYTQLCQYLN TLTLAVPYNM
     RVIHFGAGSD KGVAPGTAVL RQWLPTGTLL VDSDLNDFVS DADSTLIGDC ATVHTANKWD
     LIISDMYDPR TKHVTKENDS KEGFFTYLCG FIKQKLALGG SIAVKITEHS WNADLYKLMG
     HFSWWTAFVT NVNASSSEAF LIGANYLGKP KEQIDGYTMH ANYIFWRNTN PIQLSSYSLF
     DMSKFPLKLR GTAVMSLKEN QINDMIYSLL EKGRLIIREN NRVVVSSDIL VNN
//