R1AB_SARS
ID R1AB_SARS 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 03-AUG-2022, entry version 121.
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=Papain-like protease nsp3;
DE Short=PL-PRO;
DE EC=3.4.19.12 {ECO:0000269|PubMed:12917450, ECO:0000269|PubMed:17692280};
DE EC=3.4.22.- {ECO:0000269|PubMed:12917450, ECO:0000269|PubMed:16306590};
DE AltName: Full=Non-structural protein 3;
DE Short=nsp3;
DE AltName: Full=PL2-PRO;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE Contains:
DE RecName: Full=3C-like proteinase nsp5;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.69 {ECO:0000269|PubMed:12917450};
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 nsp12;
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 nsp13;
DE Short=Hel;
DE EC=3.6.4.12 {ECO:0000269|PubMed:22615777};
DE EC=3.6.4.13 {ECO:0000269|PubMed:22615777};
DE AltName: Full=Non-structural protein 13;
DE Short=nsp13;
DE Contains:
DE RecName: Full=Proofreading exoribonuclease nsp14 {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 {ECO:0000303|PubMed:20421945};
DE AltName: Full=Non-structural protein 14;
DE Short=nsp14;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease nsp15;
DE EC=4.6.1.- {ECO:0000269|PubMed:16828802};
DE AltName: Full=NendoU;
DE AltName: Full=Non-structural protein 15;
DE Short=nsp15;
DE Contains:
DE RecName: Full=2'-O-methyltransferase nsp16;
DE EC=2.1.1.57 {ECO:0000269|PubMed:22022266};
DE AltName: Full=Non-structural protein 16;
DE Short=nsp16;
GN Name=rep; ORFNames=1a-1b;
OS Severe acute respiratory syndrome coronavirus (SARS-CoV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC 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 NSP13).
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 CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1AB), CATALYTIC
RP ACTIVITY (3C-LIKE PROTEINASE NSP5), AND CATALYTIC ACTIVITY (PAPAIN-LIKE
RP PROTEASE NSP3).
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 NSP5), SUBUNIT (3C-LIKE PROTEINASE
RP NSP5), AND BIOPHYSICOCHEMICAL PROPERTIES (3C-LIKE PROTEINASE NSP5).
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 CLEAVAGE (ISOFORM 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 CLEAVAGE (ISOFORM 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 CATALYTIC ACTIVITY (PAPAIN-LIKE PROTEASE NSP3), FUNCTION (PAPAIN-LIKE
RP PROTEASE NSP3), PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1A),
RP COFACTOR (PAPAIN-LIKE PROTEASE NSP3), MUTAGENESIS OF CYS-1651; CYS-1688;
RP CYS-1729; CYS-1732; CYS-1764; CYS-1766 AND ASP-1826, AND ACTIVE SITE
RP (PAPAIN-LIKE PROTEASE NSP3).
RX PubMed=16306590; DOI=10.1128/jvi.79.24.15189-15198.2005;
RA Barretto N., Jukneliene D., Ratia K., Chen Z., Mesecar A.D., Baker S.C.;
RT "The papain-like protease of severe acute respiratory syndrome coronavirus
RT has deubiquitinating activity.";
RL J. Virol. 79:15189-15198(2005).
RN [29]
RP FUNCTION (3C-LIKE PROTEINASE NSP5).
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 [30]
RP SUBUNIT (3C-LIKE PROTEINASE NSP5).
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 [31]
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 [32]
RP FUNCTION (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15), MUTAGENESIS OF
RP HIS-6663, SUBUNIT (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15), COFACTOR
RP (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15), AND CATALYTIC ACTIVITY
RP (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15).
RX PubMed=16828802; DOI=10.1016/j.jmb.2006.06.021;
RA Bhardwaj K., Sun J., Holzenburg A., Guarino L.A., Kao C.C.;
RT "RNA recognition and cleavage by the SARS coronavirus endoribonuclease.";
RL J. Mol. Biol. 361:243-256(2006).
RN [33]
RP CHARACTERIZATION (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15).
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 [34]
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 [35]
RP FUNCTION (NON-STRUCTURAL PROTEIN 3), AND CATALYTIC ACTIVITY (PAPAIN-LIKE
RP PROTEASE NSP3).
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 [36]
RP SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4), AND TOPOLOGY
RP (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 [37]
RP INTERACTION WITH ORF6 PROTEIN (NON-STRUCTURAL PROTEIN 8), AND SUBCELLULAR
RP LOCATION (NON-STRUCTURAL PROTEIN 8).
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 [38]
RP FUNCTION (2'-O-METHYLTRANSFERASE NSP16).
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 [39]
RP INTERACTION WITH PROOFREADING EXORIBONUCLEASE NSP14 (NON-STRUCTURAL PROTEIN
RP 10), INTERACTION WITH 2'-O-METHYLTRANSFERASE NSP16 (NON-STRUCTURAL PROTEIN
RP 10), INTERACTION WITH NON-STRUCTURAL PROTEIN 10 (PROOFREADING
RP EXORIBONUCLEASE NSP14), AND INTERACTION WITH NON-STRUCTURAL PROTEIN 10
RP (2'-O-METHYLTRANSFERASE 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 [40]
RP TOPOLOGY (PAPAIN-LIKE PROTEASE NSP3), TOPOLOGY (NON-STRUCTURAL PROTEIN 4),
RP AND TOPOLOGY (NON-STRUCTURAL PROTEIN 6).
RX PubMed=18842706; DOI=10.1128/jvi.01219-08;
RA Oostra M., Hagemeijer M.C., van Gent M., Bekker C.P., te Lintelo E.G.,
RA Rottier P.J., de Haan C.A.;
RT "Topology and membrane anchoring of the coronavirus replication complex:
RT not all hydrophobic domains of nsp3 and nsp6 are membrane spanning.";
RL J. Virol. 82:12392-12405(2008).
RN [41]
RP FUNCTION (PAPAIN-LIKE PROTEASE NSP3).
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 [42]
RP FUNCTION (NON-STRUCTURAL PROTEIN 2), AND INTERACTION WITH HOST PHB AND PHB2
RP (NON-STRUCTURAL PROTEIN 2).
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 [43]
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 [44]
RP INTERACTION WITH HOST DDX1 (PROOFREADING EXORIBONUCLEASE NSP14).
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 [45]
RP FUNCTION (PROOFREADING EXORIBONUCLEASE NSP14), AND FUNCTION
RP (2'-O-METHYLTRANSFERASE NSP16).
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 [46]
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 [47]
RP INTERACTION WITH NON-STRUCTURAL PROTEIN 6 (NON-STRUCTURAL PROTEIN 4),
RP SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4), AND INTERACTION WITH
RP 3C-LIKE PROTEINASE NSP5 (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 [48]
RP FUNCTION (PROOFREADING EXORIBONUCLEASE NSP14).
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 [49]
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 [50]
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 [51]
RP FUNCTION (HELICASE NSP13), AND CATALYTIC ACTIVITY (HELICASE NSP13).
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 [52]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NSP12).
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 [53]
RP FUNCTION (NON-STRUCTURAL PROTEIN 10), FUNCTION (GUANINE-N7
RP METHYLTRANSFERASE), INTERACTION WITH NON-STRUCTURAL PROTEIN 14
RP (NON-STRUCTURAL PROTEIN 10), AND INTERACTION WITH NON-STRUCTURAL PROTEIN 10
RP (NON-STRUCTURAL PROTEIN 14).
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 [54]
RP FUNCTION (NON-STRUCTURAL PROTEIN 4), SUBCELLULAR LOCATION (NON-STRUCTURAL
RP PROTEIN 4), FUNCTION (PAPAIN-LIKE PROTEASE NSP3), AND FUNCTION
RP (NON-STRUCTURAL PROTEIN 6).
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 [55]
RP FUNCTION (PROOFREADING EXORIBONUCLEASE NSP14).
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 [56]
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 [57]
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 [58]
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 [59]
RP FUNCTION (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15).
RX PubMed=28158275; DOI=10.1371/journal.ppat.1006195;
RA Kindler E., Gil-Cruz C., Spanier J., Li Y., Wilhelm J., Rabouw H.H.,
RA Zuest R., Hwang M., V'kovski P., Stalder H., Marti S., Habjan M.,
RA Cervantes-Barragan L., Elliot R., Karl N., Gaughan C., van Kuppeveld F.J.,
RA Silverman R.H., Keller M., Ludewig B., Bergmann C.C., Ziebuhr J.,
RA Weiss S.R., Kalinke U., Thiel V.;
RT "Early endonuclease-mediated evasion of RNA sensing ensures efficient
RT coronavirus replication.";
RL PLoS Pathog. 13:e1006195-e1006195(2017).
RN [60]
RP FUNCTION (PROOFREADING EXORIBONUCLEASE NSP14), AND ACTIVITY REGULATION
RP (PROOFREADING EXORIBONUCLEASE NSP14).
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 [61]
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 [62]
RP PROTEOLYTIC CLEAVAGE (ISOFORM 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 [63]
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 [64]
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 [65]
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 [66]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230, INTERACTION WITH
RP NON-STRUCTURAL PROTEIN 9 (NON-STRUCTURAL PROTEIN 8), AND INTERACTION WITH
RP NON-STRUCTURAL PROTEIN 8 (NON-STRUCTURAL PROTEIN 9).
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 [67]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 3837-4117 AND 3920-4117,
RP INTERACTION WITH NON-STRUCTURAL PROTEIN 7 (NON-STRUCTURAL PROTEIN 8), AND
RP INTERACTION WITH NON-STRUCTURAL PROTEIN 8 (NON-STRUCTURAL PROTEIN 7).
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 [68]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1002-1176, AND FUNCTION (3C-LIKE
RP PROTEINASE NSP5).
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 [69]
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 [70]
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 [71]
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 [72]
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 [73]
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.
RN [74]
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 6429-6774 (URIDYLATE-SPECIFIC
RP ENDORIBONUCLEASE NSP15), FUNCTION (URIDYLATE-SPECIFIC ENDORIBONUCLEASE
RP NSP15), AND MUTAGENESIS OF HIS-6663.
RX PubMed=18045871; DOI=10.1074/jbc.m708375200;
RA Bhardwaj K., Palaninathan S., Alcantara J.M.O., Li Yi L., Guarino L.,
RA Sacchettini J.C., Kao C.C.;
RT "Structural and functional analyses of the severe acute respiratory
RT syndrome coronavirus endoribonuclease Nsp15.";
RL J. Biol. Chem. 283:3655-3664(2008).
RN [75]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4240-4382 (NON-STRUCTURAL PROTEIN
RP 10), X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6776-7073 (NON-STRUCTURAL
RP PROTEIN 10), FUNCTION (2'-O-METHYLTRANSFERASE NSP16), CATALYTIC ACTIVITY
RP (2'-O-METHYLTRANSFERASE NSP16), FUNCTION (NON-STRUCTURAL PROTEIN 10),
RP INTERACTION WITH NSP16 (NON-STRUCTURAL PROTEIN 10), INTERACTION WITH NSP10
RP (2'-O-METHYLTRANSFERASE NSP16), AND MUTAGENESIS OF 4306-TYR--ARG-4308 AND
RP 4313-HIS-PRO-4314.
RX PubMed=22022266; DOI=10.1371/journal.ppat.1002294;
RA Chen Y., Su C., Ke M., Jin X., Xu L., Zhang Z., Wu A., Sun Y., Yang Z.,
RA Tien P., Ahola T., Liang Y., Liu X., Guo D.;
RT "Biochemical and structural insights into the mechanisms of SARS
RT coronavirus RNA ribose 2'-O-methylation by nsp16/nsp10 protein complex.";
RL PLoS Pathog. 7:e1002294-e1002294(2011).
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 {ECO:0000305}.
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 (PubMed:19640993). Indeed, these two proteins play a role in
CC maintaining the functional integrity of the mitochondria and protecting
CC cells from various stresses (PubMed:19640993).
CC {ECO:0000269|PubMed:19640993}.
CC -!- FUNCTION: [Papain-like protease nsp3]: Responsible for the cleavages
CC located at the N-terminus of the replicase polyprotein
CC (PubMed:16306590). In addition, PL-PRO possesses a
CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains from cellular substrates
CC (PubMed:16306590, 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 (PubMed:23943763). Nsp3,
CC nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069).
CC Antagonizes innate immune induction of type I interferon by blocking
CC the phosphorylation, dimerization and subsequent nuclear translocation
CC of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-
CC kappa-B signaling (PubMed:19369340, PubMed:24622840).
CC {ECO:0000269|PubMed:16306590, ECO:0000269|PubMed:17692280,
CC ECO:0000269|PubMed:19369340, ECO:0000269|PubMed:23943763,
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 (PubMed:23943763). Alone
CC appears incapable to induce membrane curvature, but together with nsp3
CC is able to induce paired membranes. Nsp3, nsp4 and nsp6 together are
CC sufficient to form DMV. {ECO:0000269|PubMed:23943763,
CC ECO:0000303|PubMed:24410069}.
CC -!- FUNCTION: [3C-like proteinase nsp5]: Cleaves the C-terminus of
CC replicase polyprotein at 11 sites. Recognizes substrates containing the
CC core 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 (PubMed:24991833,
CC PubMed:24410069). Nsp3, nsp4 and nsp6 together are sufficient to form
CC DMV (PubMed:24991833, PubMed:24410069). Plays a role in the initial
CC induction of autophagosomes from host reticulum endoplasmic. Later,
CC limits the expansion of these phagosomes that are no longer able to
CC deliver viral components to lysosomes (PubMed:24991833).
CC {ECO:0000269|PubMed:24991833, 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]: Plays an essential role in viral
CC replication by forming a homodimer that binds single-stranded RNA.
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:22022266,
CC ECO:0000269|PubMed:22635272}.
CC -!- FUNCTION: [RNA-directed RNA polymerase nsp12]: Responsible for
CC replication and transcription of the viral RNA genome.
CC {ECO:0000269|PubMed:22791111}.
CC -!- FUNCTION: [Helicase nsp13]: Multi-functional protein with a zinc-
CC binding domain in N-terminus displaying RNA and DNA duplex-unwinding
CC activities with 5' to 3' polarity. Activity of helicase is dependent on
CC magnesium. {ECO:0000269|PubMed:12917423, ECO:0000269|PubMed:22615777}.
CC -!- FUNCTION: [Proofreading exoribonuclease nsp14]: 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 nsp15]: Plays a role in
CC viral transcription/replication and prevents the simultaneous
CC activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR
CC (PubMed:28158275, PubMed:18045871). Acts by degrading the 5'-
CC polyuridines generated during replication of the poly(A) region of
CC viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in
CC which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O
CC transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P)
CC (PubMed:16828802). If not degraded, poly(U) RNA would hybridize with
CC poly(A) RNA tails and activate host dsRNA sensors (PubMed:28158275,
CC PubMed:18045871). {ECO:0000269|PubMed:16828802,
CC ECO:0000269|PubMed:18045871, ECO:0000269|PubMed:28158275}.
CC -!- FUNCTION: [2'-O-methyltransferase nsp16]: Methyltransferase that
CC mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of
CC viral mRNAs (PubMed:18417574, PubMed:22022266,PubMed:20421945). N7-
CC methyl guanosine cap is a prerequisite for binding of nsp16
CC (PubMed:18417574). Therefore plays an essential role in viral mRNAs cap
CC methylation which is essential to evade immune system (PubMed:18417574,
CC PubMed:22022266,PubMed:20421945). {ECO:0000269|PubMed:18417574,
CC ECO:0000269|PubMed:20421945, ECO:0000269|PubMed:22022266, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539,
CC ECO:0000269|PubMed:14561748};
CC -!- CATALYTIC ACTIVITY: [Helicase nsp13]:
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 Evidence={ECO:0000269|PubMed:22615777};
CC -!- CATALYTIC ACTIVITY: [Helicase nsp13]:
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 Evidence={ECO:0000269|PubMed:22615777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=TSAVLQ-|-SGFRK-NH2 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:12917450, ECO:0000269|PubMed:14561748};
CC -!- CATALYTIC ACTIVITY: [Papain-like protease nsp3]:
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:12917450,
CC ECO:0000269|PubMed:17692280};
CC -!- CATALYTIC ACTIVITY: [2'-O-methyltransferase nsp16]:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000269|PubMed:22022266,
CC ECO:0000269|PubMed:28158275};
CC -!- CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease nsp15]:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000269|PubMed:16828802};
CC -!- COFACTOR: [Papain-like protease nsp3]:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16306590};
CC -!- COFACTOR: [Uridylate-specific endoribonuclease nsp15]:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16828802};
CC Note=Likely affects Nsp15 binding to RNA.
CC {ECO:0000269|PubMed:16828802};
CC -!- ACTIVITY REGULATION: [Proofreading exoribonuclease nsp14]: 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 papain-like
CC protease nsp3 and non-structural protein 6.
CC {ECO:0000269|PubMed:21345958}.
CC -!- SUBUNIT: [3C-like proteinase nsp5]: Monomer. Homodimer. Only the
CC 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]: Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure (PubMed:16228002). Interacts with ORF6 protein
CC (PubMed:17532020). {ECO:0000269|PubMed:16228002,
CC ECO:0000269|PubMed:17532020}.
CC -!- SUBUNIT: [Non-structural protein 9]: Homodimer.
CC {ECO:0000269|PubMed:19153232}.
CC -!- SUBUNIT: [Non-structural protein 10]: Homododecamer (PubMed:16873247).
CC Interacts with proofreading exoribonuclease nsp14 and 2'-O-
CC methyltransferase nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities (PubMed:18827877, PubMed:22022266,
CC PubMed:22635272). {ECO:0000269|PubMed:16873247,
CC ECO:0000269|PubMed:18827877, ECO:0000269|PubMed:22022266,
CC ECO:0000269|PubMed:22635272}.
CC -!- SUBUNIT: [Proofreading exoribonuclease nsp14]: Interacts (via N-
CC terminus) with host DDX1 (PubMed:20573827). Interacts with non-
CC structural protein 10 (PubMed:18827877). {ECO:0000269|PubMed:18827877,
CC ECO:0000269|PubMed:20573827}.
CC -!- SUBUNIT: [Uridylate-specific endoribonuclease nsp15]: Homohexamer.
CC {ECO:0000269|PubMed:16828802}.
CC -!- SUBUNIT: [2'-O-methyltransferase nsp16]: Interacts with nsp10.
CC {ECO:0000269|PubMed:18827877, ECO:0000269|PubMed:22022266}.
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; P59637: E; NbExp=5; IntAct=EBI-25474079, EBI-25487741;
CC PRO_0000037311; PRO_0000037311 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25474079, EBI-25474079;
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; Q13557: CAMK2D; Xeno; NbExp=4; IntAct=EBI-25474079, EBI-351018;
CC PRO_0000037311; Q14653: IRF3; Xeno; NbExp=5; IntAct=EBI-25474079, EBI-2650369;
CC PRO_0000037311; P05161: ISG15; Xeno; NbExp=2; IntAct=EBI-25474079, EBI-746466;
CC PRO_0000037311; Q64339: Isg15; Xeno; NbExp=4; IntAct=EBI-25474079, EBI-8345781;
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_0000037311; Q96PM5: RCHY1; Xeno; NbExp=9; IntAct=EBI-25474079, EBI-947779;
CC PRO_0000037311; Q86WV6: STING1; Xeno; NbExp=2; IntAct=EBI-25474079, EBI-2800345;
CC PRO_0000037311; P0CG48: UBC; Xeno; NbExp=3; IntAct=EBI-25474079, EBI-3390054;
CC PRO_0000037312; PRO_0000037312 [P0C6X7]: rep; NbExp=4; IntAct=EBI-25487250, EBI-25487250;
CC PRO_0000037312; PRO_0000037315 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25487250, EBI-25487941;
CC PRO_0000037312; K9N638: 1a; Xeno; NbExp=2; IntAct=EBI-25487250, EBI-25618448;
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_0000037314 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25487672, EBI-25487672;
CC PRO_0000037314; PRO_0000037315 [P0C6X7]: rep; NbExp=9; 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; Q19QW5: ORF6; NbExp=5; IntAct=EBI-25487941, EBI-25493595;
CC PRO_0000037315; PRO_0000037315 [P0C6X7]: rep; NbExp=4; 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=4; IntAct=EBI-25475825, EBI-25487941;
CC PRO_0000037316; PRO_0000037316 [P0C6X7]: rep; NbExp=5; IntAct=EBI-25475825, EBI-25475825;
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=5; 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=7; 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_0000037321; P06400: RB1; Xeno; NbExp=3; IntAct=EBI-25487301, EBI-491274;
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; PRO_0000037317 [P0C6X7]: rep; NbExp=16; IntAct=EBI-25487235, EBI-25487277;
CC PRO_0000037322; P40337: VHL; Xeno; NbExp=7; IntAct=EBI-25487235, EBI-301246;
CC PRO_0000283841; PRO_0000037311 [P0C6X7]: rep; NbExp=3; IntAct=EBI-25488721, EBI-25474079;
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 2]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endosome
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBCELLULAR LOCATION: [Papain-like protease nsp3]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein. Host cytoplasm
CC {ECO:0000269|PubMed:23943763}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-
CC pass membrane protein. Host cytoplasm {ECO:0000269|PubMed:23943763}.
CC Note=Localizes in virally-induced cytoplasmic double-membrane vesicles.
CC {ECO:0000269|PubMed:17855519, ECO:0000269|PubMed:21345958,
CC ECO:0000269|PubMed:23943763}.
CC -!- SUBCELLULAR LOCATION: [3C-like proteinase nsp5]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host Golgi apparatus
CC {ECO:0000250|UniProtKB:P0DTD1}.
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}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000269|PubMed:17532020}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Helicase nsp13]: Host endoplasmic reticulum-
CC Golgi intermediate compartment {ECO:0000305}. Note=The helicase
CC interacts with the N protein in membranous complexes and colocalizes
CC with sites of synthesis of new viral RNA.
CC -!- SUBCELLULAR LOCATION: [Proofreading exoribonuclease nsp14]: Host
CC cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease nsp15]: Host
CC cytoplasm, host perinuclear region {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Isoform replicase polyprotein 1ab is produced by -1 ribosomal
CC frameshifting at the 1a-1b genes boundary. Isoform replicase
CC polyprotein 1a is produced by conventional translation.
CC {ECO:0000305};
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: [Papain-like protease nsp3]: The hydrophobic region HD1
CC probably mediates the membrane association of the replication complex.
CC {ECO:0000305|PubMed:18842706}.
CC -!- DOMAIN: [Non-structural protein 4]: The hydrophobic region HD2 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000305|PubMed:18842706}.
CC -!- DOMAIN: [Non-structural protein 6]: The hydrophobic region HD3 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000305|PubMed:18842706}.
CC -!- PTM: [Isoform Replicase polyprotein 1ab]: Specific enzymatic cleavages
CC in vivo by its own proteases yield mature proteins (PubMed:32083638,
CC PubMed:16306590, PubMed:12917450, PubMed:15331731, PubMed:15564471).
CC 3C-like proteinase nsp5 liberates nsps 6-16 from the polyprotein
CC (PubMed:32083638). Papain-like and 3C-like proteinases are
CC autocatalytically processed. {ECO:0000269|PubMed:12917450,
CC ECO:0000269|PubMed:15331731, ECO:0000269|PubMed:15564471,
CC ECO:0000269|PubMed:16306590, 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 -!- 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};
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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 RefSeq; NP_828849.2; NC_004718.3.
DR PDB; 1Q2W; X-ray; 1.86 A; A/B=3241-3544.
DR PDB; 1QZ8; X-ray; 2.70 A; A/B=4118-4230.
DR PDB; 1UJ1; X-ray; 1.90 A; A/B=3241-3546.
DR PDB; 1UK2; X-ray; 2.20 A; A/B=3241-3546.
DR PDB; 1UK3; X-ray; 2.40 A; A/B=3241-3546.
DR PDB; 1UK4; X-ray; 2.50 A; A/B=3241-3546.
DR PDB; 1UW7; X-ray; 2.80 A; A=4118-4230.
DR PDB; 1WOF; X-ray; 2.00 A; A/B=3241-3546.
DR PDB; 1YSY; NMR; -; A=3837-3919.
DR PDB; 1Z1I; X-ray; 2.80 A; A=3241-3546.
DR PDB; 1Z1J; X-ray; 2.80 A; A/B=3241-3546.
DR PDB; 2A5A; X-ray; 2.08 A; A=3241-3546.
DR PDB; 2A5I; X-ray; 1.88 A; A=3241-3546.
DR PDB; 2A5K; X-ray; 2.30 A; A/B=3241-3546.
DR PDB; 2ACF; X-ray; 1.40 A; A/B/C/D=1002-1176.
DR PDB; 2AHM; X-ray; 2.40 A; A/B/C/D=3837-3919, E/F/G/H=3920-4117.
DR PDB; 2ALV; X-ray; 1.90 A; A=3241-3543.
DR PDB; 2AMD; X-ray; 1.85 A; A/B=3241-3546.
DR PDB; 2AMQ; X-ray; 2.30 A; A/B=3241-3546.
DR PDB; 2BX3; X-ray; 2.00 A; A=3241-3546.
DR PDB; 2BX4; X-ray; 2.79 A; A=3241-3546.
DR PDB; 2C3S; X-ray; 1.90 A; A=3241-3546.
DR PDB; 2D2D; X-ray; 2.70 A; A/B=3241-3546.
DR PDB; 2DUC; X-ray; 1.70 A; A/B=3241-3546.
DR PDB; 2FAV; X-ray; 1.80 A; A/B/C=1000-1173.
DR PDB; 2FE8; X-ray; 1.85 A; A/B/C=1541-1854.
DR PDB; 2FYG; X-ray; 1.80 A; A=4240-4362.
DR PDB; 2G9T; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=4231-4378.
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; 2K7X; NMR; -; A=3427-3546.
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; 6LNQ; X-ray; 2.24 A; A=3241-3546.
DR PDB; 6NUR; EM; 3.10 A; A=4370-5300, C=3837-3919.
DR PDB; 6NUS; EM; 3.50 A; A=4370-5300.
DR PDB; 6W79; X-ray; 1.46 A; A=3241-3546.
DR PDB; 6WCO; X-ray; 1.48 A; A=3241-3546.
DR PDB; 7LCP; X-ray; 1.90 A; A=3241-3546.
DR PDB; 7LCQ; X-ray; 2.15 A; A=3241-3546.
DR PDBsum; 1Q2W; -.
DR PDBsum; 1QZ8; -.
DR PDBsum; 1UJ1; -.
DR PDBsum; 1UK2; -.
DR PDBsum; 1UK3; -.
DR PDBsum; 1UK4; -.
DR PDBsum; 1UW7; -.
DR PDBsum; 1WOF; -.
DR PDBsum; 1YSY; -.
DR PDBsum; 1Z1I; -.
DR PDBsum; 1Z1J; -.
DR PDBsum; 2A5A; -.
DR PDBsum; 2A5I; -.
DR PDBsum; 2A5K; -.
DR PDBsum; 2ACF; -.
DR PDBsum; 2AHM; -.
DR PDBsum; 2ALV; -.
DR PDBsum; 2AMD; -.
DR PDBsum; 2AMQ; -.
DR PDBsum; 2BX3; -.
DR PDBsum; 2BX4; -.
DR PDBsum; 2C3S; -.
DR PDBsum; 2D2D; -.
DR PDBsum; 2DUC; -.
DR PDBsum; 2FAV; -.
DR PDBsum; 2FE8; -.
DR PDBsum; 2FYG; -.
DR PDBsum; 2G9T; -.
DR PDBsum; 2GA6; -.
DR PDBsum; 2GDT; -.
DR PDBsum; 2GRI; -.
DR PDBsum; 2GT7; -.
DR PDBsum; 2GT8; -.
DR PDBsum; 2GTB; -.
DR PDBsum; 2GX4; -.
DR PDBsum; 2GZ7; -.
DR PDBsum; 2GZ8; -.
DR PDBsum; 2GZ9; -.
DR PDBsum; 2H2Z; -.
DR PDBsum; 2H85; -.
DR PDBsum; 2HOB; -.
DR PDBsum; 2HSX; -.
DR PDBsum; 2IDY; -.
DR PDBsum; 2JZD; -.
DR PDBsum; 2JZE; -.
DR PDBsum; 2JZF; -.
DR PDBsum; 2K7X; -.
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; 6LNQ; -.
DR PDBsum; 6NUR; -.
DR PDBsum; 6NUS; -.
DR PDBsum; 6W79; -.
DR PDBsum; 6WCO; -.
DR PDBsum; 7LCP; -.
DR PDBsum; 7LCQ; -.
DR BMRB; P0C6X7; -.
DR SMR; P0C6X7; -.
DR BioGRID; 4383938; 1.
DR BioGRID; 4383939; 22.
DR BioGRID; 4383940; 50.
DR BioGRID; 4383941; 43.
DR BioGRID; 4383942; 32.
DR BioGRID; 4383943; 16.
DR BioGRID; 4383944; 17.
DR BioGRID; 4383945; 43.
DR BioGRID; 4383946; 52.
DR BioGRID; 4383947; 36.
DR BioGRID; 4383948; 18.
DR BioGRID; 4383949; 55.
DR BioGRID; 4383950; 98.
DR BioGRID; 4383951; 20.
DR BioGRID; 4383952; 12.
DR BioGRID; 4383953; 18.
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 ComplexPortal; CPX-6462; SARS-CoV replication and transcription complex.
DR IntAct; P0C6X7; 366.
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; DB15686; GS-441524.
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 MEROPS; C16.009; -.
DR MEROPS; C30.005; -.
DR PRIDE; P0C6X7; -.
DR DNASU; 1489680; -.
DR GeneID; 1489680; -.
DR KEGG; vg:1489680; -.
DR BRENDA; 2.1.1.56; 7599.
DR BRENDA; 2.7.7.48; 7599.
DR BRENDA; 3.4.22.69; 7599.
DR BRENDA; 3.4.22.B14; 7599.
DR BRENDA; 3.4.22.B80; 7599.
DR BRENDA; 3.6.4.12; 7599.
DR Reactome; R-HSA-9679504; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR Reactome; R-HSA-9682706; Replication of the SARS-CoV-1 genome.
DR Reactome; R-HSA-9682708; Transcription of SARS-CoV-1 sgRNAs.
DR Reactome; R-HSA-9683439; Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC).
DR Reactome; R-HSA-9684325; Maturation of replicase proteins.
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:0062243; C:double membrane vesicle viral factory outer membrane; TAS:Reactome.
DR GO; GO:1905369; C:endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:1902555; C:endoribonuclease complex; IPI:ComplexPortal.
DR GO; GO:1905354; C:exoribonuclease complex; IPI:ComplexPortal.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0044174; C:host cell endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0044177; C:host cell Golgi apparatus; 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:0044385; C:integral to membrane of host cell; IC:ComplexPortal.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0031381; C:viral RNA-directed RNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
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:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019785; F:ISG15-specific peptidase activity; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
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:0046983; F:protein dimerization activity; IDA:UniProtKB.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:ComplexPortal.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:1902680; P:positive regulation of RNA biosynthetic process; IDA:ComplexPortal.
DR GO; GO:2000158; P:positive regulation of ubiquitin-specific protease activity; IDA:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IC:ComplexPortal.
DR GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:UniProtKB.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IDA:UniProtKB.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IDA:UniProtKB.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IDA:UniProtKB.
DR GO; GO:0039604; P:suppression by virus of host translation; IDA:UniProtKB.
DR GO; GO:0039501; P:suppression by virus of host type I interferon production; IDA:UniProtKB.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; 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:0046786; P:viral replication complex formation and maintenance; IC:ComplexPortal.
DR GO; GO:0039694; P:viral RNA genome replication; IDA:UniProtKB.
DR GO; GO:0019083; P:viral transcription; IDA:UniProtKB.
DR CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21516; cv_beta_Nsp2_SARS-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21562; Macro_cv_SUD-N_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21591; SARS-CoV-like_RdRp; 1.
DR CDD; cd21525; SUD_C_SARS-CoV_Nsp3; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR DisProt; DP02924; -.
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; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.30.160.820; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.220.20; -; 1.
DR Gene3D; 3.40.220.30; -; 1.
DR Gene3D; 3.40.30.150; -; 1.
DR Gene3D; 3.40.50.11020; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044315; NSP14_betaCoV.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR044330; NSP15_alpha_betaCoV_N.
DR InterPro; IPR044322; NSP15_M_alpha_beta_CoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR021590; NSP1_bCoV.
DR InterPro; IPR038030; NSP1_sf_bCoV.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044389; NSP2_SARS-CoV-like.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR024358; NSP3_N_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR038166; NSP3_PL2pro_sf_bCoV.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044864; NSP3_SUD-N_bCoV.
DR InterPro; IPR044374; NSP3_SUD-N_SARS-CoV.
DR InterPro; IPR043478; NSP3_SUD-N_sf_bCoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044367; NSP6_betaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
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; IPR044351; RdRp_SARS-CoV-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR009469; RNA_pol_N_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF16251; bCoV_NAR; 1.
DR Pfam; PF11501; bCoV_NSP1; 1.
DR Pfam; PF12379; bCoV_NSP3_N; 1.
DR Pfam; PF12124; bCoV_SUD_C; 1.
DR Pfam; PF11633; bCoV_SUD_M; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF19216; CoV_NSP15_M; 1.
DR Pfam; PF19219; CoV_NSP15_N; 1.
DR Pfam; PF19212; CoV_NSP2_C; 1.
DR Pfam; PF19211; CoV_NSP2_N; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 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; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51963; BCOV_NSP1_C; 1.
DR PROSITE; PS51942; BCOV_NSP3C_C; 1.
DR PROSITE; PS51941; BCOV_NSP3C_M; 1.
DR PROSITE; PS51994; BCOV_NSP3E_G2M; 1.
DR PROSITE; PS51945; BCOV_NSP3E_NAB; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51962; COV_NSP1; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51991; COV_NSP2_C; 1.
DR PROSITE; PS51990; COV_NSP2_M; 1.
DR PROSITE; PS51989; COV_NSP2_N; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51940; SARS_NSP3C_N; 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 endoplasmic reticulum; Host endosome;
KW Host gene expression shutoff by virus; Host Golgi apparatus; 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 Lyase; 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 /id="PRO_0000037310"
FT CHAIN 819..2740
FT /note="Papain-like protease nsp3"
FT /id="PRO_0000037311"
FT CHAIN 2741..3240
FT /note="Non-structural protein 4"
FT /id="PRO_0000283841"
FT CHAIN 3241..3546
FT /note="3C-like proteinase nsp5"
FT /id="PRO_0000037312"
FT CHAIN 3547..3836
FT /note="Non-structural protein 6"
FT /id="PRO_0000037313"
FT CHAIN 3837..3919
FT /note="Non-structural protein 7"
FT /id="PRO_0000037314"
FT CHAIN 3920..4117
FT /note="Non-structural protein 8"
FT /id="PRO_0000037315"
FT CHAIN 4118..4230
FT /note="Non-structural protein 9"
FT /id="PRO_0000037316"
FT CHAIN 4231..4369
FT /note="Non-structural protein 10"
FT /id="PRO_0000037317"
FT CHAIN 4370..5301
FT /note="RNA-directed RNA polymerase nsp12"
FT /id="PRO_0000037318"
FT CHAIN 5302..5902
FT /note="Helicase nsp13"
FT /id="PRO_0000037319"
FT CHAIN 5903..6429
FT /note="Proofreading exoribonuclease nsp14"
FT /id="PRO_0000037320"
FT CHAIN 6430..6775
FT /note="Uridylate-specific endoribonuclease nsp15"
FT /id="PRO_0000037321"
FT CHAIN 6776..7073
FT /note="2'-O-methyltransferase nsp16"
FT /id="PRO_0000037322"
FT TOPO_DOM 1..2202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 2203..2223
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 2224..2303
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 2304..2324
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 2325..2754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 2755..2775
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 2776..3021
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3022..3042
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3043..3076
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3077..3097
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3098..3104
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3105..3125
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3126..3563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3564..3584
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3585
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3586..3606
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3607..3611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3612..3632
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3633..3657
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3658..3678
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3679..3727
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3728..3748
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3749..3755
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:18842706"
FT TRANSMEM 3756..3776
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18842706"
FT TOPO_DOM 3777..7073
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18842706"
FT DOMAIN 12..127
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 148..179
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 183..456
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 458..688
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 690..818
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 822..930
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1003..1169
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1207..1335
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1343..1470
FT /note="Macro 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1472..1538
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1542..1597
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1611..1875
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1888..1998
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2023..2132
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2637..2740
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3142..3240
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3241..3546
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3837..3919
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3920..4117
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4118..4230
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4231..4369
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4376..4630
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4734..5301
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
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 DOMAIN 5974..6189
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6198..6429
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6430..6490
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6491..6616
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6633..6772
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6777..7071
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1729..1766
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444,
FT ECO:0000269|PubMed:16306590"
FT ZN_FING 4304..4320
FT ZN_FING 4347..4360
FT REGION 200..236
FT /note="C2H2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 323..344
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 370..416
FT /note="C2HC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 972..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2203..2324
FT /note="HD1"
FT /evidence="ECO:0000305|PubMed:18842706"
FT REGION 2755..3125
FT /note="HD2"
FT /evidence="ECO:0000305|PubMed:18842706"
FT REGION 3564..3776
FT /note="HD3"
FT /evidence="ECO:0000305|PubMed:18842706"
FT REGION 6316..6330
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT COMPBIAS 972..997
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1651
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444,
FT ECO:0000269|PubMed:16306590"
FT ACT_SITE 1812
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444,
FT ECO:0000269|PubMed:16306590"
FT ACT_SITE 1826
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000269|PubMed:16306590"
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 ACT_SITE 5128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5994
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6093
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6678
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6718
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6821
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6945
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6978
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297,
FT ECO:0000269|PubMed:22022266"
FT BINDING 4307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297,
FT ECO:0000269|PubMed:22022266"
FT BINDING 4313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297,
FT ECO:0000269|PubMed:22022266"
FT BINDING 4320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297,
FT ECO:0000269|PubMed:22022266"
FT BINDING 4347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297,
FT ECO:0000269|PubMed:22022266"
FT BINDING 4350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297,
FT ECO:0000269|PubMed:22022266"
FT BINDING 4358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297,
FT ECO:0000269|PubMed:22022266"
FT BINDING 4360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297,
FT ECO:0000269|PubMed:22022266"
FT BINDING 5306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5583..5590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 6109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6233..6239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 180..181
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000269|PubMed:16306590"
FT SITE 818..819
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000269|PubMed:16306590"
FT SITE 2740..2741
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000269|PubMed:16306590"
FT SITE 3240..3241
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748"
FT SITE 3546..3547
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748"
FT SITE 3836..3837
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748,
FT ECO:0000269|PubMed:32083638"
FT SITE 3919..3920
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748,
FT ECO:0000269|PubMed:32083638"
FT SITE 4117..4118
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748,
FT ECO:0000269|PubMed:32083638"
FT SITE 4230..4231
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748,
FT ECO:0000269|PubMed:32083638"
FT SITE 4369..4370
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748"
FT SITE 5301..5302
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748"
FT SITE 5902..5903
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748"
FT SITE 6429..6430
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748"
FT SITE 6775..6776
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000269|PubMed:14561748"
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 1651
FT /note="C->A: Complete loss of PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:16306590"
FT MUTAGEN 1688
FT /note="C->A: No effect on PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:16306590"
FT MUTAGEN 1729
FT /note="C->A: Complete loss of PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:16306590"
FT MUTAGEN 1732
FT /note="C->A: Complete loss of PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:16306590"
FT MUTAGEN 1764
FT /note="C->A: Complete loss of PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:16306590"
FT MUTAGEN 1766
FT /note="C->A: Complete loss of PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:16306590"
FT MUTAGEN 1826
FT /note="D->A: Complete loss of PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:16306590"
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 MUTAGEN 4306..4308
FT /note="YCR->AAA: Complete loss of NSP16 binding to SAM and
FT NSP16 MTase activity."
FT /evidence="ECO:0000269|PubMed:22022266"
FT MUTAGEN 4313..4314
FT /note="HP->AA: Complete loss of NSP16 binding to SAM and
FT NSP16 MTase activity."
FT /evidence="ECO:0000269|PubMed:22022266"
FT MUTAGEN 6663
FT /note="H->A: Complete loss of NSP15 endonuclease activity."
FT /evidence="ECO:0000269|PubMed:16828802,
FT ECO:0000269|PubMed:18045871"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2GDT"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2GDT"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:2GDT"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2GDT"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2GDT"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2GDT"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2GDT"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:2GDT"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2GDT"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2GDT"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:2GDT"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:2GRI"
FT TURN 831..833
FT /evidence="ECO:0007829|PDB:2GRI"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:2GRI"
FT STRAND 848..851
FT /evidence="ECO:0007829|PDB:2GRI"
FT TURN 852..856
FT /evidence="ECO:0007829|PDB:2GRI"
FT STRAND 860..862
FT /evidence="ECO:0007829|PDB:2GRI"
FT TURN 869..871
FT /evidence="ECO:0007829|PDB:2GRI"
FT HELIX 872..882
FT /evidence="ECO:0007829|PDB:2GRI"
FT HELIX 888..894
FT /evidence="ECO:0007829|PDB:2GRI"
FT HELIX 898..901
FT /evidence="ECO:0007829|PDB:2GRI"
FT STRAND 907..909
FT /evidence="ECO:0007829|PDB:2GRI"
FT STRAND 911..915
FT /evidence="ECO:0007829|PDB:2GRI"
FT STRAND 918..920
FT /evidence="ECO:0007829|PDB:2GRI"
FT STRAND 922..926
FT /evidence="ECO:0007829|PDB:2GRI"
FT STRAND 1013..1021
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1023..1030
FT /evidence="ECO:0007829|PDB:2ACF"
FT STRAND 1033..1038
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1048..1056
FT /evidence="ECO:0007829|PDB:2ACF"
FT TURN 1057..1059
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1060..1072
FT /evidence="ECO:0007829|PDB:2ACF"
FT STRAND 1080..1084
FT /evidence="ECO:0007829|PDB:2ACF"
FT TURN 1086..1088
FT /evidence="ECO:0007829|PDB:2ACF"
FT STRAND 1090..1095
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1100..1102
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1108..1114
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1115..1118
FT /evidence="ECO:0007829|PDB:2ACF"
FT STRAND 1119..1124
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1130..1132
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1136..1146
FT /evidence="ECO:0007829|PDB:2ACF"
FT STRAND 1149..1156
FT /evidence="ECO:0007829|PDB:2ACF"
FT HELIX 1158..1168
FT /evidence="ECO:0007829|PDB:2ACF"
FT STRAND 1345..1347
FT /evidence="ECO:0007829|PDB:2JZF"
FT HELIX 1351..1361
FT /evidence="ECO:0007829|PDB:2JZD"
FT STRAND 1364..1368
FT /evidence="ECO:0007829|PDB:2JZD"
FT HELIX 1372..1381
FT /evidence="ECO:0007829|PDB:2JZD"
FT STRAND 1389..1401
FT /evidence="ECO:0007829|PDB:2JZD"
FT HELIX 1407..1417
FT /evidence="ECO:0007829|PDB:2JZD"
FT STRAND 1421..1424
FT /evidence="ECO:0007829|PDB:2JZF"
FT STRAND 1426..1428
FT /evidence="ECO:0007829|PDB:2JZD"
FT HELIX 1429..1431
FT /evidence="ECO:0007829|PDB:2JZD"
FT HELIX 1435..1442
FT /evidence="ECO:0007829|PDB:2JZD"
FT STRAND 1449..1452
FT /evidence="ECO:0007829|PDB:2JZF"
FT HELIX 1457..1467
FT /evidence="ECO:0007829|PDB:2JZD"
FT STRAND 1544..1555
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1557..1562
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1567..1571
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1572..1576
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1582..1584
FT /evidence="ECO:0007829|PDB:5E6J"
FT HELIX 1588..1590
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1594..1597
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1602..1612
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1619..1630
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1639..1642
FT /evidence="ECO:0007829|PDB:5E6J"
FT TURN 1648..1650
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1651..1661
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1667..1669
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1670..1681
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1685..1694
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1705..1713
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1722..1729
FT /evidence="ECO:0007829|PDB:2FE8"
FT TURN 1730..1732
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1733..1740
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1742..1745
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1746..1749
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1753..1758
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1760..1763
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1767..1794
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1795..1797
FT /evidence="ECO:0007829|PDB:5E6J"
FT STRAND 1799..1806
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 1808..1810
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1812..1826
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1829..1846
FT /evidence="ECO:0007829|PDB:2FE8"
FT STRAND 1848..1851
FT /evidence="ECO:0007829|PDB:2FE8"
FT HELIX 3251..3254
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3257..3262
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3265..3272
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3275..3279
FT /evidence="ECO:0007829|PDB:6W79"
FT HELIX 3280..3283
FT /evidence="ECO:0007829|PDB:6W79"
FT HELIX 3286..3288
FT /evidence="ECO:0007829|PDB:6WCO"
FT STRAND 3289..3291
FT /evidence="ECO:0007829|PDB:6W79"
FT HELIX 3294..3299
FT /evidence="ECO:0007829|PDB:6W79"
FT HELIX 3303..3305
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3306..3310
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3313..3315
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3317..3323
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3326..3333
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3340..3343
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3351..3358
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3361..3369
FT /evidence="ECO:0007829|PDB:6W79"
FT HELIX 3379..3381
FT /evidence="ECO:0007829|PDB:2QCY"
FT STRAND 3388..3393
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3396..3406
FT /evidence="ECO:0007829|PDB:6W79"
FT TURN 3408..3410
FT /evidence="ECO:0007829|PDB:1UJ1"
FT STRAND 3412..3415
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3421..3424
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3427..3430
FT /evidence="ECO:0007829|PDB:5C5O"
FT HELIX 3441..3453
FT /evidence="ECO:0007829|PDB:6W79"
FT TURN 3458..3460
FT /evidence="ECO:0007829|PDB:3EBN"
FT HELIX 3467..3476
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3477..3479
FT /evidence="ECO:0007829|PDB:1Z1J"
FT HELIX 3484..3489
FT /evidence="ECO:0007829|PDB:6W79"
FT HELIX 3491..3497
FT /evidence="ECO:0007829|PDB:6W79"
FT HELIX 3501..3514
FT /evidence="ECO:0007829|PDB:6W79"
FT STRAND 3516..3518
FT /evidence="ECO:0007829|PDB:2BX3"
FT STRAND 3521..3523
FT /evidence="ECO:0007829|PDB:1UK4"
FT STRAND 3524..3526
FT /evidence="ECO:0007829|PDB:6W79"
FT HELIX 3533..3539
FT /evidence="ECO:0007829|PDB:6W79"
FT TURN 3540..3542
FT /evidence="ECO:0007829|PDB:2QC2"
FT HELIX 3837..3855
FT /evidence="ECO:0007829|PDB:2AHM"
FT HELIX 3858..3860
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 3862..3876
FT /evidence="ECO:0007829|PDB:2AHM"
FT STRAND 3878..3880
FT /evidence="ECO:0007829|PDB:1YSY"
FT HELIX 3881..3905
FT /evidence="ECO:0007829|PDB:2AHM"
FT HELIX 3906..3909
FT /evidence="ECO:0007829|PDB:1YSY"
FT TURN 3910..3912
FT /evidence="ECO:0007829|PDB:1YSY"
FT HELIX 3913..3916
FT /evidence="ECO:0007829|PDB:1YSY"
FT HELIX 3922..3924
FT /evidence="ECO:0007829|PDB:2AHM"
FT HELIX 3929..3946
FT /evidence="ECO:0007829|PDB:2AHM"
FT HELIX 3951..3956
FT /evidence="ECO:0007829|PDB:2AHM"
FT TURN 3959..3963
FT /evidence="ECO:0007829|PDB:2AHM"
FT TURN 3970..3972
FT /evidence="ECO:0007829|PDB:2AHM"
FT HELIX 3973..3987
FT /evidence="ECO:0007829|PDB:2AHM"
FT HELIX 3997..4017
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 4020..4030
FT /evidence="ECO:0007829|PDB:5F22"
FT STRAND 4035..4037
FT /evidence="ECO:0007829|PDB:5F22"
FT STRAND 4046..4051
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 4054..4060
FT /evidence="ECO:0007829|PDB:5F22"
FT STRAND 4065..4068
FT /evidence="ECO:0007829|PDB:5F22"
FT STRAND 4071..4079
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 4088..4090
FT /evidence="ECO:0007829|PDB:5F22"
FT TURN 4093..4095
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 4096..4098
FT /evidence="ECO:0007829|PDB:5F22"
FT STRAND 4103..4109
FT /evidence="ECO:0007829|PDB:5F22"
FT STRAND 4120..4125
FT /evidence="ECO:0007829|PDB:1UW7"
FT STRAND 4127..4137
FT /evidence="ECO:0007829|PDB:1QZ8"
FT STRAND 4141..4150
FT /evidence="ECO:0007829|PDB:1QZ8"
FT TURN 4152..4154
FT /evidence="ECO:0007829|PDB:1QZ8"
FT STRAND 4157..4164
FT /evidence="ECO:0007829|PDB:1QZ8"
FT STRAND 4170..4174
FT /evidence="ECO:0007829|PDB:1QZ8"
FT STRAND 4176..4179
FT /evidence="ECO:0007829|PDB:1QZ8"
FT STRAND 4181..4186
FT /evidence="ECO:0007829|PDB:1QZ8"
FT STRAND 4190..4194
FT /evidence="ECO:0007829|PDB:1QZ8"
FT STRAND 4201..4208
FT /evidence="ECO:0007829|PDB:1QZ8"
FT HELIX 4213..4226
FT /evidence="ECO:0007829|PDB:1QZ8"
FT HELIX 4238..4240
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 4243..4248
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 4250..4252
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 4253..4262
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 4284..4288
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 4295..4300
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 4301..4303
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 4305..4308
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 4314..4318
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 4325..4330
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 4331..4333
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 4337..4343
FT /evidence="ECO:0007829|PDB:2XYQ"
FT TURN 4348..4350
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 4351..4353
FT /evidence="ECO:0007829|PDB:5NFY"
FT TURN 4354..4357
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 4490..4492
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4493..4501
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4505..4507
FT /evidence="ECO:0007829|PDB:6NUS"
FT HELIX 4509..4517
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4523..4527
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 4529..4532
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4534..4537
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4540..4544
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4545..4547
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4548..4567
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4570..4573
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4576..4578
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4600..4602
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4604..4616
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 4617..4620
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4621..4624
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4645..4655
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4667..4669
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4671..4673
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4674..4686
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4687..4689
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4692..4694
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4695..4704
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4707..4717
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 4718..4720
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4721..4724
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4731..4734
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4737..4744
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4748..4751
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4754..4759
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4766..4770
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4786..4793
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 4794..4798
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4818..4822
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4823..4827
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4835..4847
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 4848..4851
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4859..4861
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4875..4877
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4881..4885
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4890..4899
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 4900..4902
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4908..4913
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4918..4920
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4925..4928
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4931..4949
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4953..4956
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 4963..4965
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4966..4975
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4979..4985
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4991..4994
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4997..5007
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5008..5010
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5012..5014
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5017..5031
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5035..5038
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5041..5044
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5053..5055
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5056..5077
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5081..5083
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5087..5097
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 5098..5100
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5108..5121
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5122..5127
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5130..5136
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5137..5140
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 5141..5143
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5148..5158
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5165..5167
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5169..5171
FT /evidence="ECO:0007829|PDB:6NUS"
FT STRAND 5184..5190
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5192..5200
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5203..5211
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 5217..5219
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5221..5234
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5236..5240
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5244..5263
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5278..5282
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 5283..5285
FT /evidence="ECO:0007829|PDB:6NUR"
FT TURN 5307..5309
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5312..5314
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5316..5320
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5328..5335
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5343..5349
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5361..5363
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5368..5372
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5374..5376
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5382..5386
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5393..5397
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5404..5412
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5418..5426
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5429..5446
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5447..5449
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5453..5457
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5461..5468
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5483..5488
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5493..5503
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5509..5516
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5525..5528
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5561..5566
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5567..5570
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5572..5575
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5576..5581
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5589..5599
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5605..5610
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5612..5616
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5617..5622
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5623..5626
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5630..5633
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5640..5642
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5647..5649
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5655..5660
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5661..5663
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5666..5668
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5670..5674
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5677..5679
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5682..5691
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5695..5700
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5720..5722
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5725..5730
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5743..5745
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5747..5750
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5751..5754
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5756..5759
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5791..5793
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5794..5796
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5797..5800
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5815..5818
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5819..5827
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5834..5836
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5843..5848
FT /evidence="ECO:0007829|PDB:6JYT"
FT TURN 5854..5856
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5859..5866
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5873..5876
FT /evidence="ECO:0007829|PDB:6JYT"
FT HELIX 5882..5884
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5893..5895
FT /evidence="ECO:0007829|PDB:6JYT"
FT STRAND 5922..5924
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 5928..5931
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 5933..5935
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 5955..5957
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 5978..5983
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 5986..5997
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6000..6002
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6006..6016
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6018..6020
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6024..6028
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6033..6037
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6046..6053
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6054..6057
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6061..6076
FT /evidence="ECO:0007829|PDB:5C8T"
FT TURN 6077..6079
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6084..6089
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6091..6100
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6112..6115
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6118..6120
FT /evidence="ECO:0007829|PDB:5C8T"
FT TURN 6121..6124
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6125..6127
FT /evidence="ECO:0007829|PDB:5C8T"
FT TURN 6129..6131
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6137..6140
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6142..6145
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6146..6149
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6155..6162
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6164..6166
FT /evidence="ECO:0007829|PDB:5C8U"
FT HELIX 6172..6188
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6204..6226
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6229..6235
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6242..6245
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6247..6256
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6263..6267
FT /evidence="ECO:0007829|PDB:5C8S"
FT HELIX 6272..6275
FT /evidence="ECO:0007829|PDB:5C8T"
FT TURN 6276..6278
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6281..6288
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6296..6303
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6312..6314
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6320..6322
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6324..6326
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6328..6330
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6335..6338
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6341..6343
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6373..6376
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6381..6383
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6387..6405
FT /evidence="ECO:0007829|PDB:5C8T"
FT STRAND 6408..6412
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6419..6425
FT /evidence="ECO:0007829|PDB:5C8T"
FT HELIX 6431..6441
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6453..6456
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6459..6464
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6467..6473
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6476..6478
FT /evidence="ECO:0007829|PDB:2H85"
FT HELIX 6480..6488
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6493..6495
FT /evidence="ECO:0007829|PDB:2OZK"
FT HELIX 6498..6503
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6508..6513
FT /evidence="ECO:0007829|PDB:2H85"
FT TURN 6517..6520
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6521..6530
FT /evidence="ECO:0007829|PDB:2H85"
FT TURN 6532..6534
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6535..6539
FT /evidence="ECO:0007829|PDB:2H85"
FT HELIX 6543..6545
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6550..6553
FT /evidence="ECO:0007829|PDB:2H85"
FT HELIX 6559..6565
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6567..6575
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6589..6591
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6594..6596
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6599..6601
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6606..6611
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6614..6616
FT /evidence="ECO:0007829|PDB:2RHB"
FT HELIX 6629..6631
FT /evidence="ECO:0007829|PDB:2H85"
FT HELIX 6637..6644
FT /evidence="ECO:0007829|PDB:2H85"
FT HELIX 6647..6653
FT /evidence="ECO:0007829|PDB:2H85"
FT HELIX 6661..6664
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6670..6673
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6677..6679
FT /evidence="ECO:0007829|PDB:2OZK"
FT HELIX 6680..6689
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6692..6698
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6703..6711
FT /evidence="ECO:0007829|PDB:2H85"
FT TURN 6712..6714
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6717..6724
FT /evidence="ECO:0007829|PDB:2H85"
FT HELIX 6728..6736
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6741..6751
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6754..6763
FT /evidence="ECO:0007829|PDB:2H85"
FT STRAND 6766..6772
FT /evidence="ECO:0007829|PDB:2H85"
FT HELIX 6777..6780
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6781..6785
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 6788..6791
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 6817..6829
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6841..6846
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 6855..6863
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6869..6876
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6881..6888
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 6890..6892
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6893..6897
FT /evidence="ECO:0007829|PDB:3R24"
FT STRAND 6899..6904
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 6924..6935
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6936..6946
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6948..6950
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 6953..6959
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6962..6970
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 6971..6973
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 6979..6986
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 6996..7009
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 7017..7020
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 7033..7035
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 7039..7041
FT /evidence="ECO:0007829|PDB:2XYQ"
FT HELIX 7044..7051
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 7055..7057
FT /evidence="ECO:0007829|PDB:2XYQ"
FT STRAND 7065..7067
FT /evidence="ECO:0007829|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
