ID R1A_SARS Reviewed; 4382 AA.
AC P0C6U8; P59641;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Replicase polyprotein 1a;
DE Short=pp1a;
DE AltName: Full=ORF1a 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:17692280};
DE EC=3.4.22.- {ECO:0000269|PubMed:12917450, ECO:0000269|PubMed:16306590, ECO:0000269|PubMed:17692280};
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=RNA-capping enzyme subunit nsp9;
DE AltName: Full=Non-structural protein 9;
DE Short=nsp9;
DE EC=2.7.7.50;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE Contains:
DE RecName: Full=Non-structural protein 11;
DE Short=nsp11;
GN ORFNames=1a;
OS 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 AND 1655-4382.
RC STRAIN=Isolate Shanghai LY;
RA Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [21]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1A), CATALYTIC ACTIVITY
RP (3C-LIKE PROTEINASE NSP5), AND CATALYTIC ACTIVITY (PAPAIN-LIKE PROTEASE
RP 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 [22]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1A).
RX PubMed=15331731; DOI=10.1128/jvi.78.18.9977-9986.2004;
RA Prentice E., McAuliffe J., Lu X., Subbarao K., Denison M.R.;
RT "Identification and characterization of severe acute respiratory syndrome
RT coronavirus replicase proteins.";
RL J. Virol. 78:9977-9986(2004).
RN [23]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1A).
RC STRAIN=Isolate Urbani;
RX PubMed=15564471; DOI=10.1128/jvi.78.24.13600-13612.2004;
RA Harcourt B.H., Jukneliene D., Kanjanahaluethai A., Bechill J.,
RA Severson K.M., Smith C.M., Rota P.A., Baker S.C.;
RT "Identification of severe acute respiratory syndrome coronavirus replicase
RT products and characterization of papain-like protease activity.";
RL J. Virol. 78:13600-13612(2004).
RN [24]
RP 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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
RP INTERACTION WITH ORF6 PROTEIN (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 [31]
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 [32]
RP FUNCTION (NON-STRUCTURAL PROTEIN 3).
RX PubMed=19369340; DOI=10.1128/jvi.02220-08;
RA Frieman M., Ratia K., Johnston R.E., Mesecar A.D., Baric R.S.;
RT "Severe acute respiratory syndrome coronavirus papain-like protease
RT ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and
RT NF-kappaB signaling.";
RL J. Virol. 83:6689-6705(2009).
RN [33]
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 [34]
RP FUNCTION (NON-STRUCTURAL PROTEIN 9).
RX PubMed=19153232; DOI=10.1128/jvi.01505-08;
RA Miknis Z.J., Donaldson E.F., Umland T.C., Rimmer R.A., Baric R.S.,
RA Schultz L.W.;
RT "Severe acute respiratory syndrome coronavirus nsp9 dimerization is
RT essential for efficient viral growth.";
RL J. Virol. 83:3007-3018(2009).
RN [35]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1).
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 [36]
RP INTERACTION WITH PAPAIN-LIKE PROTEASE NSP3 (NON-STRUCTURAL PROTEIN 4),
RP SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4), AND INTERACTION WITH
RP NON-STRUCTURAL PROTEIN 6 (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 [37]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1).
RX PubMed=23035226; DOI=10.1128/jvi.01958-12;
RA Lokugamage K.G., Narayanan K., Huang C., Makino S.;
RT "Severe acute respiratory syndrome coronavirus protein nsp1 is a novel
RT eukaryotic translation inhibitor that represses multiple steps of
RT translation initiation.";
RL J. Virol. 86:13598-13608(2012).
RN [38]
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 [39]
RP FUNCTION (NON-STRUCTURAL PROTEIN 10), AND INTERACTION WITH PROOFREADING
RP EXORIBONUCLEASE NSP14 (NON-STRUCTURAL PROTEIN 10).
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 [40]
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 [41]
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 [42]
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 [43]
RP FUNCTION (PAPAIN-LIKE PROTEASE NSP3).
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 [44]
RP INTERACTION WITH NUP93 (HOST TRANSLATION INHIBITOR NSP1), AND FUNCTION
RP (HOST TRANSLATION INHIBITOR NSP1).
RX PubMed=30943371; DOI=10.1139/bcb-2018-0394;
RA Gomez G.N., Abrar F., Dodhia M.P., Gonzalez F.G., Nag A.;
RT "SARS coronavirus protein nsp1 disrupts localization of Nup93 from the
RT nuclear pore complex.";
RL Biochem. Cell Biol. 97:758-766(2019).
RN [45]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1A), 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 [46]
RP 3D-STRUCTURE MODELING OF 3241-3540, AND CHARACTERIZATION (3C-LIKE
RP PROTEINASE NSP5).
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 [47]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4118-4230 (NON-STRUCTURAL PROTEIN
RP 9).
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 [48]
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 [49]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230.
RX PubMed=14962394; DOI=10.1016/j.str.2004.01.016;
RA Sutton G., Fry E., Carter L., Sainsbury S., Walter T., Nettleship J.,
RA Berrow N., Owens R., Gilbert R., Davidson A., Siddell S., Poon L.L.M.,
RA Diprose J., Alderton D., Walsh M., Grimes J.M., Stuart D.I.;
RT "The nsp9 replicase protein of SARS-coronavirus, structure and functional
RT insights.";
RL Structure 12:341-353(2004).
RN [50]
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 [51]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1002-1176.
RX PubMed=16271890; DOI=10.1016/j.str.2005.07.022;
RA Saikatendu K.S., Joseph J.S., Subramanian V., Clayton T., Griffith M.,
RA Moy K., Velasquez J., Neuman B.W., Buchmeier M.J., Stevens R.C., Kuhn P.;
RT "Structural basis of severe acute respiratory syndrome coronavirus ADP-
RT ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.";
RL Structure 13:1665-1675(2005).
RN [52]
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 [53]
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 [54]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4231-4378.
RX PubMed=16873247; DOI=10.1128/jvi.00483-06;
RA Su D., Lou Z., Sun F., Zhai Y., Yang H., Zhang R., Joachimiak A.,
RA Zhang X.C., Bartlam M., Rao Z.;
RT "Dodecamer structure of severe acute respiratory syndrome coronavirus
RT nonstructural protein nsp10.";
RL J. Virol. 80:7902-7908(2006).
RN [55]
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 [56]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3241-3546.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of Sars coronavirus main proteinase(3CLPRO).";
RL Submitted (JUL-2007) to the PDB data bank.
CC -!- FUNCTION: [Isoform Replicase polyprotein 1a]: 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. In addition,
CC PL-PRO possesses a deubiquitinating/deISGylating activity and processes
CC both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular
CC substrates (PubMed:17692280). Plays a role in host membrane
CC rearrangement that leads to creation of cytoplasmic double-membrane
CC vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3,
CC nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069,
CC PubMed:23943763). Antagonizes innate immune induction of type I
CC interferon by blocking the phosphorylation, dimerization and subsequent
CC nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840).
CC Prevents also host NF-kappa-B signaling (PubMed:19369340,
CC PubMed:24622840). {ECO:0000269|PubMed:16271890,
CC ECO:0000269|PubMed:17692280, ECO:0000269|PubMed:19369340,
CC ECO:0000269|PubMed:23943763, ECO:0000269|PubMed:24622840,
CC ECO:0000303|PubMed:24410069}.
CC -!- FUNCTION: [Non-structural protein 4]: Plays a role in host membrane
CC rearrangement that leads to creation of cytoplasmic double-membrane
CC vesicles (DMV) necessary for viral replication (PubMed:23943763,
CC PubMed:24410069). Alone appears incapable to induce membrane curvature,
CC but together with nsp3 is able to induce paired membranes
CC (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form
CC DMV (PubMed:23943763, PubMed:24410069). {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:23943763). Nsp3,
CC nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763,
CC PubMed:24410069). Plays a role in the initial induction of
CC autophagosomes from host reticulum endoplasmic. Later, limits the
CC expansion of these phagosomes that are no longer able to deliver viral
CC components to lysosomes (PubMed:24991833).
CC {ECO:0000269|PubMed:23943763, ECO:0000269|PubMed:24991833,
CC ECO:0000303|PubMed:24410069}.
CC -!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}.
CC -!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}.
CC -!- FUNCTION: [RNA-capping enzyme subunit nsp9]: Catalytic subunit of viral
CC RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction
CC for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12
CC transfers RNA to the amino terminus of NSP9, forming a covalent RNA-
CC protein intermediate. Subsequently, the NiRAN domain transfers RNA to
CC GDP, forming the core cap structure GpppA-RNA. The NSP14 and NSP16
CC methyltransferases then add methyl groups to form functional cap
CC structures. {ECO:0000250|UniProtKB:P0DTC1,
CC ECO:0000269|PubMed:19153232}.
CC -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
CC 2'-O-methyltransferase activities. Therefore plays an essential role in
CC viral mRNAs cap methylation. {ECO:0000269|PubMed:22635272}.
CC -!- CATALYTIC ACTIVITY: [3C-like proteinase nsp5]:
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: [RNA-capping enzyme subunit nsp9]:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000250|UniProtKB:P0DTC1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67014;
CC Evidence={ECO:0000250|UniProtKB:P0DTC1};
CC -!- COFACTOR: [Papain-like protease nsp3]:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16306590};
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 and non-structural protein 6. {ECO:0000269|PubMed:21345958}.
CC -!- SUBUNIT: [3C-like proteinase nsp5]: Exists as monomer and homodimer.
CC Only the homodimer shows catalytic activity.
CC {ECO:0000269|PubMed:14561748, 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: [RNA-capping enzyme subunit nsp9]: Homodimer.
CC {ECO:0000269|PubMed:19153232}.
CC -!- SUBUNIT: [Non-structural protein 10]: Homododecamer.
CC {ECO:0000269|PubMed:16873247}.
CC -!- INTERACTION:
CC P0C6U8; P0C6U8: 1a; NbExp=6; IntAct=EBI-15810860, EBI-15810860;
CC P0C6U8; PRO_0000338259 [P0C6U8]: 1a; NbExp=3; IntAct=EBI-15810860, EBI-25496008;
CC PRO_0000338257; P05161: ISG15; Xeno; NbExp=5; IntAct=EBI-25635190, EBI-746466;
CC PRO_0000338257; Q64339: Isg15; Xeno; NbExp=3; IntAct=EBI-25635190, EBI-8345781;
CC PRO_0000338257; L5LC70: MDA_GLEAN10007532; Xeno; NbExp=2; IntAct=EBI-25635190, EBI-25760965;
CC PRO_0000338257; Q9H074-2: PAIP1; Xeno; NbExp=7; IntAct=EBI-25635190, EBI-12101100;
CC PRO_0000338257; PRO_0000396474 [P62992]: RPS27A; Xeno; NbExp=2; IntAct=EBI-25635190, EBI-25820711;
CC PRO_0000338263; PRO_0000338263 [P0C6U8]: 1a; NbExp=4; IntAct=EBI-25610723, EBI-25610723;
CC PRO_0000338265; PRO_0000037310 [P0C6X7]: rep; NbExp=2; IntAct=EBI-25492625, EBI-25474098;
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:21345958, 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: [RNA-capping enzyme subunit nsp9]: Host
CC cytoplasm, host 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 -!- 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 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6U8-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6X7-1; Sequence=External;
CC -!- DOMAIN: [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 1a]: 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 6-11 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: [RNA-capping enzyme subunit nsp9]: 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}.
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DR EMBL; AY278741; AAP13439.1; -; Genomic_RNA.
DR EMBL; AY274119; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278554; AAP13575.1; -; Genomic_RNA.
DR EMBL; AY282752; AAP30712.1; -; Genomic_RNA.
DR EMBL; AY304495; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY304486; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY304488; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283795; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283796; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283797; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283798; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY286320; AAR16181.1; -; Genomic_RNA.
DR EMBL; AY278488; AAP30029.1; -; Genomic_RNA.
DR EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278489; AAP51226.1; -; Genomic_RNA.
DR EMBL; AY291451; AAP37016.1; -; Genomic_RNA.
DR EMBL; AY310120; AAP50484.1; -; Genomic_RNA.
DR EMBL; AY291315; AAP33695.1; -; Genomic_RNA.
DR EMBL; AY323977; AAP72974.2; -; Genomic_RNA.
DR EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY338174; AAQ01595.1; -; Genomic_RNA.
DR EMBL; AY338175; AAQ01607.1; -; Genomic_RNA.
DR EMBL; AY348314; AAP97880.1; -; Genomic_RNA.
DR EMBL; AP006557; BAC81347.1; -; Genomic_RNA.
DR EMBL; AP006558; BAC81361.1; -; Genomic_RNA.
DR EMBL; AP006559; BAC81375.1; -; Genomic_RNA.
DR EMBL; AP006560; BAC81389.1; -; Genomic_RNA.
DR EMBL; AP006561; BAC81403.1; -; Genomic_RNA.
DR EMBL; AY427439; AAQ94059.1; -; Genomic_RNA.
DR EMBL; AH012999; AAP82966.1; -; Genomic_RNA.
DR EMBL; AH012999; AAP82976.1; -; Genomic_RNA.
DR EMBL; AY463059; -; NOT_ANNOTATED_CDS; Genomic_RNA.
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=4231-4382.
DR PDB; 2GA6; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=4231-4382.
DR PDB; 2GDT; NMR; -; A=13-127.
DR PDB; 2GRI; NMR; -; A=819-930.
DR PDB; 2GT7; X-ray; 1.82 A; A/B=3241-3546.
DR PDB; 2GT8; X-ray; 2.00 A; A=3241-3546.
DR PDB; 2GTB; X-ray; 2.00 A; A=3241-3546.
DR PDB; 2GX4; X-ray; 1.93 A; A=3241-3546.
DR PDB; 2GZ7; X-ray; 1.86 A; A=3241-3546.
DR PDB; 2GZ8; X-ray; 1.97 A; A=3241-3546.
DR PDB; 2GZ9; X-ray; 2.17 A; A=3241-3546.
DR PDB; 2H2Z; X-ray; 1.60 A; A=3241-3546.
DR PDB; 2HOB; X-ray; 1.95 A; A=3241-3546.
DR PDB; 2HSX; NMR; -; A=13-127.
DR PDB; 2IDY; NMR; -; A=819-930.
DR PDB; 2KAF; NMR; -; A=1473-1538.
DR PDB; 2KQV; NMR; -; A=1345-1538.
DR PDB; 2KQW; NMR; -; A=1345-1538.
DR PDB; 2KYS; NMR; -; A=3837-3919.
DR PDB; 2LIZ; NMR; -; A=3427-3546.
DR PDB; 2OP9; X-ray; 1.80 A; A/B=3241-3541.
DR PDB; 2PWX; X-ray; 2.50 A; A=3241-3546.
DR PDB; 2W2G; X-ray; 2.22 A; A/B=1207-1470.
DR PDB; 2WCT; X-ray; 2.79 A; A/B/C/D=1207-1470.
DR PDB; 2Z3C; X-ray; 1.79 A; A=3241-3546.
DR PDB; 2Z3D; X-ray; 2.10 A; A=3241-3546.
DR PDB; 2Z3E; X-ray; 2.32 A; A=3241-3546.
DR PDB; 2ZU4; X-ray; 1.93 A; A=3241-3546.
DR PDB; 2ZU5; X-ray; 1.65 A; A=3241-3546.
DR PDB; 3ATW; X-ray; 2.36 A; A/B=3241-3546.
DR PDB; 3AVZ; X-ray; 2.46 A; A=3241-3546.
DR PDB; 3AW0; X-ray; 2.30 A; A=3241-3546.
DR PDB; 3AW1; X-ray; 2.00 A; A/B=3241-3546.
DR PDB; 3E91; X-ray; 2.55 A; A/B=3241-3546.
DR PDB; 3EA7; X-ray; 2.65 A; A/B=3241-3546.
DR PDB; 3EA8; X-ray; 2.25 A; A=3241-3546.
DR PDB; 3EA9; X-ray; 2.40 A; A=3241-3546.
DR PDB; 3EAJ; X-ray; 2.70 A; A/B=3241-3546.
DR PDB; 3EE7; X-ray; 2.60 A; A/B/C/D=4118-4230.
DR PDB; 3F9E; X-ray; 2.50 A; A=3241-3546.
DR PDB; 3F9F; X-ray; 2.30 A; A/B=3241-3546.
DR PDB; 3F9G; X-ray; 2.60 A; A/B=3241-3541.
DR PDB; 3F9H; X-ray; 2.90 A; A/B=3241-3546.
DR PDB; 3FZD; X-ray; 2.35 A; A=3241-3541.
DR PDB; 3IWM; X-ray; 3.20 A; A/B/C/D=3241-3546.
DR PDB; 3M3S; X-ray; 2.30 A; A/B=3241-3546.
DR PDB; 3M3T; X-ray; 2.90 A; A=3241-3546.
DR PDB; 3M3V; X-ray; 2.70 A; A/B=3241-3546.
DR PDB; 3MJ5; X-ray; 2.63 A; A/B=1541-1855.
DR PDB; 3R24; X-ray; 2.00 A; B=4240-4382.
DR PDB; 3SN8; X-ray; 1.99 A; A=3241-3546.
DR PDB; 3SNA; X-ray; 3.05 A; A=3241-3541.
DR PDB; 3SNB; X-ray; 2.40 A; A=3241-3546.
DR PDB; 3SNC; X-ray; 2.58 A; A=3241-3546.
DR PDB; 3SND; X-ray; 1.89 A; A/B=3241-3546.
DR PDB; 3SNE; X-ray; 2.60 A; A=3241-3546.
DR PDB; 3SZN; X-ray; 1.69 A; A=3241-3546.
DR PDB; 3TIT; X-ray; 1.99 A; A=3241-3546.
DR PDB; 3TIU; X-ray; 2.08 A; A=3241-3546.
DR PDB; 3TNS; X-ray; 1.99 A; A=3241-3546.
DR PDB; 3TNT; X-ray; 1.59 A; A=3241-3546.
DR PDB; 3V3M; X-ray; 1.96 A; A=3241-3546.
DR PDB; 3VB3; X-ray; 2.20 A; A/B=3241-3546.
DR PDB; 3VB4; X-ray; 2.20 A; A/B=3241-3546.
DR PDB; 3VB5; X-ray; 1.95 A; A/B=3241-3546.
DR PDB; 3VB6; X-ray; 2.50 A; A/B=3241-3546.
DR PDB; 3VB7; X-ray; 1.95 A; A/B=3241-3546.
DR PDB; 4HI3; X-ray; 2.09 A; A/B=3241-3546.
DR PDB; 4M0W; X-ray; 1.40 A; A=1541-1858.
DR PDB; 4MDS; X-ray; 1.60 A; A=3241-3542.
DR PDB; 4MM3; X-ray; 2.75 A; B=1541-1855.
DR PDB; 4OVZ; X-ray; 2.50 A; A/B=1541-1855.
DR PDB; 4OW0; X-ray; 2.10 A; A/B=1541-1855.
DR PDB; 5F22; X-ray; 2.15 A; A=3837-3919.
DR PDB; 5Y3E; X-ray; 1.65 A; A=1541-1854.
DR PDB; 5Y3Q; X-ray; 1.65 A; A=1541-1854.
DR PDB; 6LNY; X-ray; 2.25 A; A=3241-3546.
DR PDB; 6LO0; X-ray; 1.94 A; A=3241-3546.
DR PDB; 6NUR; EM; 3.10 A; B/D=3920-4117.
DR PDB; 6NUS; EM; 3.50 A; B=3920-4117.
DR PDB; 6W2A; X-ray; 1.65 A; A/B=3241-3543.
DR PDB; 6XHL; X-ray; 1.47 A; A/B=3241-3546.
DR PDB; 6XHN; X-ray; 1.38 A; A/B=3241-3546.
DR PDB; 6XHO; X-ray; 1.45 A; A/B=3241-3546.
DR PDB; 6Y7M; X-ray; 1.90 A; AAA=3241-3546.
DR PDB; 6YXJ; X-ray; 3.50 A; A=1207-1344.
DR PDB; 7DQZ; X-ray; 1.99 A; A/B=3241-3546.
DR PDB; 7END; X-ray; 1.99 A; A=3241-3546.
DR PDB; 7EO8; X-ray; 2.28 A; A/B=3241-3546.
DR PDB; 7FA1; X-ray; 1.60 A; A=181-456.
DR PDB; 7FAC; X-ray; 2.71 A; A=292-818.
DR PDB; 7K0G; X-ray; 1.85 A; A=3241-3543.
DR PDB; 7K0H; X-ray; 1.70 A; A/B=3241-3543.
DR PDB; 7LFU; X-ray; 2.29 A; D=1541-1856.
DR PDB; 7LFV; X-ray; 2.23 A; A/B=1541-1856.
DR PDB; 7LMG; X-ray; 1.60 A; AAA=3241-3546.
DR PDB; 7LMH; X-ray; 1.85 A; AAA=3241-3546.
DR PDB; 7LMI; X-ray; 1.71 A; AAA=3241-3546.
DR PDB; 7LMJ; X-ray; 1.69 A; AAA=3241-3546.
DR PDB; 7OPL; EM; 4.12 A; E=13-127.
DR PDB; 7RC1; X-ray; 1.63 A; A=3241-3546.
DR PDB; 7VLO; X-ray; 2.02 A; A/B=3242-3540.
DR PDB; 7WQI; X-ray; 1.93 A; A/B=3242-3540.
DR PDB; 7XAX; X-ray; 2.25 A; A/B=3241-3546.
DR PDB; 7YGQ; X-ray; 2.04 A; A/B=3242-3539.
DR PDB; 7ZQW; X-ray; 2.53 A; A=3241-3546.
DR PDB; 8HUS; X-ray; 1.97 A; A/B=3242-3539.
DR PDB; 8UFL; X-ray; 2.51 A; A/B=1207-1470.
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; 2HOB; -.
DR PDBsum; 2HSX; -.
DR PDBsum; 2IDY; -.
DR PDBsum; 2KAF; -.
DR PDBsum; 2KQV; -.
DR PDBsum; 2KQW; -.
DR PDBsum; 2KYS; -.
DR PDBsum; 2LIZ; -.
DR PDBsum; 2OP9; -.
DR PDBsum; 2PWX; -.
DR PDBsum; 2W2G; -.
DR PDBsum; 2WCT; -.
DR PDBsum; 2Z3C; -.
DR PDBsum; 2Z3D; -.
DR PDBsum; 2Z3E; -.
DR PDBsum; 2ZU4; -.
DR PDBsum; 2ZU5; -.
DR PDBsum; 3ATW; -.
DR PDBsum; 3AVZ; -.
DR PDBsum; 3AW0; -.
DR PDBsum; 3AW1; -.
DR PDBsum; 3E91; -.
DR PDBsum; 3EA7; -.
DR PDBsum; 3EA8; -.
DR PDBsum; 3EA9; -.
DR PDBsum; 3EAJ; -.
DR PDBsum; 3EE7; -.
DR PDBsum; 3F9E; -.
DR PDBsum; 3F9F; -.
DR PDBsum; 3F9G; -.
DR PDBsum; 3F9H; -.
DR PDBsum; 3FZD; -.
DR PDBsum; 3IWM; -.
DR PDBsum; 3M3S; -.
DR PDBsum; 3M3T; -.
DR PDBsum; 3M3V; -.
DR PDBsum; 3MJ5; -.
DR PDBsum; 3R24; -.
DR PDBsum; 3SN8; -.
DR PDBsum; 3SNA; -.
DR PDBsum; 3SNB; -.
DR PDBsum; 3SNC; -.
DR PDBsum; 3SND; -.
DR PDBsum; 3SNE; -.
DR PDBsum; 3SZN; -.
DR PDBsum; 3TIT; -.
DR PDBsum; 3TIU; -.
DR PDBsum; 3TNS; -.
DR PDBsum; 3TNT; -.
DR PDBsum; 3V3M; -.
DR PDBsum; 3VB3; -.
DR PDBsum; 3VB4; -.
DR PDBsum; 3VB5; -.
DR PDBsum; 3VB6; -.
DR PDBsum; 3VB7; -.
DR PDBsum; 4HI3; -.
DR PDBsum; 4M0W; -.
DR PDBsum; 4MDS; -.
DR PDBsum; 4MM3; -.
DR PDBsum; 4OVZ; -.
DR PDBsum; 4OW0; -.
DR PDBsum; 5F22; -.
DR PDBsum; 5Y3E; -.
DR PDBsum; 5Y3Q; -.
DR PDBsum; 6LNY; -.
DR PDBsum; 6LO0; -.
DR PDBsum; 6NUR; -.
DR PDBsum; 6NUS; -.
DR PDBsum; 6W2A; -.
DR PDBsum; 6XHL; -.
DR PDBsum; 6XHN; -.
DR PDBsum; 6XHO; -.
DR PDBsum; 6Y7M; -.
DR PDBsum; 6YXJ; -.
DR PDBsum; 7DQZ; -.
DR PDBsum; 7END; -.
DR PDBsum; 7EO8; -.
DR PDBsum; 7FA1; -.
DR PDBsum; 7FAC; -.
DR PDBsum; 7K0G; -.
DR PDBsum; 7K0H; -.
DR PDBsum; 7LFU; -.
DR PDBsum; 7LFV; -.
DR PDBsum; 7LMG; -.
DR PDBsum; 7LMH; -.
DR PDBsum; 7LMI; -.
DR PDBsum; 7LMJ; -.
DR PDBsum; 7OPL; -.
DR PDBsum; 7RC1; -.
DR PDBsum; 7VLO; -.
DR PDBsum; 7WQI; -.
DR PDBsum; 7XAX; -.
DR PDBsum; 7YGQ; -.
DR PDBsum; 7ZQW; -.
DR PDBsum; 8HUS; -.
DR PDBsum; 8UFL; -.
DR BMRB; P0C6U8; -.
DR EMDB; EMD-0520; -.
DR EMDB; EMD-0521; -.
DR EMDB; EMD-13020; -.
DR SASBDB; P0C6U8; -.
DR SMR; P0C6U8; -.
DR BioGRID; 4383931; 1.
DR BioGRID; 4383933; 1.
DR BioGRID; 4383934; 5.
DR BioGRID; 4383935; 2.
DR BioGRID; 4383936; 2.
DR BioGRID; 4383937; 4.
DR DIP; DIP-48580N; -.
DR IntAct; P0C6U8; 20.
DR BindingDB; P0C6U8; -.
DR ChEMBL; CHEMBL3927; -.
DR DrugBank; DB07620; 2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE.
DR DrugBank; DB08732; NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE.
DR DrugBank; DB07743; S-[5-(TRIFLUOROMETHYL)-4H-1,2,4-TRIAZOL-3-YL] 5-(PHENYLETHYNYL)FURAN-2-CARBOTHIOATE.
DR MEROPS; C16.009; -.
DR MEROPS; C30.005; -.
DR BRENDA; 3.4.22.69; 7599.
DR BRENDA; 3.4.22.B50; 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 Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses.
DR Reactome; R-HSA-9735869; SARS-CoV-1 modulates host translation machinery.
DR SABIO-RK; P0C6U8; -.
DR EvolutionaryTrace; P0C6U8; -.
DR Proteomes; UP000000354; Segment.
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:0062243; C:double membrane vesicle viral factory outer membrane; TAS:Reactome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; 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:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1990380; F:K48-linked deubiquitinase activity; EXP:Reactome.
DR GO; GO:0061578; F:K63-linked deubiquitinase activity; EXP:Reactome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; TAS:Reactome.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; TAS:Reactome.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21516; betaCoV_Nsp2_SARS-like; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd21827; betaCoV_Nsp7; 1.
DR CDD; cd21831; betaCoV_Nsp8; 1.
DR CDD; cd21898; betaCoV_Nsp9; 1.
DR CDD; cd21732; betaCoV_PLPro; 1.
DR CDD; cd21872; CoV_Nsp10; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR CDD; cd21562; Macro_cv_SUD-N_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd22662; SARS-CoV-like_Nsp1_C; 1.
DR CDD; cd21796; SARS-CoV-like_Nsp1_N; 1.
DR CDD; cd21814; SARS-CoV-like_Nsp3_betaSM; 1.
DR CDD; cd21822; SARS-CoV-like_Nsp3_NAB; 1.
DR CDD; cd21525; SUD_C_SARS-CoV_Nsp3; 1.
DR CDD; cd21717; TM_Y_SARS-CoV-like_Nsp3_C; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR Gene3D; 1.10.8.1190; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 6.10.140.2090; -; 1.
DR Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR Gene3D; 3.40.30.150; Coronavirus polyprotein cleavage domain; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR Gene3D; 3.40.220.20; Nsp3, SUD-M subdomain; 1.
DR Gene3D; 3.40.220.30; Nsp3, SUD-N subdomain; 1.
DR Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR Gene3D; 3.40.50.11020; Replicase polyprotein, nucleic acid-binding domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR046443; a/bCoV_NSP1_glob.
DR InterPro; IPR046442; bCoV_NSP1_C.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR047573; CoV_NSP2_M.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR047566; CoV_NSP3_Y3.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR021590; NSP1_glob_bCoV.
DR InterPro; IPR038030; NSP1_glob_sf_bCoV.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044389; NSP2_SARS-CoV-like.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR047567; NSP3_G2M_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; 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; IPR018995; RNA_synth_NSP10_CoV.
DR Pfam; PF16251; bCoV_NAB; 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; PF09401; CoV_NSP10; 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; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF144246; Coronavirus NSP10-like; 1.
DR SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF159936; NSP3A-like; 1.
DR SUPFAM; SSF101816; Replicase NSP9; 1.
DR SUPFAM; SSF160099; SARS Nsp1-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; PS51993; COV_3ECTO; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51962; COV_NSP1; 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_Y; 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; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
DR PROSITE; PS51940; SARS_NSP3C_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus;
KW Decay of host mRNAs by virus; Disulfide bond; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW 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 IRF3 by virus; Inhibition of host ISG15 by virus;
KW Inhibition of host RLR pathway by virus;
KW Interferon antiviral system evasion; Lyase; Membrane; Metal-binding;
KW Methyltransferase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Nuclease; Protease;
KW Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..4382
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338254"
FT CHAIN 1..180
FT /note="Host translation inhibitor nsp1"
FT /id="PRO_0000338255"
FT CHAIN 181..818
FT /note="Non-structural protein 2"
FT /id="PRO_0000338256"
FT CHAIN 819..2740
FT /note="Papain-like protease nsp3"
FT /id="PRO_0000338257"
FT CHAIN 2741..3240
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338258"
FT CHAIN 3241..3546
FT /note="3C-like proteinase nsp5"
FT /id="PRO_0000338259"
FT CHAIN 3547..3836
FT /note="Non-structural protein 6"
FT /id="PRO_0000338260"
FT CHAIN 3837..3919
FT /note="Non-structural protein 7"
FT /id="PRO_0000338261"
FT CHAIN 3920..4117
FT /note="Non-structural protein 8"
FT /id="PRO_0000338262"
FT CHAIN 4118..4230
FT /note="RNA-capping enzyme subunit nsp9"
FT /id="PRO_0000338263"
FT CHAIN 4231..4369
FT /note="Non-structural protein 10"
FT /id="PRO_0000338264"
FT CHAIN 4370..4382
FT /note="Non-structural protein 11"
FT /id="PRO_0000338265"
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..4382
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 2224..2294
FT /note="3Ecto"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT DOMAIN 2372..2740
FT /note="CoV Nsp3 Y"
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 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 2372..2462
FT /note="Y1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2376..2389
FT /note="ZF1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2422..2432
FT /note="ZF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2463..2740
FT /note="CoV-Y"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2463..2557
FT /note="Y2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2558..2639
FT /note="Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2640..2740
FT /note="Y4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
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 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 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:0000255|PROSITE-ProRule:PRU00444,
FT ECO:0000269|PubMed:16306590"
FT ACT_SITE 3281
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772,
FT ECO:0000269|PubMed:16306590"
FT ACT_SITE 3385
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
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 1729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1766
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 2376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 4304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
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 DISULFID 2240..2268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT DISULFID 2259..2265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT VARIANT 82
FT /note="G -> C (in strain: Isolate GD01)"
FT VARIANT 130
FT /note="G -> R (in strain: Isolate GD01)"
FT VARIANT 138
FT /note="I -> T (in strain: Isolate SZ16)"
FT VARIANT 181
FT /note="A -> V (in strain: Isolate Shanghai LY)"
FT VARIANT 225
FT /note="K -> Q (in strain: Isolate GD01)"
FT VARIANT 249
FT /note="Y -> C (in strain: Isolate Shanghai LY)"
FT VARIANT 306
FT /note="V -> F (in strain: Isolate BJ04)"
FT VARIANT 549
FT /note="A -> S (in strain: Isolate SZ3)"
FT VARIANT 765
FT /note="A -> T (in strain: Isolate FRA and Isolate
FT Frankfurt-1)"
FT VARIANT 852
FT /note="K -> R (in strain: Isolate SZ16)"
FT VARIANT 1004
FT /note="N -> H (in strain: Isolate BJ03)"
FT VARIANT 1021
FT /note="V -> A (in strain: Isolate SZ3 and Isolate SZ16)"
FT VARIANT 1023
FT /note="I -> T (in strain: Isolate Shanghai QXC1)"
FT VARIANT 1121
FT /note="I -> T (in strain: Isolate GD01, Isolate SZ3 and
FT Isolate SZ16)"
FT VARIANT 1136
FT /note="P -> L (in strain: Isolate SZ3 and Isolate SZ16)"
FT VARIANT 1257
FT /note="K -> E (in strain: Isolate Shanghai QXC1)"
FT VARIANT 1319
FT /note="K -> R (in strain: Isolate GD01)"
FT VARIANT 1329
FT /note="F -> S (in strain: Isolate GD01)"
FT VARIANT 1361
FT /note="T -> A (in strain: Isolate Shanghai QXC1)"
FT VARIANT 1385
FT /note="I -> V (in strain: Isolate Shanghai QXC1)"
FT VARIANT 1538
FT /note="S -> T (in strain: Isolate GD01)"
FT VARIANT 1563
FT /note="M -> K (in strain: Isolate BJ02)"
FT VARIANT 1663
FT /note="L -> I (in strain: Isolate SZ3 and Isolate SZ16)"
FT VARIANT 1762
FT /note="I -> L (in strain: Isolate BJ03)"
FT VARIANT 1776..1777
FT /note="QQ -> PP (in strain: Isolate BJ03)"
FT VARIANT 1790
FT /note="E -> G (in strain: Isolate Shanghai QXC1)"
FT VARIANT 1806
FT /note="G -> V (in strain: Isolate BJ02)"
FT VARIANT 1962
FT /note="L -> I (in strain: Isolate BJ04)"
FT VARIANT 2116
FT /note="L -> F (in strain: Isolate GD01, Isolate SZ3 and
FT Isolate SZ16)"
FT VARIANT 2222
FT /note="C -> Y (in strain: Isolate GD01, Isolate SZ3 and
FT Isolate SZ16)"
FT VARIANT 2269
FT /note="L -> S (in strain: Isolate SZ3 and Isolate SZ16)"
FT VARIANT 2326
FT /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT VARIANT 2392..2394
FT /note="RNR -> CNH (in strain: Isolate Shanghai QXC1)"
FT VARIANT 2480
FT /note="L -> P (in strain: Isolate Shanghai QXC1)"
FT VARIANT 2552
FT /note="A -> V (in strain: Isolate Urbani and Isolate Taiwan
FT TC2)"
FT VARIANT 2556
FT /note="D -> N (in strain: Isolate HKU-39849)"
FT VARIANT 2564
FT /note="S -> P (in strain: Isolate GD01)"
FT VARIANT 2648
FT /note="N -> Y (in strain: Isolate Shanghai QXC1)"
FT VARIANT 2708
FT /note="S -> T (in strain: Isolate HKU-39849)"
FT VARIANT 2718
FT /note="R -> T (in strain: Isolate HKU-39849)"
FT VARIANT 2746
FT /note="C -> W (in strain: Isolate SZ3 and Isolate SZ16)"
FT VARIANT 2770
FT /note="V -> L (in strain: Isolate BJ01 and Isolate BJ02)"
FT VARIANT 2944
FT /note="T -> I (in strain: Isolate SIN2500, Isolate GD01 and
FT Isolate GZ50)"
FT VARIANT 2971
FT /note="V -> A (in strain: Isolate GD01 and Isolate SZ16)"
FT VARIANT 3020
FT /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT VARIANT 3047
FT /note="V -> A (in strain: Isolate CUHK-W1, Isolate GD01,
FT Isolate SZ3, Isolate SZ16, Isolate BJ01, Isolate BJ02,
FT Isolate BJ03 and Isolate Shanghai QXC1)"
FT VARIANT 3072
FT /note="V -> A (in strain: Isolate CUHK-W1, Isolate SZ3,
FT Isolate SZ16 and Isolate GD01)"
FT VARIANT 3197
FT /note="A -> V (in strain: Isolate BJ01, Isolate BJ02,
FT Isolate BJ03, Isolate BJ04 and Isolate Shanghai QXC1)"
FT VARIANT 3429
FT /note="Q -> P (in strain: Isolate BJ02)"
FT VARIANT 3488
FT /note="D -> E (in strain: Isolate BJ04)"
FT VARIANT 3717
FT /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT VARIANT 3818
FT /note="N -> T (in strain: Isolate BJ04)"
FT VARIANT 3903
FT /note="D -> N (in strain: Isolate BJ03)"
FT VARIANT 3904
FT /note="I -> F (in strain: Isolate BJ02)"
FT VARIANT 3911
FT /note="M -> V (in strain: Isolate Shanghai QXC1)"
FT VARIANT 4001
FT /note="K -> Q (in strain: Isolate Shanghai LY)"
FT VARIANT 4003
FT /note="T -> A (in strain: Isolate Shanghai LY)"
FT VARIANT 4085
FT /note="I -> H (in strain: Isolate ZJ01)"
FT VARIANT 4114
FT /note="V -> A (in strain: Isolate Shanghai QXC1)"
FT VARIANT 4202
FT /note="V -> M (in strain: Isolate Shanghai QXC1)"
FT VARIANT 4240
FT /note="N -> H (in strain: Isolate ZJ01)"
FT VARIANT 4296
FT /note="E -> G (in strain: Isolate Shanghai QXC1)"
FT VARIANT 4377..4378
FT /note="LN -> FK (in strain: Isolate Shanghai QXC1)"
FT STRAND 1208..1211
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1214..1216
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1219..1222
FT /evidence="ECO:0007829|PDB:2W2G"
FT TURN 1223..1225
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1229..1233
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1241..1244
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1253..1255
FT /evidence="ECO:0007829|PDB:2W2G"
FT TURN 1256..1258
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1266..1269
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1272..1276
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1280..1282
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1286..1293
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1298..1303
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1315..1324
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1325..1331
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1343..1345
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1351..1361
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1364..1368
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1372..1381
FT /evidence="ECO:0007829|PDB:2W2G"
FT TURN 1382..1384
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1389..1401
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1403..1405
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1407..1417
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1421..1423
FT /evidence="ECO:0007829|PDB:2W2G"
FT TURN 1429..1431
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1435..1442
FT /evidence="ECO:0007829|PDB:2W2G"
FT STRAND 1449..1452
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1456..1467
FT /evidence="ECO:0007829|PDB:2W2G"
FT HELIX 1473..1484
FT /evidence="ECO:0007829|PDB:2KAF"
FT STRAND 1485..1487
FT /evidence="ECO:0007829|PDB:2KQW"
FT STRAND 1500..1506
FT /evidence="ECO:0007829|PDB:2KAF"
FT STRAND 1509..1513
FT /evidence="ECO:0007829|PDB:2KAF"
FT STRAND 1515..1518
FT /evidence="ECO:0007829|PDB:2KAF"
FT STRAND 1521..1523
FT /evidence="ECO:0007829|PDB:2KAF"
FT STRAND 1526..1528
FT /evidence="ECO:0007829|PDB:2KQW"
FT HELIX 1530..1537
FT /evidence="ECO:0007829|PDB:2KAF"
FT STRAND 1544..1555
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1557..1562
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1563..1565
FT /evidence="ECO:0007829|PDB:4OVZ"
FT HELIX 1567..1570
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1571..1576
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 1581..1583
FT /evidence="ECO:0007829|PDB:4OW0"
FT HELIX 1588..1590
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1594..1597
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 1602..1612
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 1619..1630
FT /evidence="ECO:0007829|PDB:4M0W"
FT TURN 1648..1650
FT /evidence="ECO:0007829|PDB:4OW0"
FT HELIX 1651..1660
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1667..1669
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 1670..1680
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 1685..1695
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 1705..1713
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1722..1729
FT /evidence="ECO:0007829|PDB:4M0W"
FT TURN 1730..1732
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1733..1740
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 1741..1744
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1746..1749
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 1753..1758
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1760..1763
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1767..1794
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1799..1806
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1811..1826
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1829..1846
FT /evidence="ECO:0007829|PDB:4M0W"
FT STRAND 1848..1851
FT /evidence="ECO:0007829|PDB:4M0W"
FT HELIX 3251..3254
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3257..3262
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3265..3272
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3275..3279
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3280..3283
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3288..3290
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3294..3299
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3303..3305
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3307..3310
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3313..3315
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3317..3323
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3326..3333
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3340..3343
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3351..3358
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3361..3370
FT /evidence="ECO:0007829|PDB:6XHN"
FT TURN 3380..3383
FT /evidence="ECO:0007829|PDB:3F9F"
FT STRAND 3388..3393
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3396..3406
FT /evidence="ECO:0007829|PDB:6XHN"
FT TURN 3408..3410
FT /evidence="ECO:0007829|PDB:3F9E"
FT STRAND 3412..3415
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3417..3419
FT /evidence="ECO:0007829|PDB:3F9G"
FT STRAND 3421..3424
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3427..3430
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3441..3453
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3467..3476
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3484..3489
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3491..3497
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3501..3514
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3521..3523
FT /evidence="ECO:0007829|PDB:3F9E"
FT STRAND 3524..3526
FT /evidence="ECO:0007829|PDB:6XHN"
FT HELIX 3533..3540
FT /evidence="ECO:0007829|PDB:6XHN"
FT STRAND 3541..3543
FT /evidence="ECO:0007829|PDB:2LIZ"
FT HELIX 3838..3855
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 3858..3860
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 3862..3877
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 3881..3896
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 3904..3913
FT /evidence="ECO:0007829|PDB:5F22"
FT HELIX 3997..4017
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4020..4027
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4029..4032
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4036..4038
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4040..4043
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4045..4053
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4054..4058
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4063..4068
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4071..4079
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4088..4090
FT /evidence="ECO:0007829|PDB:6NUR"
FT HELIX 4096..4098
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4101..4109
FT /evidence="ECO:0007829|PDB:6NUR"
FT STRAND 4127..4136
FT /evidence="ECO:0007829|PDB:3EE7"
FT TURN 4137..4139
FT /evidence="ECO:0007829|PDB:3EE7"
FT STRAND 4142..4150
FT /evidence="ECO:0007829|PDB:3EE7"
FT STRAND 4157..4164
FT /evidence="ECO:0007829|PDB:3EE7"
FT STRAND 4170..4173
FT /evidence="ECO:0007829|PDB:3EE7"
FT STRAND 4180..4186
FT /evidence="ECO:0007829|PDB:3EE7"
FT STRAND 4190..4194
FT /evidence="ECO:0007829|PDB:3EE7"
FT STRAND 4201..4208
FT /evidence="ECO:0007829|PDB:3EE7"
FT HELIX 4213..4224
FT /evidence="ECO:0007829|PDB:3EE7"
FT HELIX 4240..4248
FT /evidence="ECO:0007829|PDB:2FYG"
FT STRAND 4250..4252
FT /evidence="ECO:0007829|PDB:2FYG"
FT HELIX 4253..4262
FT /evidence="ECO:0007829|PDB:2FYG"
FT STRAND 4273..4275
FT /evidence="ECO:0007829|PDB:2G9T"
FT STRAND 4284..4288
FT /evidence="ECO:0007829|PDB:2FYG"
FT STRAND 4295..4299
FT /evidence="ECO:0007829|PDB:2FYG"
FT HELIX 4301..4303
FT /evidence="ECO:0007829|PDB:2FYG"
FT HELIX 4305..4309
FT /evidence="ECO:0007829|PDB:2FYG"
FT STRAND 4314..4318
FT /evidence="ECO:0007829|PDB:3R24"
FT TURN 4321..4324
FT /evidence="ECO:0007829|PDB:2GA6"
FT STRAND 4325..4330
FT /evidence="ECO:0007829|PDB:2FYG"
FT HELIX 4331..4333
FT /evidence="ECO:0007829|PDB:2FYG"
FT HELIX 4337..4343
FT /evidence="ECO:0007829|PDB:2FYG"
FT TURN 4348..4350
FT /evidence="ECO:0007829|PDB:2FYG"
FT TURN 4354..4356
FT /evidence="ECO:0007829|PDB:2FYG"
SQ SEQUENCE 4382 AA; 486373 MW; E1F65D5FD5DFF828 CRC64;
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT CGLVELEKGV
LPQLEQPYVF IKRSDALSTN HGHKVVELVA EMDGIQYGRS GITLGVLVPH VGETPIAYRN
VLLRKNGNKG AGGHSYGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGAL RELTRELNGG
AVTRYVDNNF CGPDGYPLDC IKDFLARAGK SMCTLSEQLD YIESKRGVYC CRDHEHEIAW
FTERSDKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVASPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEHCGTENLV IEGPTTCGYL
PTNAVVKMPC PACQDPEIGP EHSVADYHNH SNIETRLRKG GRTRCFGGCV FAYVGCYNKR
AYWVPRASAD IGSGHTGITG DNVETLNEDL LEILSRERVN INIVGDFHLN EEVAIILASF
SASTSAFIDT IKSLDYKSFK TIVESCGNYK VTKGKPVKGA WNIGQQRSVL TPLCGFPSQA
AGVIRSIFAR TLDAANHSIP DLQRAAVTIL DGISEQSLRL VDAMVYTSDL LTNSVIIMAY
VTGGLVQQTS QWLSNLLGTT VEKLRPIFEW IEAKLSAGVE FLKDAWEILK FLITGVFDIV
KGQIQVASDN IKDCVKCFID VVNKALEMCI DQVTIAGAKL RSLNLGEVFI AQSKGLYRQC
IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV LTSEEVVLKN GELEALETPV DSFTNGAIVG
TPVCVNGLML LEIKDKEQYC ALSPGLLATN NVFRLKGGAP IKGVTFGEDT VWEVQGYKNV
RITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
WSVATFYLFD DAGEENFSSR MYCSFYPPDE EEEDDAECEE EEIDETCEHE YGTEDDYQGL
PLEFGASAET VRVEEEEEED WLDDTTEQSE IEPEPEPTPE EPVNQFTGYL KLTDNVAIKC
VDIVKEAQSA NPMVIVNAAN IHLKHGGGVA GALNKATNGA MQKESDDYIK LNGPLTVGGS
CLLSGHNLAK KCLHVVGPNL NAGEDIQLLK AAYENFNSQD ILLAPLLSAG IFGAKPLQSL
QVCVQTVRTQ VYIAVNDKAL YEQVVMDYLD NLKPRVEAPK QEEPPNTEDS KTEEKSVVQK
PVDVKPKIKA CIDEVTTTLE ETKFLTNKLL LFADINGKLY HDSQNMLRGE DMSFLEKDAP
YMVGDVITSG DITCVVIPSK KAGGTTEMLS RALKKVPVDE YITTYPGQGC AGYTLEEAKT
ALKKCKSAFY VLPSEAPNAK EEILGTVSWN LREMLAHAEE TRKLMPICMD VRAIMATIQR
KYKGIKIQEG IVDYGVRFFF YTSKEPVASI ITKLNSLNEP LVTMPIGYVT HGFNLEEAAR
CMRSLKAPAV VSVSSPDAVT TYNGYLTSSS KTSEEHFVET VSLAGSYRDW SYSGQRTELG
VEFLKRGDKI VYHTLESPVE FHLDGEVLSL DKLKSLLSLR EVKTIKVFTT VDNTNLHTQL
VDMSMTYGQQ FGPTYLDGAD VTKIKPHVNH EGKTFFVLPS DDTLRSEAFE YYHTLDESFL
GRYMSALNHT KKWKFPQVGG LTSIKWADNN CYLSSVLLAL QQLEVKFNAP ALQEAYYRAR
AGDAANFCAL ILAYSNKTVG ELGDVRETMT HLLQHANLES AKRVLNVVCK HCGQKTTTLT
GVEAVMYMGT LSYDNLKTGV SIPCVCGRDA TQYLVQQESS FVMMSAPPAE YKLQQGTFLC
ANEYTGNYQC GHYTHITAKE TLYRIDGAHL TKMSEYKGPV TDVFYKETSY TTTIKPVSYK
LDGVTYTEIE PKLDGYYKKD NAYYTEQPID LVPTQPLPNA SFDNFKLTCS NTKFADDLNQ
MTGFTKPASR ELSVTFFPDL NGDVVAIDYR HYSASFKKGA KLLHKPIVWH INQATTKTTF
KPNTWCLRCL WSTKPVDTSN SFEVLAVEDT QGMDNLACES QQPTSEEVVE NPTIQKEVIE
CDVKTTEVVG NVILKPSDEG VKVTQELGHE DLMAAYVENT SITIKKPNEL SLALGLKTIA
THGIAAINSV PWSKILAYVK PFLGQAAITT SNCAKRLAQR VFNNYMPYVF TLLFQLCTFT
KSTNSRIRAS LPTTIAKNSV KSVAKLCLDA GINYVKSPKF SKLFTIAMWL LLLSICLGSL
ICVTAAFGVL LSNFGAPSYC NGVRELYLNS SNVTTMDFCE GSFPCSICLS GLDSLDSYPA
LETIQVTISS YKLDLTILGL AAEWVLAYML FTKFFYLLGL SAIMQVFFGY FASHFISNSW
LMWFIISIVQ MAPVSAMVRM YIFFASFYYI WKSYVHIMDG CTSSTCMMCY KRNRATRVEC
TTIVNGMKRS FYVYANGGRG FCKTHNWNCL NCDTFCTGST FISDEVARDL SLQFKRPINP
TDQSSYIVDS VAVKNGALHL YFDKAGQKTY ERHPLSHFVN LDNLRANNTK GSLPINVIVF
DGKSKCDESA SKSASVYYSQ LMCQPILLLD QALVSDVGDS TEVSVKMFDA YVDTFSATFS
VPMEKLKALV ATAHSELAKG VALDGVLSTF VSAARQGVVD TDVDTKDVIE CLKLSHHSDL
EVTGDSCNNF MLTYNKVENM TPRDLGACID CNARHINAQV AKSHNVSLIW NVKDYMSLSE
QLRKQIRSAA KKNNIPFRLT CATTRQVVNV ITTKISLKGG KIVSTCFKLM LKATLLCVLA
ALVCYIVMPV HTLSIHDGYT NEIIGYKAIQ DGVTRDIIST DDCFANKHAG FDAWFSQRGG
SYKNDKSCPV VAAIITREIG FIVPGLPGTV LRAINGDFLH FLPRVFSAVG NICYTPSKLI
EYSDFATSAC VLAAECTIFK DAMGKPVPYC YDTNLLEGSI SYSELRPDTR YVLMDGSIIQ
FPNTYLEGSV RVVTTFDAEY CRHGTCERSE VGICLSTSGR WVLNNEHYRA LSGVFCGVDA
MNLIANIFTP LVQPVGALDV SASVVAGGII AILVTCAAYY FMKFRRVFGE YNHVVAANAL
LFLMSFTILC LVPAYSFLPG VYSVFYLYLT FYFTNDVSFL AHLQWFAMFS PIVPFWITAI
YVFCISLKHC HWFFNNYLRK RVMFNGVTFS TFEEAALCTF LLNKEMYLKL RSETLLPLTQ
YNRYLALYNK YKYFSGALDT TSYREAACCH LAKALNDFSN SGADVLYQPP QTSITSAVLQ
SGFRKMAFPS GKVEGCMVQV TCGTTTLNGL WLDDTVYCPR HVICTAEDML NPNYEDLLIR
KSNHSFLVQA GNVQLRVIGH SMQNCLLRLK VDTSNPKTPK YKFVRIQPGQ TFSVLACYNG
SPSGVYQCAM RPNHTIKGSF LNGSCGSVGF NIDYDCVSFC YMHHMELPTG VHAGTDLEGK
FYGPFVDRQT AQAAGTDTTI TLNVLAWLYA AVINGDRWFL NRFTTTLNDF NLVAMKYNYE
PLTQDHVDIL GPLSAQTGIA VLDMCAALKE LLQNGMNGRT ILGSTILEDE FTPFDVVRQC
SGVTFQGKFK KIVKGTHHWM LLTFLTSLLI LVQSTQWSLF FFVYENAFLP FTLGIMAIAA
CAMLLVKHKH AFLCLFLLPS LATVAYFNMV YMPASWVMRI MTWLELADTS LSGYRLKDCV
MYASALVLLI LMTARTVYDD AARRVWTLMN VITLVYKVYY GNALDQAISM WALVISVTSN
YSGVVTTIMF LARAIVFVCV EYYPLLFITG NTLQCIMLVY CFLGYCCCCY FGLFCLLNRY
FRLTLGVYDY LVSTQEFRYM NSQGLLPPKS SIDAFKLNIK LLGIGGKPCI KVATVQSKMS
DVKCTSVVLL SVLQQLRVES SSKLWAQCVQ LHNDILLAKD TTEAFEKMVS LLSVLLSMQG
AVDINRLCEE MLDNRATLQA IASEFSSLPS YAAYATAQEA YEQAVANGDS EVVLKKLKKS
LNVAKSEFDR DAAMQRKLEK MADQAMTQMY KQARSEDKRA KVTSAMQTML FTMLRKLDND
ALNNIINNAR DGCVPLNIIP LTTAAKLMVV VPDYGTYKNT CDGNTFTYAS ALWEIQQVVD
ADSKIVQLSE INMDNSPNLA WPLIVTALRA NSAVKLQNNE LSPVALRQMS CAAGTTQTAC
TDDNALAYYN NSKGGRFVLA LLSDHQDLKW ARFPKSDGTG TIYTELEPPC RFVTDTPKGP
KVKYLYFIKG LNNLNRGMVL GSLAATVRLQ AGNATEVPAN STVLSFCAFA VDPAKAYKDY
LASGGQPITN CVKMLCTHTG TGQAITVTPE ANMDQESFGG ASCCLYCRCH IDHPNPKGFC
DLKGKYVQIP TTCANDPVGF TLRNTVCTVC GMWKGYGCSC DQLREPLMQS ADASTFLNGF
AV
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