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 R1AB_CVHSA              Reviewed;        7073 AA.
P0C6X7; P59641; Q6WGN0; Q7T697; Q808C0; Q80BV7; Q80BV8; Q80E51;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 91.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Host translation inhibitor nsp1;
Short=nsp1;
AltName: Full=Leader protein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65 homolog;
Contains:
RecName: Full=Papain-like proteinase;
Short=PL-PRO;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=Non-structural protein 3;
Short=nsp3;
AltName: Full=PL2-PRO;
AltName: Full=SARS coronavirus main proteinase;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
Contains:
RecName: Full=Guanine-N7 methyltransferase;
Short=ExoN;
EC=2.1.1.-;
EC=3.1.13.-;
AltName: Full=nsp14;
Contains:
RecName: Full=Uridylate-specific endoribonuclease;
EC=3.1.-.-;
AltName: Full=NendoU;
AltName: Full=nsp15;
Contains:
RecName: Full=2'-O-methyltransferase;
EC=2.1.1.-;
AltName: Full=nsp16;
Name=rep; ORFNames=1a-1b;
Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome
coronavirus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=227859;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9675; Paguma larvata (Masked palm civet).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Urbani;
PubMed=12730500; DOI=10.1126/science.1085952;
Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R.,
Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H.,
Tong S., Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D.,
Erdman D.D., Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E.,
Sanchez A., Liffick S., Holloway B., Limor J., McCaustland K.,
Olsen-Rasmussen M., Fouchier R., Guenther S., Osterhaus A.D.M.E.,
Drosten C., Pallansch M.A., Anderson L.J., Bellini W.J.;
"Characterization of a novel coronavirus associated with severe acute
respiratory syndrome.";
Science 300:1394-1399(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Tor2;
PubMed=12730501; DOI=10.1126/science.1085953;
Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A.,
Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y.,
Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L.,
Leach S.R., Mayo M., McDonald H., Montgomery S.B., Pandoh P.K.,
Petrescu A.S., Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E.,
Stott J.M., Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N.,
Bernard K., Booth T.F., Bowness D., Czub M., Drebot M., Fernando L.,
Flick R., Garbutt M., Gray M., Grolla A., Jones S., Feldmann H.,
Meyers A., Kabani A., Li Y., Normand S., Stroher U., Tipples G.A.,
Tyler S., Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M.,
Petric M., Skowronski D.M., Upton C., Roper R.L.;
"The genome sequence of the SARS-associated coronavirus.";
Science 300:1399-1404(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1;
PubMed=12853594; DOI=10.1056/NEJM200307103490216;
Tsui S.K.W., Chim S.S.C., Lo Y.M.D.;
"Coronavirus genomic-sequence variations and the epidemiology of the
severe acute respiratory syndrome.";
N. Engl. J. Med. 349:187-188(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate GZ50, Isolate SZ16, and Isolate SZ3;
PubMed=12958366; DOI=10.1126/science.1087139;
Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L.,
Luo S.W., Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L.,
Chan K.W., Lim W., Shortridge K.F., Yuen K.Y., Peiris J.S.M.,
Poon L.L.M.;
"Isolation and characterization of viruses related to the SARS
coronavirus from animals in southern China.";
Science 302:276-278(2003).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU-39849;
PubMed=12876307; DOI=10.1177/15353702-0322807-13;
Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C.,
Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B.,
Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.;
"The complete genome sequence of severe acute respiratory syndrome
coronavirus strain HKU-39849 (HK-39).";
Exp. Biol. Med. 228:866-873(2003).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Sin2500, Isolate Sin2677, Isolate Sin2679,
Isolate Sin2748, and Isolate sin2774;
PubMed=12781537; DOI=10.1016/S0140-6736(03)13414-9;
Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M.,
Liu E.T.;
"Comparative full-length genome sequence analysis of 14 SARS
coronavirus isolates and common mutations associated with putative
origins of infection.";
Lancet 361:1779-1785(2003).
[7]
ERRATUM.
Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M.,
Liu E.T.;
Lancet 361:1832-1832(2003).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate ZJ01;
PubMed=14527350;
Li L., Wang Z., Lu Y., Bao Q., Chen S., Wu N., Cheng S., Weng J.,
Zhang Y., Yan J., Mei L., Wang X., Zhu H., Yu Y., Zhang M., Li M.,
Yao J., Lu Q., Yao P., Bo X., Wo J., Wang S., Hu S.;
"Severe acute respiratory syndrome-associated coronavirus genotype and
its characterization.";
Chin. Med. J. 116:1288-1292(2003).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and
Isolate GD01;
Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W.,
Jiang T., Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y.,
Li X., Lu F., Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L.,
Deng Y., Dong W., Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H.,
Li S., Li S., Li W., Li W., Lin W., Liu J., Liu Z., Lu H., Ni P.,
Qi Q., Sun Y., Tang L., Tong Z., Wang J., Wang X., Wu Q., Xi Y.,
Xu Z., Yang L., Ye C., Ye J., Zhang B., Zhang F., Zhang J., Zhang X.,
Zhou J., Yang H.;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TW1;
Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.;
"The complete genome of SARS coronavirus clone TW1.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate FRA;
PubMed=14645828; DOI=10.1126/science.302.5650.1504b;
Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K.,
Censini S., Guidotti S., Masignani V., Scarselli M., Mora M.,
Donati C., Han J.H., Song H.C., Abrignani S., Covacci A., Rappuoli R.;
"Phylogeny of the SARS coronavirus.";
Science 302:1504-1505(2003).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Frankfurt-1;
Thiel V., Hertzig T., Putics A., Ivanov K.A., Schelle B., Bayer S.,
Scheiner B., Weinand H., Weissbrich B., Ziebuhr J.;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TWC;
Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee S.C., Lin Y.-C.,
Hsu C.-K., Chen H.-Y., Chang J.G., Chen P.-J., Su I.-J.;
"Genomic sequence of SARS isolate from the first fatal case in
Taiwan.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Shanghai QXC1;
Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
"Analysis of SARS coronavirus genome in Shanghai isolates.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HSR 1;
Canducci F., Clementi M., Poli G., Vicenzi E.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3;
Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L.,
Shih M.-C.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and
Isolate TWY;
Shu H.Y., Wu K.M., Tsai S.F.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[18]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate AS;
Balotta C., Corvasce S., Violin M., Galli M., Moroni M.,
Vigevani G.M., Ruan Y.J., Salemi M.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[19]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate ZJ01;
Wang Z., Cheng S., Zhang Y.;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[20]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-507; 1655-5170 AND 6903-7073.
STRAIN=Isolate Shanghai LY;
Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[21]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4993-5127.
STRAIN=Isolate Vietnam;
Emery S., Erdman D.D., Peret T.C.T., Ksiazek T.G.;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[22]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4993-5136.
STRAIN=Isolate Taiwan;
Lin J.-H., Chiu S.-C., Yang J.-Y., Wang S.-F., Chen H.-Y.;
"Detection of a novel human coronavirus in a severe acute respiratory
syndrome patient in Taiwan.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[23]
FUNCTION (HELICASE).
PubMed=12917423; DOI=10.1074/jbc.C300328200;
Tanner J.A., Watt R.M., Chai Y.-B., Lu L.-Y., Lin M.C., Peiris J.S.,
Poon L.L.M., Kung H.-F., Huang J.-D.;
"The severe acute respiratory syndrome (SARS) coronavirus
NTPase/helicase belongs to a distinct class of 5' to 3' viral
helicases.";
J. Biol. Chem. 278:39578-39582(2003).
[24]
PROTEOLYTIC PROCESSING (REPLICASE POLYPROTEIN 1AB).
PubMed=12917450; DOI=10.1099/vir.0.19424-0;
Thiel V., Ivanov K.A., Putics A., Hertzig T., Schelle B., Bayer S.,
Weissbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E.,
Ziebuhr J.;
"Mechanisms and enzymes involved in SARS coronavirus genome
expression.";
J. Gen. Virol. 84:2305-2315(2003).
[25]
CATALYTIC ACTIVITY (3C-LIKE PROTEINASE), SUBUNIT (3C-LIKE PROTEINASE),
AND BIOPHYSICOCHEMICAL PROPERTIES (3C-LIKE PROTEINASE).
PubMed=14561748; DOI=10.1074/jbc.M310875200;
Fan K., Wei P., Feng Q., Chen S., Huang C., Ma L., Lai B., Pei J.,
Liu Y., Chen J., Lai L.;
"Biosynthesis, purification, and substrate specificity of severe acute
respiratory syndrome coronavirus 3C-like proteinase.";
J. Biol. Chem. 279:1637-1642(2004).
[26]
PROTEOLYTIC PROCESSING (REPLICASE POLYPROTEIN 1AB).
PubMed=15331731; DOI=10.1128/JVI.78.18.9977-9986.2004;
Prentice E., McAuliffe J., Lu X., Subbarao K., Denison M.R.;
"Identification and characterization of severe acute respiratory
syndrome coronavirus replicase proteins.";
J. Virol. 78:9977-9986(2004).
[27]
PROTEOLYTIC PROCESSING (REPLICASE POLYPROTEIN 1AB).
STRAIN=Isolate Urbani;
PubMed=15564471; DOI=10.1128/JVI.78.24.13600-13612.2004;
Harcourt B.H., Jukneliene D., Kanjanahaluethai A., Bechill J.,
Severson K.M., Smith C.M., Rota P.A., Baker S.C.;
"Identification of severe acute respiratory syndrome coronavirus
replicase products and characterization of papain-like protease
activity.";
J. Virol. 78:13600-13612(2004).
[28]
FUNCTION (GUANINE-N7 METHYLTRANSFERASE).
STRAIN=Isolate Frankfurt-1;
PubMed=16549795; DOI=10.1073/pnas.0508200103;
Minskaia E., Hertzig T., Gorbalenya A.E., Campanacci V., Cambillau C.,
Canard B., Ziebuhr J.;
"Discovery of an RNA virus 3'->5' exoribonuclease that is critically
involved in coronavirus RNA synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 103:5108-5113(2006).
[29]
CHARACTERIZATION (URIDYLATE-SPECIFIC ENDORIBONUCLEASE).
PubMed=16882730; DOI=10.1073/pnas.0601708103;
Ricagno S., Egloff M.-P., Ulferts R., Coutard B., Nurizzo D.,
Campanacci V., Cambillau C., Ziebuhr J., Canard B.;
"Crystal structure and mechanistic determinants of SARS coronavirus
nonstructural protein 15 define an endoribonuclease family.";
Proc. Natl. Acad. Sci. U.S.A. 103:11892-11897(2006).
[30]
FUNCTION (NON-STRUCTURAL PROTEIN 8).
PubMed=17024178; DOI=10.1038/sj.emboj.7601368;
Imbert I., Guillemot J.-C., Bourhis J.-M., Bussetta C., Coutard B.,
Egloff M.-P., Ferron F., Gorbalenya A.E., Canard B.;
"A second, non-canonical RNA-dependent RNA polymerase in SARS
coronavirus.";
EMBO J. 25:4933-4942(2006).
[31]
FUNCTION (PAPAIN-LIKE PROTEINASE).
PubMed=17692280; DOI=10.1016/j.abb.2007.07.006;
Lindner H.A., Lytvyn V., Qi H., Lachance P., Ziomek E., Menard R.;
"Selectivity in ISG15 and ubiquitin recognition by the SARS
coronavirus papain-like protease.";
Arch. Biochem. Biophys. 466:8-14(2007).
[32]
SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4).
PubMed=17855519; DOI=10.1128/JVI.01506-07;
Oostra M., te Lintelo E.G., Deijs M., Verheije M.H., Rottier P.J.,
de Haan C.A.;
"Localization and membrane topology of coronavirus nonstructural
protein 4: involvement of the early secretory pathway in
replication.";
J. Virol. 81:12323-12336(2007).
[33]
FUNCTION (2'-O-METHYLTRANSFERASE).
PubMed=18417574; DOI=10.1128/JVI.00407-08;
Decroly E., Imbert I., Coutard B., Bouvet M., Selisko B., Alvarez K.,
Gorbalenya A.E., Snijder E.J., Canard B.;
"Coronavirus nonstructural protein 16 is a cap-0 binding enzyme
possessing (nucleoside-2'O)-methyltransferase activity.";
J. Virol. 82:8071-8084(2008).
[34]
INTERACTION OF NSP10 WITH NSP14 AND NSP16.
PubMed=18827877; DOI=10.1371/journal.pone.0003299;
Pan J., Peng X., Gao Y., Li Z., Lu X., Chen Y., Ishaq M., Liu D.,
Dediego M.L., Enjuanes L., Guo D.;
"Genome-wide analysis of protein-protein interactions and involvement
of viral proteins in SARS-CoV replication.";
PLoS ONE 3:E3299-E3299(2008).
[35]
FUNCTION (PAPAIN-LIKE PROTEINASE).
PubMed=19369340; DOI=10.1128/JVI.02220-08;
Frieman M., Ratia K., Johnston R.E., Mesecar A.D., Baric R.S.;
"Severe acute respiratory syndrome coronavirus papain-like protease
ubiquitin-like domain and catalytic domain regulate antagonism of IRF3
and NF-kappaB signaling.";
J. Virol. 83:6689-6705(2009).
[36]
FUNCTION (NON-STRUCTURAL PROTEIN 2), AND INTERACTION WITH HOST PHB AND
PHB2.
PubMed=19640993; DOI=10.1128/JVI.00842-09;
Cornillez-Ty C.T., Liao L., Yates J.R., Kuhn P., Buchmeier M.J.;
"Severe acute respiratory syndrome coronavirus nonstructural protein 2
interacts with a host protein complex involved in mitochondrial
biogenesis and intracellular signaling.";
J. Virol. 83:10314-10318(2009).
[37]
FUNCTION (NON-STRUCTURAL PROTEIN 9), AND MUTAGENESIS OF GLY-4217 AND
GLY-4221.
PubMed=19153232; DOI=10.1128/JVI.01505-08;
Miknis Z.J., Donaldson E.F., Umland T.C., Rimmer R.A., Baric R.S.,
Schultz L.W.;
"Severe acute respiratory syndrome coronavirus nsp9 dimerization is
essential for efficient viral growth.";
J. Virol. 83:3007-3018(2009).
[38]
INTERACTION OF NSP14 WITH DDX1.
PubMed=20573827; DOI=10.1128/JVI.00392-10;
Xu L., Khadijah S., Fang S., Wang L., Tay F.P., Liu D.X.;
"The cellular RNA helicase DDX1 interacts with coronavirus
nonstructural protein 14 and enhances viral replication.";
J. Virol. 84:8571-8583(2010).
[39]
FUNCTION (GUANINE-N7 METHYLTRANSFERASE), AND FUNCTION
(2'-O-METHYLTRANSFERASE).
PubMed=20421945; DOI=10.1371/journal.ppat.1000863;
Bouvet M., Debarnot C., Imbert I., Selisko B., Snijder E.J.,
Canard B., Decroly E.;
"In vitro reconstitution of SARS-coronavirus mRNA cap methylation.";
PLoS Pathog. 6:E1000863-E1000863(2010).
[40]
FUNCTION (HOST TRANSLATION INHIBITOR NSP1).
PubMed=22174690; DOI=10.1371/journal.ppat.1002433;
Huang C., Lokugamage K.G., Rozovics J.M., Narayanan K., Semler B.L.,
Makino S.;
"SARS coronavirus nsp1 protein induces template-dependent
endonucleolytic cleavage of mRNAs: viral mRNAs are resistant to nsp1-
induced RNA cleavage.";
PLoS Pathog. 7:E1002433-E1002433(2011).
[41]
INTERACTION OF NSP4 WITH PL-PRO AND NSP6, AND SUBCELLULAR LOCATION
(NON-STRUCTURAL PROTEIN 4).
PubMed=21345958; DOI=10.1128/JVI.00042-11;
Hagemeijer M.C., Ulasli M., Vonk A.M., Reggiori F., Rottier P.J.,
de Haan C.A.;
"Mobility and interactions of coronavirus nonstructural protein 4.";
J. Virol. 85:4572-4577(2011).
[42]
FUNCTION (NON-STRUCTURAL PROTEIN 7), AND FUNCTION (NON-STRUCTURAL
PROTEIN 8).
PubMed=22039154; DOI=10.1093/nar/gkr893;
te Velthuis A.J., van den Worm S.H., Snijder E.J.;
"The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA
polymerase capable of both de novo initiation and primer extension.";
Nucleic Acids Res. 40:1737-1747(2012).
[43]
FUNCTION (HOST TRANSLATION INHIBITOR NSP1).
PubMed=23035226; DOI=10.1128/JVI.01958-12;
Lokugamage K.G., Narayanan K., Huang C., Makino S.;
"Severe acute respiratory syndrome coronavirus protein nsp1 is a novel
eukaryotic translation inhibitor that represses multiple steps of
translation initiation.";
J. Virol. 86:13598-13608(2012).
[44]
FUNCTION (HELICASE).
PubMed=22615777; DOI=10.1371/journal.pone.0036521;
Adedeji A.O., Marchand B., Te Velthuis A.J., Snijder E.J., Weiss S.,
Eoff R.L., Singh K., Sarafianos S.G.;
"Mechanism of nucleic acid unwinding by SARS-CoV helicase.";
PLoS ONE 7:E36521-E36521(2012).
[45]
FUNCTION (RNA-DIRECTED RNA POLYMERASE).
PubMed=22791111; DOI=10.1007/s00705-012-1404-x;
Ahn D.G., Choi J.K., Taylor D.R., Oh J.W.;
"Biochemical characterization of a recombinant SARS coronavirus nsp12
RNA-dependent RNA polymerase capable of copying viral RNA templates.";
Arch. Virol. 157:2095-2104(2012).
[46]
FUNCTION (NON-STRUCTURAL PROTEIN 10), FUNCTION (GUANINE-N7
METHYLTRANSFERASE), AND INTERACTION OF NSP10 AND NSP14.
PubMed=22635272; DOI=10.1073/pnas.1201130109;
Bouvet M., Imbert I., Subissi L., Gluais L., Canard B., Decroly E.;
"RNA 3'-end mismatch excision by the severe acute respiratory syndrome
coronavirus nonstructural protein nsp10/nsp14 exoribonuclease
complex.";
Proc. Natl. Acad. Sci. U.S.A. 109:9372-9377(2012).
[47]
FUNCTION (NON-STRUCTURAL PROTEIN 4), AND SUBCELLULAR LOCATION
(NON-STRUCTURAL PROTEIN 4).
PubMed=23943763; DOI=10.1128/mBio.00524-13;
Angelini M.M., Akhlaghpour M., Neuman B.W., Buchmeier M.J.;
"Severe acute respiratory syndrome coronavirus nonstructural proteins
3, 4, and 6 induce double-membrane vesicles.";
MBio 4:0-0(2013).
[48]
FUNCTION (NON-STRUCTURAL PROTEIN 6).
PubMed=24991833; DOI=10.4161/auto.29309;
Cottam E.M., Whelband M.C., Wileman T.;
"Coronavirus NSP6 restricts autophagosome expansion.";
Autophagy 10:1426-1441(2014).
[49]
3D-STRUCTURE MODELING OF 3241-3540, AND CHARACTERIZATION.
PubMed=12746549; DOI=10.1126/science.1085658;
Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.;
"Coronavirus main proteinase (3CLpro) structure: basis for design of
anti-SARS drugs.";
Science 300:1763-1767(2003).
[50]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4118-4230 (NSP9).
STRAIN=Isolate Frankfurt-1;
PubMed=12925794; DOI=10.1107/S0907444903016779;
Campanacci V., Egloff M.-P., Longhi S., Ferron F., Rancurel C.,
Salomoni A., Durousseau C., Tocque F., Bremond N., Dobbe J.C.,
Snijder E.J., Canard B., Cambillau C.;
"Structural genomics of the SARS coronavirus: cloning, expression,
crystallization and preliminary crystallographic study of the Nsp9
protein.";
Acta Crystallogr. D 59:1628-1631(2003).
[51]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 4118-4230.
PubMed=15007178; DOI=10.1073/pnas.0307877101;
Egloff M.-P., Ferron F., Campanacci V., Longhi S., Rancurel C.,
Dutartre H., Snijder E.J., Gorbalenya A.E., Cambillau C., Canard B.;
"The severe acute respiratory syndrome-coronavirus replicative protein
nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus
world.";
Proc. Natl. Acad. Sci. U.S.A. 101:3792-3796(2004).
[52]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230, AND INTERACTION OF
NSP8 WITH NSP9.
PubMed=14962394; DOI=10.1016/j.str.2004.01.016;
Sutton G., Fry E., Carter L., Sainsbury S., Walter T., Nettleship J.,
Berrow N., Owens R., Gilbert R., Davidson A., Siddell S., Poon L.L.M.,
Diprose J., Alderton D., Walsh M., Grimes J.M., Stuart D.I.;
"The nsp9 replicase protein of SARS-coronavirus, structure and
functional insights.";
Structure 12:341-353(2004).
[53]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 3837-4117 AND 3920-4117, AND
INTERACTION OF NSP7 WITH NSP8.
PubMed=16228002; DOI=10.1038/nsmb999;
Zhai Y., Sun F., Li X., Pang H., Xu X., Bartlam M., Rao Z.;
"Insights into SARS-CoV transcription and replication from the
structure of the nsp7-nsp8 hexadecamer.";
Nat. Struct. Mol. Biol. 12:980-986(2005).
[54]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1002-1176, AND FUNCTION
(3C-LIKE PROTEINASE).
PubMed=16271890; DOI=10.1016/j.str.2005.07.022;
Saikatendu K.S., Joseph J.S., Subramanian V., Clayton T., Griffith M.,
Moy K., Velasquez J., Neuman B.W., Buchmeier M.J., Stevens R.C.,
Kuhn P.;
"Structural basis of severe acute respiratory syndrome coronavirus
ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of
nsP3.";
Structure 13:1665-1675(2005).
[55]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1541-1854.
PubMed=16581910; DOI=10.1073/pnas.0510851103;
Ratia K., Saikatendu K.S., Santarsiero B.D., Barretto N., Baker S.C.,
Stevens R.C., Mesecar A.D.;
"Severe acute respiratory syndrome coronavirus papain-like protease:
structure of a viral deubiquitinating enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 103:5717-5722(2006).
[56]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4240-4362.
STRAIN=Isolate Tor2;
PubMed=16873246; DOI=10.1128/JVI.00467-06;
Joseph J.S., Saikatendu K.S., Subramanian V., Neuman B.W., Brooun A.,
Griffith M., Moy K., Yadav M.K., Velasquez J., Buchmeier M.J.,
Stevens R.C., Kuhn P.;
"Crystal structure of nonstructural protein 10 from the severe acute
respiratory syndrome coronavirus reveals a novel fold with two zinc-
binding motifs.";
J. Virol. 80:7894-7901(2006).
[57]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4231-4378, AND SUBUNIT
(NON-STRUCTURAL PROTEIN 10).
PubMed=16873247; DOI=10.1128/JVI.00483-06;
Su D., Lou Z., Sun F., Zhai Y., Yang H., Zhang R., Joachimiak A.,
Zhang X.C., Bartlam M., Rao Z.;
"Dodecamer structure of severe acute respiratory syndrome coronavirus
nonstructural protein nsp10.";
J. Virol. 80:7902-7908(2006).
[58]
STRUCTURE BY NMR OF 13-127.
PubMed=17202208; DOI=10.1128/JVI.01939-06;
Almeida M.S., Johnson M.A., Herrmann T., Geralt M., Wuthrich K.;
"Novel beta-barrel fold in the nuclear magnetic resonance structure of
the replicase nonstructural protein 1 from the severe acute
respiratory syndrome coronavirus.";
J. Virol. 81:3151-3161(2007).
[59]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3241-3546.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of Sars coronavirus main proteinase(3CLPRO).";
Submitted (JUL-2007) to the PDB data bank.
-!- FUNCTION: Replicase polyprotein 1ab: Multifunctional protein
involved in the transcription and replication of viral RNAs.
Contains the proteinases responsible for the cleavages of the
polyprotein.
-!- FUNCTION: Host translation inhibitor nsp1: Inhibits host
translation by interacting with the 40S ribosomal subunit. The
nsp1-40S ribosome complex further induces an endonucleolytic
cleavage near the 5'UTR of host mRNAs, targeting them for
degradation. Viral mRNAs are not susceptible to nsp1-mediated
endonucleolytic RNA cleavage thanks to the presence of a 5'-end
leader sequence and are therefore protected from degradation. By
suppressing host gene expression, nsp1 facilitates efficient viral
gene expression in infected cells and evasion from host immune
response. {ECO:0000269|PubMed:23035226}.
-!- FUNCTION: Non-structural protein 2: May play a role in the
modulation of host cell survival signaling pathway by interacting
with host PHB and PHB2. Indeed, these two proteins play a role in
maintaining the functional integrity of the mitochondria and
protecting cells from various stresses.
{ECO:0000269|PubMed:19640993}.
-!- FUNCTION: Papain-like proteinase: Responsible for the cleavages
located at the N-terminus of the replicase polyprotein. In
addition, PL-PRO possesses a deubiquitinating/deISGylating
activity and processes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains from cellular substrates. Participates
together with nsp4 in the assembly of virally-induced cytoplasmic
double-membrane vesicles necessary for viral replication.
Antagonizes innate immune induction of type I interferon by
blocking the phosphorylation, dimerization and subsequent nuclear
translocation of host IRF3. Prevents also host NF-kappa-B
signaling. {ECO:0000269|PubMed:17692280,
ECO:0000269|PubMed:19369340}.
-!- FUNCTION: Non-structural protein 4: Participates in the assembly
of virally-induced cytoplasmic double-membrane vesicles necessary
for viral replication. {ECO:0000269|PubMed:23943763}.
-!- FUNCTION: Proteinase 3CL-PRO: Ccleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-
phosphate (ADRP). {ECO:0000255|PROSITE-ProRule:PRU00772,
ECO:0000269|PubMed:16271890}.
-!- FUNCTION: Non-structural protein 6: Plays a role in the initial
induction of autophagosomes from host reticulum endoplasmic.
Later, limits the expansion of these phagosomes that are no longer
able to deliver viral components to lysosomes.
{ECO:0000269|PubMed:24991833}.
-!- FUNCTION: Non-structural protein 7: Forms a hexadecamer with nsp8
(8 subunits of each) that may participate in viral replication by
acting as a primase. Alternatively, may synthesize substantially
longer products than oligonucleotide primers.
{ECO:0000269|PubMed:22039154}.
-!- FUNCTION: Non-structural protein 8: Forms a hexadecamer with nsp7
(8 subunits of each) that may participate in viral replication by
acting as a primase. Alternatively, may synthesize substantially
longer products than oligonucleotide primers.
{ECO:0000269|PubMed:22039154}.
-!- FUNCTION: Non-structural protein 9: May participate in viral
replication by acting as a ssRNA-binding protein.
{ECO:0000269|PubMed:19153232}.
-!- FUNCTION: Non-structural protein 10: Plays a pivotal role in viral
transcription by stimulating both nsp14 3'-5' exoribonuclease and
nsp16 2'-O-methyltransferase activities. Therefore plays an
essential role in viral mRNAs cap methylation.
{ECO:0000269|PubMed:22635272}.
-!- FUNCTION: RNA-directed RNA polymerase: Responsible for replication
and transcription of the viral RNA genome.
{ECO:0000269|PubMed:22791111}.
-!- FUNCTION: Helicase: Multi-functional protein with a zinc-binding
domain in N-terminus displaying RNA and DNA duplex-unwinding
activities with 5' to 3' polarity. Activity of helicase is
dependent on magnesium. {ECO:0000269|PubMed:12917423,
ECO:0000269|PubMed:22615777}.
-!- FUNCTION: Guanine-N7 methyltransferase: Enzyme possessing two
different activities: an exoribonuclease activity acting on both
ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine
methyltransferase activity. {ECO:0000269|PubMed:16549795,
ECO:0000269|PubMed:20421945, ECO:0000269|PubMed:22635272}.
-!- FUNCTION: Uridylate-specific endoribonuclease: Mn(2+)-dependent,
uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5'
to the cleaved bond.
-!- FUNCTION: 2'-O-methyltransferase: Methyltransferase that mediates
mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
mRNAs. N7-methyl guanosine cap is a prerequisite for binding of
nsp16. Therefore plays an essential role in viral mRNAs cap
methylation which is essential to evade immune system.
{ECO:0000269|PubMed:18417574, ECO:0000269|PubMed:20421945,
ECO:0000305}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539,
ECO:0000269|PubMed:14561748}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:14561748}.
-!- CATALYTIC ACTIVITY: TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the
two peptides corresponding to the two self-cleavage sites of the
SARS 3C-like proteinase are the two most reactive peptide
substrates. The enzyme exhibits a strong preference for substrates
containing Gln at P1 position and Leu at P2 position.
{ECO:0000269|PubMed:14561748}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
{ECO:0000269|PubMed:14561748}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.15 mM for peptide TSAVLQ/SGFRK-NH(2)
{ECO:0000269|PubMed:14561748};
KM=0.58 mM for peptide SGVTFQ/GKFKK
{ECO:0000269|PubMed:14561748};
KM=1.44 mM for peptide ATVRLQ/AGNAT
{ECO:0000269|PubMed:14561748};
Note=The kinetic parameters are studied for the 3C-like
proteinase domain. The cleavage takes place at the /.;
pH dependence:
Optimum pH is 7.0 for 3C-like proteinase activity.
{ECO:0000269|PubMed:14561748};
-!- SUBUNIT: Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as
monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only
the homodimer shows catalytic activity. Eight copies of nsp7 and
eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-
encircling ring structure. Nsp9 is a dimer. Nsp10 forms a
dodecamer and interacts with nsp14 and nsp16; these interactions
enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via
N-terminus) with DDX1. {ECO:0000269|PubMed:14561748,
ECO:0000269|PubMed:16228002, ECO:0000269|PubMed:16873247,
ECO:0000269|PubMed:18827877, ECO:0000269|PubMed:19640993,
ECO:0000269|PubMed:20573827, ECO:0000269|PubMed:21345958,
ECO:0000269|PubMed:22635272}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-7843867, EBI-7843867;
-!- SUBCELLULAR LOCATION: Papain-like proteinase: Host membrane;
Multi-pass membrane protein. Host cytoplasm
{ECO:0000269|PubMed:23943763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane;
Multi-pass membrane protein. Host cytoplasm. Note=Localizes in
virally-induced cytoplasmic double-membrane vesicles.
{ECO:0000269|PubMed:17855519, ECO:0000269|PubMed:21345958,
ECO:0000269|PubMed:23943763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 6: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 7: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 8: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 9: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 10: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Helicase: Host endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000305}. Note=The helicase
interacts with the N protein in membranous complexes and
colocalizes with sites of synthesis of new viral RNA.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Uridylate-specific endoribonuclease: Host
cytoplasm, host perinuclear region {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X7-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6U8-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. 3CL-PRO and PL-PRO proteinases are
autocatalytically processed (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- CAUTION: Isolates SZ3 and SZ16 have been isolated from Paguma
larvata and are described as SARS-like in literature.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAP13440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAP41036.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAP82975.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAP97881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAQ01596.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAQ01608.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY278741; AAP13442.1; -; Genomic_RNA.
EMBL; AY278741; AAP13440.1; ALT_SEQ; Genomic_RNA.
EMBL; AY274119; AAP41036.1; ALT_SEQ; Genomic_RNA.
EMBL; AY278554; AAP13566.1; -; Genomic_RNA.
EMBL; AY282752; AAP30711.1; -; Genomic_RNA.
EMBL; AY304495; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY304486; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY304488; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283795; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283796; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283797; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283798; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY286320; AAP49011.4; -; Genomic_RNA.
EMBL; AY278488; AAP30028.1; -; Genomic_RNA.
EMBL; AY278489; AAP51225.1; -; Genomic_RNA.
EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY291451; AAP37015.1; -; Genomic_RNA.
EMBL; AY310120; AAP50483.1; -; Genomic_RNA.
EMBL; AY291315; AAP33696.1; -; Genomic_RNA.
EMBL; AY323977; AAP72973.2; -; Genomic_RNA.
EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY338174; AAQ01594.1; -; Genomic_RNA.
EMBL; AY338174; AAQ01596.1; ALT_SEQ; Genomic_RNA.
EMBL; AY338175; AAQ01606.1; -; Genomic_RNA.
EMBL; AY338175; AAQ01608.1; ALT_SEQ; Genomic_RNA.
EMBL; AY348314; AAP97879.1; -; Genomic_RNA.
EMBL; AY348314; AAP97881.1; ALT_SEQ; Genomic_RNA.
EMBL; AP006557; BAC81346.1; -; Genomic_RNA.
EMBL; AP006558; BAC81360.1; -; Genomic_RNA.
EMBL; AP006559; BAC81374.1; -; Genomic_RNA.
EMBL; AP006560; BAC81388.1; -; Genomic_RNA.
EMBL; AP006561; BAC81402.1; -; Genomic_RNA.
EMBL; AY427439; AAQ94058.1; -; Genomic_RNA.
EMBL; AY322205; AAP82966.1; -; Genomic_RNA.
EMBL; AY322206; AAP82975.1; ALT_SEQ; Genomic_RNA.
EMBL; AY322207; AAP82967.1; -; Genomic_RNA.
EMBL; AY463059; AAP82978.2; -; Genomic_RNA.
EMBL; AY269391; AAP04003.1; -; Genomic_RNA.
EMBL; AY268049; AAP04587.1; -; Genomic_RNA.
RefSeq; NP_828849.2; NC_004718.3. [P0C6X7-1]
PDB; 1O5S; Model; -; A=4745-5301.
PDB; 1P76; Model; -; A=3241-3541, B=4225-4231.
PDB; 1P9T; Model; -; A=3241-3544.
PDB; 1PA5; Model; -; A=3241-3546.
PDB; 1PUK; Model; -; A=3241-3550.
PDB; 1Q1X; Model; -; A=3241-3542.
PDB; 1Q2W; X-ray; 1.86 A; A/B=3241-3544.
PDB; 1QZ8; X-ray; 2.70 A; A/B=4118-4230.
PDB; 1SXF; Model; -; A=4765-5244.
PDB; 1UJ1; X-ray; 1.90 A; A/B=3241-3546.
PDB; 1UK2; X-ray; 2.20 A; A/B=3241-3546.
PDB; 1UK3; X-ray; 2.40 A; A/B=3241-3546.
PDB; 1UK4; X-ray; 2.50 A; A/B=3241-3546.
PDB; 1UW7; X-ray; 2.80 A; A=4118-4230.
PDB; 1WOF; X-ray; 2.00 A; A/B=3241-3546.
PDB; 1YSY; NMR; -; A=3837-3919.
PDB; 1Z1I; X-ray; 2.80 A; A=3241-3546.
PDB; 1Z1J; X-ray; 2.80 A; A/B=3241-3546.
PDB; 2A5A; X-ray; 2.08 A; A=3241-3546.
PDB; 2A5I; X-ray; 1.88 A; A=3241-3546.
PDB; 2A5K; X-ray; 2.30 A; A/B=3241-3546.
PDB; 2ACF; X-ray; 1.40 A; A/B/C/D=1002-1176.
PDB; 2AHM; X-ray; 2.40 A; A/B/C/D=3837-3919, E/F/G/H=3920-4117.
PDB; 2AJ5; Model; -; A=3241-3546.
PDB; 2ALV; X-ray; 1.90 A; A=3241-3543.
PDB; 2AMD; X-ray; 1.85 A; A/B=3241-3546.
PDB; 2AMQ; X-ray; 2.30 A; A/B=3241-3546.
PDB; 2BX3; X-ray; 2.00 A; A=3241-3546.
PDB; 2BX4; X-ray; 2.79 A; A=3241-3546.
PDB; 2C3S; X-ray; 1.90 A; A=3241-3546.
PDB; 2D2D; X-ray; 2.70 A; A/B=3241-3546.
PDB; 2DUC; X-ray; 1.70 A; A/B=3241-3546.
PDB; 2FAV; X-ray; 1.80 A; A/B/C=1000-1173.
PDB; 2FE8; X-ray; 1.85 A; A/B/C=1541-1854.
PDB; 2FYG; X-ray; 1.80 A; A=4240-4362.
PDB; 2G1F; Model; -; A/B=5302-5877.
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.
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.
PDB; 2GDT; NMR; -; A=13-127.
PDB; 2GRI; NMR; -; A=819-930.
PDB; 2GT7; X-ray; 1.82 A; A/B=3241-3546.
PDB; 2GT8; X-ray; 2.00 A; A=3241-3546.
PDB; 2GTB; X-ray; 2.00 A; A=3241-3546.
PDB; 2GX4; X-ray; 1.93 A; A=3241-3546.
PDB; 2GZ7; X-ray; 1.86 A; A=3241-3546.
PDB; 2GZ8; X-ray; 1.97 A; A=3241-3546.
PDB; 2GZ9; X-ray; 2.17 A; A=3241-3546.
PDB; 2H2Z; X-ray; 1.60 A; A=3241-3546.
PDB; 2H85; X-ray; 2.60 A; A=6429-6774.
PDB; 2HOB; X-ray; 1.95 A; A=3241-3546.
PDB; 2HSX; NMR; -; A=13-127.
PDB; 2IDY; NMR; -; A=819-930.
PDB; 2JZD; NMR; -; A=1345-1469.
PDB; 2JZE; NMR; -; A=1345-1469.
PDB; 2JZF; NMR; -; A=1331-1469.
PDB; 2K87; NMR; -; A=1884-1998.
PDB; 2OP9; X-ray; 1.80 A; A/B=3241-3541.
PDB; 2OZK; X-ray; 2.90 A; A/B/C/D=6430-6775.
PDB; 2PWX; X-ray; 2.50 A; A=3241-3546.
PDB; 2Q6G; X-ray; 2.50 A; A/B=3241-3546.
PDB; 2QC2; X-ray; 2.70 A; A/B=3241-3546.
PDB; 2QCY; X-ray; 1.75 A; A=3241-3546.
PDB; 2QIQ; X-ray; 1.90 A; A=3242-3541.
PDB; 2RHB; X-ray; 2.80 A; A/B/C/D/E/F=6430-6775.
PDB; 2RNK; NMR; -; A=1331-1469.
PDB; 2V6N; X-ray; 1.98 A; A=3241-3546.
PDB; 2VJ1; X-ray; 2.25 A; A/B=3242-3544.
PDB; 2XYQ; X-ray; 2.00 A; A=6776-7065, B=4240-4361.
PDB; 2XYR; X-ray; 2.50 A; A=6776-7067, B=4240-4361.
PDB; 2XYV; X-ray; 2.06 A; A=6776-7067, B=4240-4361.
PDB; 2Z3C; X-ray; 1.79 A; A=3241-3546.
PDB; 2Z3D; X-ray; 2.10 A; A=3241-3546.
PDB; 2Z3E; X-ray; 2.32 A; A=3241-3546.
PDB; 2Z94; X-ray; 1.78 A; A=3241-3546.
PDB; 2Z9G; X-ray; 1.86 A; A=3241-3546.
PDB; 2Z9J; X-ray; 1.95 A; A/B=3241-3546.
PDB; 2Z9K; X-ray; 1.85 A; A/B=3241-3546.
PDB; 2Z9L; X-ray; 2.10 A; A/B=3241-3546.
PDB; 3D62; X-ray; 2.70 A; A=3243-3541.
PDB; 3E9S; X-ray; 2.50 A; A=1541-1855.
PDB; 3EBN; X-ray; 2.40 A; A/B/C/D=3429-3546.
PDB; 3R24; X-ray; 2.00 A; A=6776-7073, B=4240-4382.
PDB; 4TWW; X-ray; 2.42 A; A/B=3241-3546.
PDB; 4TWY; X-ray; 1.60 A; A=3241-3546.
PDB; 4WY3; X-ray; 1.89 A; A=3241-3546.
PDB; 4ZUH; X-ray; 2.39 A; C=3235-3245.
PDB; 5B6O; X-ray; 2.20 A; A/B=3241-3556.
PDB; 5C5N; X-ray; 1.69 A; A=3241-3546.
PDB; 5C5O; X-ray; 1.50 A; A/B=3241-3546.
PDB; 5C8S; X-ray; 3.33 A; A/C=4231-4369, B/D=5903-6429.
PDB; 5C8T; X-ray; 3.20 A; A/C=4231-4369, B/D=5903-6429.
PDB; 5C8U; X-ray; 3.40 A; A/C=4231-4369, B/D=5903-6429.
PDB; 5E6J; X-ray; 2.85 A; A/D=1541-1856.
PDB; 5F22; X-ray; 2.15 A; B=3989-4117.
PDBsum; 1O5S; -.
PDBsum; 1P76; -.
PDBsum; 1P9T; -.
PDBsum; 1PA5; -.
PDBsum; 1PUK; -.
PDBsum; 1Q1X; -.
PDBsum; 1Q2W; -.
PDBsum; 1QZ8; -.
PDBsum; 1SXF; -.
PDBsum; 1UJ1; -.
PDBsum; 1UK2; -.
PDBsum; 1UK3; -.
PDBsum; 1UK4; -.
PDBsum; 1UW7; -.
PDBsum; 1WOF; -.
PDBsum; 1YSY; -.
PDBsum; 1Z1I; -.
PDBsum; 1Z1J; -.
PDBsum; 2A5A; -.
PDBsum; 2A5I; -.
PDBsum; 2A5K; -.
PDBsum; 2ACF; -.
PDBsum; 2AHM; -.
PDBsum; 2AJ5; -.
PDBsum; 2ALV; -.
PDBsum; 2AMD; -.
PDBsum; 2AMQ; -.
PDBsum; 2BX3; -.
PDBsum; 2BX4; -.
PDBsum; 2C3S; -.
PDBsum; 2D2D; -.
PDBsum; 2DUC; -.
PDBsum; 2FAV; -.
PDBsum; 2FE8; -.
PDBsum; 2FYG; -.
PDBsum; 2G1F; -.
PDBsum; 2G9T; -.
PDBsum; 2GA6; -.
PDBsum; 2GDT; -.
PDBsum; 2GRI; -.
PDBsum; 2GT7; -.
PDBsum; 2GT8; -.
PDBsum; 2GTB; -.
PDBsum; 2GX4; -.
PDBsum; 2GZ7; -.
PDBsum; 2GZ8; -.
PDBsum; 2GZ9; -.
PDBsum; 2H2Z; -.
PDBsum; 2H85; -.
PDBsum; 2HOB; -.
PDBsum; 2HSX; -.
PDBsum; 2IDY; -.
PDBsum; 2JZD; -.
PDBsum; 2JZE; -.
PDBsum; 2JZF; -.
PDBsum; 2K87; -.
PDBsum; 2OP9; -.
PDBsum; 2OZK; -.
PDBsum; 2PWX; -.
PDBsum; 2Q6G; -.
PDBsum; 2QC2; -.
PDBsum; 2QCY; -.
PDBsum; 2QIQ; -.
PDBsum; 2RHB; -.
PDBsum; 2RNK; -.
PDBsum; 2V6N; -.
PDBsum; 2VJ1; -.
PDBsum; 2XYQ; -.
PDBsum; 2XYR; -.
PDBsum; 2XYV; -.
PDBsum; 2Z3C; -.
PDBsum; 2Z3D; -.
PDBsum; 2Z3E; -.
PDBsum; 2Z94; -.
PDBsum; 2Z9G; -.
PDBsum; 2Z9J; -.
PDBsum; 2Z9K; -.
PDBsum; 2Z9L; -.
PDBsum; 3D62; -.
PDBsum; 3E9S; -.
PDBsum; 3EBN; -.
PDBsum; 3R24; -.
PDBsum; 4TWW; -.
PDBsum; 4TWY; -.
PDBsum; 4WY3; -.
PDBsum; 4ZUH; -.
PDBsum; 5B6O; -.
PDBsum; 5C5N; -.
PDBsum; 5C5O; -.
PDBsum; 5C8S; -.
PDBsum; 5C8T; -.
PDBsum; 5C8U; -.
PDBsum; 5E6J; -.
PDBsum; 5F22; -.
ProteinModelPortal; P0C6X7; -.
SMR; P0C6X7; -.
MINT; MINT-1487760; -.
BindingDB; P0C6X7; -.
ChEMBL; CHEMBL5118; -.
DrugBank; DB08748; 4-(DIMETHYLAMINO)BENZOIC ACID.
DrugBank; DB08656; 5-amino-2-methyl-N-[(1R)-1-naphthalen-1-ylethyl]benzamide.
DrugBank; DB07293; benzyl (2-oxopropyl)carbamate.
DrugBank; DB08732; NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE.
PRIDE; P0C6X7; -.
GeneID; 1489680; -.
KEGG; vg:1489680; -.
OrthoDB; VOG09000000; -.
BRENDA; 2.7.7.48; 7599.
BRENDA; 3.4.22.B14; 7599.
BRENDA; 3.6.4.12; 7599.
EvolutionaryTrace; P0C6X7; -.
Proteomes; UP000000354; Genome.
Proteomes; UP000103670; Genome.
Proteomes; UP000109640; Genome.
Proteomes; UP000116947; Genome.
Proteomes; UP000121636; Genome.
Proteomes; UP000131569; Genome.
Proteomes; UP000131955; Genome.
Proteomes; UP000137377; Genome.
Proteomes; UP000138690; Genome.
Proteomes; UP000143093; Genome.
Proteomes; UP000145651; Genome.
Proteomes; UP000146108; Genome.
Proteomes; UP000146181; Genome.
Proteomes; UP000146296; Genome.
Proteomes; UP000148194; Genome.
Proteomes; UP000153467; Genome.
Proteomes; UP000160648; Genome.
Proteomes; UP000164441; Genome.
Proteomes; UP000172416; Genome.
GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:CACAO.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IDA:UniProtKB.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IDA:UniProtKB.
GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039519; P:modulation by virus of host autophagy; IDA:UniProtKB.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IDA:UniProtKB.
GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
GO; GO:2000158; P:positive regulation of ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:UniProtKB.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IDA:UniProtKB.
GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0039604; P:suppression by virus of host translation; IDA:UniProtKB.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0001172; P:transcription, RNA-templated; IDA:UniProtKB.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019083; P:viral transcription; IMP:CACAO.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR009461; Coronavirus_NSP16.
InterPro; IPR027352; CV_ZBD.
InterPro; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR021590; NSP1.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR009466; NSP11.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR024358; SARS-CoV_Nsp3_N.
InterPro; IPR022733; SARS_polyprot_cleavage.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF06478; Corona_RPol_N; 1.
Pfam; PF12379; DUF3655; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF11501; Nsp1; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF06471; NSP11; 1.
Pfam; PF06460; NSP13; 1.
Pfam; PF12124; Nsp3_PL2pro; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF11633; SUD-M; 1.
Pfam; PF08715; Viral_protease; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF142877; SSF142877; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51653; CV_ZBD; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Complete proteome; Decay of host mRNAs by virus; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
Host cytoplasm; Host gene expression shutoff by virus; Host membrane;
Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host ISG15 by virus;
Inhibition of host NF-kappa-B by virus; Membrane; Metal-binding;
Methyltransferase;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway;
Viral immunoevasion; Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 180 Host translation inhibitor nsp1.
{ECO:0000250}.
/FTId=PRO_0000037309.
CHAIN 181 818 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000037310.
CHAIN 819 2740 Papain-like proteinase. {ECO:0000250}.
/FTId=PRO_0000037311.
CHAIN 2741 3240 Non-structural protein 4. {ECO:0000255}.
/FTId=PRO_0000283841.
CHAIN 3241 3546 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000037312.
CHAIN 3547 3836 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000037313.
CHAIN 3837 3919 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000037314.
CHAIN 3920 4117 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000037315.
CHAIN 4118 4230 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000037316.
CHAIN 4231 4369 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000037317.
CHAIN 4370 5301 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000037318.
CHAIN 5302 5902 Helicase. {ECO:0000250}.
/FTId=PRO_0000037319.
CHAIN 5903 6429 Guanine-N7 methyltransferase.
{ECO:0000250}.
/FTId=PRO_0000037320.
CHAIN 6430 6775 Uridylate-specific endoribonuclease.
{ECO:0000250}.
/FTId=PRO_0000037321.
CHAIN 6776 7073 2'-O-methyltransferase. {ECO:0000250}.
/FTId=PRO_0000037322.
TRANSMEM 2092 2112 Helical. {ECO:0000255}.
TRANSMEM 2203 2223 Helical. {ECO:0000255}.
TRANSMEM 2304 2324 Helical. {ECO:0000255}.
TRANSMEM 2326 2346 Helical. {ECO:0000255}.
TRANSMEM 2351 2371 Helical. {ECO:0000255}.
TRANSMEM 2755 2775 Helical. {ECO:0000255}.
TRANSMEM 2830 2850 Helical. {ECO:0000255}.
TRANSMEM 2879 2899 Helical. {ECO:0000255}.
TRANSMEM 2992 3012 Helical. {ECO:0000255}.
TRANSMEM 3022 3042 Helical. {ECO:0000255}.
TRANSMEM 3054 3074 Helical. {ECO:0000255}.
TRANSMEM 3077 3097 Helical. {ECO:0000255}.
TRANSMEM 3105 3125 Helical. {ECO:0000255}.
TRANSMEM 3142 3162 Helical. {ECO:0000255}.
TRANSMEM 3564 3584 Helical. {ECO:0000255}.
TRANSMEM 3586 3606 Helical. {ECO:0000255}.
TRANSMEM 3612 3632 Helical. {ECO:0000255}.
TRANSMEM 3658 3678 Helical. {ECO:0000255}.
TRANSMEM 3707 3727 Helical. {ECO:0000255}.
TRANSMEM 3728 3748 Helical. {ECO:0000255}.
TRANSMEM 3756 3776 Helical. {ECO:0000255}.
DOMAIN 1003 1169 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1611 1875 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3241 3546 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 4981 5143 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 5302 5385 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5558 5739 (+)RNA virus helicase ATP-binding.
DOMAIN 5740 5909 (+)RNA virus helicase C-terminal.
ZN_FING 1729 1766 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4304 4320
ZN_FING 4347 4360
NP_BIND 5583 5590 ATP. {ECO:0000250}.
REGION 2092 2371 HD1.
REGION 2755 3162 HD2.
REGION 3564 3776 HD3.
COMPBIAS 930 1001 Glu-rich.
COMPBIAS 2210 2213 Poly-Leu.
COMPBIAS 3766 3769 Poly-Cys.
ACT_SITE 1651 1651 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1812 1812 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3281 3281 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3385 3385 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 4304 4304 Zinc.
METAL 4307 4307 Zinc.
METAL 4313 4313 Zinc.
METAL 4320 4320 Zinc.
METAL 4347 4347 Zinc.
METAL 4350 4350 Zinc.
METAL 4358 4358 Zinc.
METAL 5306 5306 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5309 5309 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5317 5317 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5320 5320 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5327 5327 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5330 5330 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5334 5334 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5340 5340 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5351 5351 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5356 5356 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5373 5373 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5376 5376 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 180 181 Cleavage. {ECO:0000250}.
SITE 818 819 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 2740 2741 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3240 3241 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3546 3547 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3836 3837 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3919 3920 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4117 4118 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4230 4231 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4369 4370 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5301 5302 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5902 5903 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6429 6430 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6775 6776 Cleavage; by 3CL-PRO. {ECO:0000250}.
VARIANT 82 82 G -> C (in strain: Isolate GD01).
VARIANT 130 130 G -> R (in strain: Isolate GD01).
VARIANT 138 138 I -> T (in strain: Isolate SZ16).
VARIANT 181 181 A -> V (in strain: Isolate Shanghai LY).
VARIANT 225 225 K -> Q (in strain: Isolate GD01).
VARIANT 249 249 Y -> C (in strain: Isolate Shanghai LY).
VARIANT 306 306 V -> F (in strain: Isolate BJ04).
VARIANT 549 549 A -> S (in strain: Isolate SZ3).
VARIANT 765 765 A -> T (in strain: Isolate FRA and
Isolate Frankfurt-1).
VARIANT 852 852 K -> R (in strain: Isolate SZ16).
VARIANT 1004 1004 N -> H (in strain: Isolate BJ03).
VARIANT 1021 1021 V -> A (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 1023 1023 I -> T (in strain: Isolate Shanghai
QXC1).
VARIANT 1121 1121 I -> T (in strain: Isolate GD01, Isolate
SZ3 and Isolate SZ16).
VARIANT 1136 1136 P -> L (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 1257 1257 K -> E (in strain: Isolate Shanghai
QXC1).
VARIANT 1319 1319 K -> R (in strain: Isolate GD01).
VARIANT 1329 1329 F -> S (in strain: Isolate GD01).
VARIANT 1361 1361 T -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 1385 1385 I -> V (in strain: Isolate Shanghai
QXC1).
VARIANT 1538 1538 S -> T (in strain: Isolate GD01).
VARIANT 1563 1563 M -> K (in strain: Isolate BJ02).
VARIANT 1663 1663 L -> I (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 1762 1762 I -> L (in strain: Isolate BJ03).
VARIANT 1776 1777 QQ -> PP (in strain: Isolate BJ03).
VARIANT 1790 1790 E -> G (in strain: Isolate Shanghai
QXC1).
VARIANT 1806 1806 G -> V (in strain: Isolate BJ02).
VARIANT 1962 1962 L -> I (in strain: Isolate BJ04).
VARIANT 2116 2116 L -> F (in strain: Isolate GD01, Isolate
SZ3 and Isolate SZ16).
VARIANT 2222 2222 C -> Y (in strain: Isolate GD01, Isolate
SZ3 and Isolate SZ16).
VARIANT 2269 2269 L -> S (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 2326 2326 V -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 2392 2394 RNR -> CNH (in strain: Isolate Shanghai
QXC1).
VARIANT 2480 2480 L -> P (in strain: Isolate Shanghai
QXC1).
VARIANT 2552 2552 A -> V (in strain: Isolate Urbani and
Isolate Taiwan TC2).
VARIANT 2556 2556 D -> N (in strain: Isolate HKU-39849).
VARIANT 2564 2564 S -> P (in strain: Isolate GD01).
VARIANT 2648 2648 N -> Y (in strain: Isolate Shanghai
QXC1).
VARIANT 2708 2708 S -> T (in strain: Isolate HKU-39849).
VARIANT 2718 2718 R -> T (in strain: Isolate HKU-39849).
VARIANT 2746 2746 C -> W (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 2770 2770 V -> L (in strain: Isolate BJ01 and
Isolate BJ02).
VARIANT 2944 2944 T -> I (in strain: Isolate SIN2500,
Isolate GD01 and Isolate GZ50).
VARIANT 2971 2971 V -> A (in strain: Isolate GD01 and
Isolate SZ16).
VARIANT 3020 3020 V -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 3047 3047 V -> A (in strain: Isolate CUHK-W1,
Isolate GD01, Isolate SZ3, Isolate SZ16,
Isolate BJ01, Isolate BJ02, Isolate BJ03
and Isolate Shanghai QXC1).
VARIANT 3072 3072 V -> A (in strain: Isolate CUHK-W1,
Isolate SZ3, Isolate SZ16 and Isolate
GD01).
VARIANT 3197 3197 A -> V (in strain: Isolate BJ01, Isolate
BJ02, Isolate BJ03, Isolate BJ04 and
Isolate Shanghai QXC1).
VARIANT 3429 3429 Q -> P (in strain: Isolate BJ02).
VARIANT 3488 3488 D -> E (in strain: Isolate BJ04).
VARIANT 3717 3717 V -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 3818 3818 N -> T (in strain: Isolate BJ04).
VARIANT 3903 3903 D -> N (in strain: Isolate BJ03).
VARIANT 3904 3904 I -> F (in strain: Isolate BJ02).
VARIANT 3911 3911 M -> V (in strain: Isolate Shanghai
QXC1).
VARIANT 4001 4001 K -> Q (in strain: Isolate Shanghai LY).
VARIANT 4003 4003 T -> A (in strain: Isolate Shanghai LY).
VARIANT 4085 4085 I -> H (in strain: Isolate ZJ01).
VARIANT 4114 4114 V -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 4202 4202 V -> M (in strain: Isolate Shanghai
QXC1).
VARIANT 4240 4240 N -> H (in strain: Isolate ZJ01).
VARIANT 4296 4296 E -> G (in strain: Isolate Shanghai
QXC1).
VARIANT 4377 4378 LN -> FK (in strain: Isolate Shanghai
QXC1).
VARIANT 4411 4411 V -> S (in strain: Isolate HKU-39849).
VARIANT 4459 4459 V -> I (in strain: Isolate Shanghai
QXC1).
VARIANT 4592 4592 V -> E (in strain: Isolate ZJ01).
VARIANT 4910 4910 Q -> L (in strain: Isolate ZJ01).
VARIANT 5112 5112 D -> G (in strain: Isolate SZ3).
VARIANT 5131 5131 A -> G (in strain: Isolate Taiwan).
VARIANT 5134 5135 CY -> VL (in strain: Isolate Taiwan).
VARIANT 5623 5623 L -> S (in strain: Isolate GD01).
VARIANT 5720 5720 P -> S (in strain: Isolate GZ50 and
Isolate SIN2500).
VARIANT 5744 5744 R -> C (in strain: Isolate ZJ01).
VARIANT 5767 5767 D -> E (in strain: Isolate CUHK-W1,
Isolate BJ01, Isolate BJ02, Isolate BJ03,
Isolate BJ04, Isolate SIN2500, Isolate
GD01, Isolate GZ50, Isolate SZ3, Isolate
SZ16 and Isolate Shanghai QXC1).
VARIANT 6274 6274 T -> I (in strain: Isolate FRA, Isolate
Frankfurt-1 Isolate SIN2677, Isolate
SIN2679 and Isolate SIN2748).
VARIANT 6474 6474 N -> S (in strain: Isolate Shanghai
QXC1).
VARIANT 6700 6700 M -> I (in strain: Isolate BJ03).
VARIANT 6721 6721 C -> R (in strain: Isolate Shanghai
QXC1).
VARIANT 6729 6729 D -> N (in strain: Isolate GD01).
VARIANT 6840 6840 M -> L (in strain: Isolate BJ02).
VARIANT 6862 6862 Q -> P (in strain: Isolate BJ04).
VARIANT 6877 6877 D -> E (in strain: Isolate GD01).
VARIANT 6910 6910 R -> K (in strain: Isolate SZ3 and
Isolate SZ16).
VARIANT 6937 6937 A -> P (in strain: Isolate BJ03).
VARIANT 6992 6992 E -> D (in strain: Isolate BJ04).
VARIANT 7008 7008 N -> K (in strain: Isolate GD01).
VARIANT 7024 7024 K -> Q (in strain: Isolate BJ04).
MUTAGEN 4217 4217 G->E: Complete loss of nsp9 dimerization.
{ECO:0000269|PubMed:19153232}.
MUTAGEN 4221 4221 G->E: Complete loss of nsp9 dimerization.
{ECO:0000269|PubMed:19153232}.
STRAND 14 20 {ECO:0000244|PDB:2GDT}.
TURN 23 25 {ECO:0000244|PDB:2GDT}.
HELIX 35 48 {ECO:0000244|PDB:2GDT}.
STRAND 51 54 {ECO:0000244|PDB:2GDT}.
HELIX 61 63 {ECO:0000244|PDB:2GDT}.
STRAND 68 72 {ECO:0000244|PDB:2GDT}.
STRAND 87 93 {ECO:0000244|PDB:2GDT}.
TURN 95 98 {ECO:0000244|PDB:2GDT}.
STRAND 99 102 {ECO:0000244|PDB:2GDT}.
STRAND 105 109 {ECO:0000244|PDB:2GDT}.
STRAND 116 123 {ECO:0000244|PDB:2GDT}.
STRAND 827 829 {ECO:0000244|PDB:2GRI}.
TURN 831 833 {ECO:0000244|PDB:2GRI}.
STRAND 839 841 {ECO:0000244|PDB:2GRI}.
STRAND 848 851 {ECO:0000244|PDB:2GRI}.
TURN 852 856 {ECO:0000244|PDB:2GRI}.
STRAND 860 862 {ECO:0000244|PDB:2GRI}.
TURN 869 871 {ECO:0000244|PDB:2GRI}.
HELIX 872 882 {ECO:0000244|PDB:2GRI}.
HELIX 888 894 {ECO:0000244|PDB:2GRI}.
HELIX 898 901 {ECO:0000244|PDB:2GRI}.
STRAND 907 909 {ECO:0000244|PDB:2GRI}.
STRAND 911 915 {ECO:0000244|PDB:2GRI}.
STRAND 918 920 {ECO:0000244|PDB:2GRI}.
STRAND 922 926 {ECO:0000244|PDB:2GRI}.
STRAND 1013 1021 {ECO:0000244|PDB:2ACF}.
HELIX 1023 1030 {ECO:0000244|PDB:2ACF}.
STRAND 1033 1038 {ECO:0000244|PDB:2ACF}.
HELIX 1048 1056 {ECO:0000244|PDB:2ACF}.
TURN 1057 1059 {ECO:0000244|PDB:2ACF}.
HELIX 1060 1072 {ECO:0000244|PDB:2ACF}.
STRAND 1080 1084 {ECO:0000244|PDB:2ACF}.
TURN 1086 1088 {ECO:0000244|PDB:2ACF}.
STRAND 1090 1095 {ECO:0000244|PDB:2ACF}.
HELIX 1100 1102 {ECO:0000244|PDB:2ACF}.
HELIX 1108 1114 {ECO:0000244|PDB:2ACF}.
HELIX 1115 1118 {ECO:0000244|PDB:2ACF}.
STRAND 1119 1124 {ECO:0000244|PDB:2ACF}.
HELIX 1130 1132 {ECO:0000244|PDB:2ACF}.
HELIX 1136 1146 {ECO:0000244|PDB:2ACF}.
STRAND 1149 1156 {ECO:0000244|PDB:2ACF}.
HELIX 1158 1168 {ECO:0000244|PDB:2ACF}.
STRAND 1345 1347 {ECO:0000244|PDB:2JZF}.
HELIX 1351 1361 {ECO:0000244|PDB:2JZD}.
STRAND 1364 1368 {ECO:0000244|PDB:2JZD}.
HELIX 1372 1381 {ECO:0000244|PDB:2JZD}.
STRAND 1389 1401 {ECO:0000244|PDB:2JZD}.
HELIX 1407 1417 {ECO:0000244|PDB:2JZD}.
STRAND 1421 1424 {ECO:0000244|PDB:2JZF}.
STRAND 1426 1428 {ECO:0000244|PDB:2JZD}.
HELIX 1429 1431 {ECO:0000244|PDB:2JZD}.
HELIX 1435 1442 {ECO:0000244|PDB:2JZD}.
STRAND 1449 1452 {ECO:0000244|PDB:2JZF}.
HELIX 1457 1467 {ECO:0000244|PDB:2JZD}.
STRAND 1544 1555 {ECO:0000244|PDB:3E9S}.
STRAND 1557 1562 {ECO:0000244|PDB:3E9S}.
HELIX 1567 1571 {ECO:0000244|PDB:3E9S}.
STRAND 1572 1576 {ECO:0000244|PDB:3E9S}.
STRAND 1582 1584 {ECO:0000244|PDB:5E6J}.
HELIX 1588 1590 {ECO:0000244|PDB:3E9S}.
STRAND 1594 1597 {ECO:0000244|PDB:3E9S}.
HELIX 1602 1612 {ECO:0000244|PDB:3E9S}.
HELIX 1619 1630 {ECO:0000244|PDB:3E9S}.
STRAND 1639 1642 {ECO:0000244|PDB:5E6J}.
TURN 1648 1650 {ECO:0000244|PDB:5E6J}.
HELIX 1651 1661 {ECO:0000244|PDB:3E9S}.
STRAND 1667 1669 {ECO:0000244|PDB:3E9S}.
HELIX 1670 1680 {ECO:0000244|PDB:3E9S}.
HELIX 1685 1694 {ECO:0000244|PDB:3E9S}.
HELIX 1705 1713 {ECO:0000244|PDB:3E9S}.
STRAND 1722 1728 {ECO:0000244|PDB:3E9S}.
STRAND 1730 1732 {ECO:0000244|PDB:3E9S}.
STRAND 1734 1740 {ECO:0000244|PDB:3E9S}.
HELIX 1742 1745 {ECO:0000244|PDB:3E9S}.
STRAND 1746 1749 {ECO:0000244|PDB:3E9S}.
HELIX 1753 1758 {ECO:0000244|PDB:3E9S}.
STRAND 1760 1763 {ECO:0000244|PDB:3E9S}.
STRAND 1765 1785 {ECO:0000244|PDB:3E9S}.
STRAND 1790 1793 {ECO:0000244|PDB:3E9S}.
HELIX 1795 1797 {ECO:0000244|PDB:5E6J}.
STRAND 1799 1807 {ECO:0000244|PDB:3E9S}.
STRAND 1810 1826 {ECO:0000244|PDB:3E9S}.
STRAND 1829 1834 {ECO:0000244|PDB:3E9S}.
STRAND 1836 1846 {ECO:0000244|PDB:3E9S}.
STRAND 1904 1911 {ECO:0000244|PDB:2K87}.
HELIX 1912 1921 {ECO:0000244|PDB:2K87}.
STRAND 1929 1936 {ECO:0000244|PDB:2K87}.
STRAND 1942 1948 {ECO:0000244|PDB:2K87}.
HELIX 1949 1951 {ECO:0000244|PDB:2K87}.
HELIX 1954 1956 {ECO:0000244|PDB:2K87}.
STRAND 1963 1966 {ECO:0000244|PDB:2K87}.
STRAND 1969 1971 {ECO:0000244|PDB:2K87}.
HELIX 1977 1990 {ECO:0000244|PDB:2K87}.
HELIX 3251 3254 {ECO:0000244|PDB:5C5O}.
STRAND 3257 3262 {ECO:0000244|PDB:5C5O}.
STRAND 3265 3272 {ECO:0000244|PDB:5C5O}.
STRAND 3275 3279 {ECO:0000244|PDB:5C5O}.
HELIX 3280 3283 {ECO:0000244|PDB:5C5O}.
HELIX 3286 3290 {ECO:0000244|PDB:5C5O}.
HELIX 3294 3299 {ECO:0000244|PDB:5C5O}.
HELIX 3303 3305 {ECO:0000244|PDB:5C5O}.
STRAND 3307 3310 {ECO:0000244|PDB:5C5O}.
STRAND 3313 3315 {ECO:0000244|PDB:5C5O}.
STRAND 3317 3323 {ECO:0000244|PDB:5C5O}.
STRAND 3326 3333 {ECO:0000244|PDB:5C5O}.
STRAND 3340 3343 {ECO:0000244|PDB:5C5O}.
STRAND 3351 3358 {ECO:0000244|PDB:5C5O}.
STRAND 3361 3369 {ECO:0000244|PDB:5C5O}.
HELIX 3379 3381 {ECO:0000244|PDB:2QCY}.
STRAND 3388 3393 {ECO:0000244|PDB:5C5O}.
STRAND 3396 3406 {ECO:0000244|PDB:5C5O}.
TURN 3408 3410 {ECO:0000244|PDB:1UJ1}.
STRAND 3412 3415 {ECO:0000244|PDB:5C5O}.
STRAND 3421 3424 {ECO:0000244|PDB:5C5O}.
STRAND 3427 3430 {ECO:0000244|PDB:5C5O}.
HELIX 3441 3453 {ECO:0000244|PDB:5C5O}.
TURN 3458 3460 {ECO:0000244|PDB:3EBN}.
HELIX 3467 3476 {ECO:0000244|PDB:5C5O}.
STRAND 3477 3479 {ECO:0000244|PDB:1Z1J}.
HELIX 3484 3489 {ECO:0000244|PDB:5C5O}.
HELIX 3491 3497 {ECO:0000244|PDB:5C5O}.
HELIX 3501 3514 {ECO:0000244|PDB:5C5O}.
STRAND 3516 3518 {ECO:0000244|PDB:2BX3}.
STRAND 3521 3523 {ECO:0000244|PDB:1UK4}.
STRAND 3524 3526 {ECO:0000244|PDB:5C5O}.
HELIX 3533 3539 {ECO:0000244|PDB:5C5O}.
TURN 3540 3542 {ECO:0000244|PDB:2QC2}.
HELIX 3837 3855 {ECO:0000244|PDB:2AHM}.
HELIX 3862 3876 {ECO:0000244|PDB:2AHM}.
STRAND 3878 3880 {ECO:0000244|PDB:1YSY}.
HELIX 3881 3905 {ECO:0000244|PDB:2AHM}.
HELIX 3906 3909 {ECO:0000244|PDB:1YSY}.
TURN 3910 3912 {ECO:0000244|PDB:1YSY}.
HELIX 3913 3916 {ECO:0000244|PDB:1YSY}.
HELIX 3922 3924 {ECO:0000244|PDB:2AHM}.
HELIX 3929 3946 {ECO:0000244|PDB:2AHM}.
HELIX 3951 3956 {ECO:0000244|PDB:2AHM}.
TURN 3959 3963 {ECO:0000244|PDB:2AHM}.
TURN 3970 3972 {ECO:0000244|PDB:2AHM}.
HELIX 3973 3987 {ECO:0000244|PDB:2AHM}.
HELIX 3996 4017 {ECO:0000244|PDB:2AHM}.
HELIX 4020 4030 {ECO:0000244|PDB:2AHM}.
STRAND 4034 4037 {ECO:0000244|PDB:2AHM}.
STRAND 4046 4051 {ECO:0000244|PDB:2AHM}.
HELIX 4054 4060 {ECO:0000244|PDB:2AHM}.
STRAND 4065 4068 {ECO:0000244|PDB:2AHM}.
STRAND 4071 4079 {ECO:0000244|PDB:2AHM}.
HELIX 4088 4090 {ECO:0000244|PDB:2AHM}.
TURN 4093 4095 {ECO:0000244|PDB:2AHM}.
HELIX 4096 4098 {ECO:0000244|PDB:2AHM}.
STRAND 4103 4109 {ECO:0000244|PDB:2AHM}.
STRAND 4120 4125 {ECO:0000244|PDB:1UW7}.
STRAND 4127 4131 {ECO:0000244|PDB:1UW7}.
STRAND 4134 4137 {ECO:0000244|PDB:1UW7}.
STRAND 4145 4150 {ECO:0000244|PDB:1UW7}.
STRAND 4153 4155 {ECO:0000244|PDB:1UW7}.
STRAND 4157 4164 {ECO:0000244|PDB:1UW7}.
STRAND 4170 4174 {ECO:0000244|PDB:1UW7}.
STRAND 4181 4186 {ECO:0000244|PDB:1UW7}.
STRAND 4191 4194 {ECO:0000244|PDB:1UW7}.
STRAND 4201 4208 {ECO:0000244|PDB:1UW7}.
HELIX 4213 4222 {ECO:0000244|PDB:1UW7}.
HELIX 4224 4227 {ECO:0000244|PDB:1UW7}.
HELIX 4238 4240 {ECO:0000244|PDB:5C8T}.
HELIX 4243 4248 {ECO:0000244|PDB:2XYQ}.
STRAND 4250 4252 {ECO:0000244|PDB:2XYQ}.
HELIX 4253 4262 {ECO:0000244|PDB:2XYQ}.
STRAND 4284 4288 {ECO:0000244|PDB:2XYQ}.
STRAND 4295 4300 {ECO:0000244|PDB:2XYQ}.
HELIX 4301 4303 {ECO:0000244|PDB:2XYQ}.
HELIX 4305 4308 {ECO:0000244|PDB:2XYQ}.
STRAND 4314 4318 {ECO:0000244|PDB:2XYQ}.
STRAND 4325 4330 {ECO:0000244|PDB:2XYQ}.
HELIX 4331 4333 {ECO:0000244|PDB:2XYQ}.
HELIX 4337 4343 {ECO:0000244|PDB:2XYQ}.
TURN 4348 4350 {ECO:0000244|PDB:2XYQ}.
TURN 4354 4357 {ECO:0000244|PDB:2XYQ}.
STRAND 5922 5924 {ECO:0000244|PDB:5C8T}.
STRAND 5928 5931 {ECO:0000244|PDB:5C8T}.
HELIX 5933 5935 {ECO:0000244|PDB:5C8T}.
STRAND 5955 5957 {ECO:0000244|PDB:5C8T}.
HELIX 5978 5983 {ECO:0000244|PDB:5C8T}.
STRAND 5986 5997 {ECO:0000244|PDB:5C8T}.
STRAND 6000 6002 {ECO:0000244|PDB:5C8T}.
STRAND 6006 6016 {ECO:0000244|PDB:5C8T}.
STRAND 6018 6020 {ECO:0000244|PDB:5C8T}.
STRAND 6024 6028 {ECO:0000244|PDB:5C8T}.
STRAND 6033 6037 {ECO:0000244|PDB:5C8T}.
HELIX 6046 6053 {ECO:0000244|PDB:5C8T}.
HELIX 6054 6057 {ECO:0000244|PDB:5C8T}.
HELIX 6061 6076 {ECO:0000244|PDB:5C8T}.
TURN 6077 6079 {ECO:0000244|PDB:5C8T}.
STRAND 6084 6089 {ECO:0000244|PDB:5C8T}.
HELIX 6091 6100 {ECO:0000244|PDB:5C8T}.
STRAND 6112 6115 {ECO:0000244|PDB:5C8T}.
STRAND 6118 6120 {ECO:0000244|PDB:5C8T}.
TURN 6121 6124 {ECO:0000244|PDB:5C8T}.
STRAND 6125 6127 {ECO:0000244|PDB:5C8T}.
TURN 6129 6131 {ECO:0000244|PDB:5C8T}.
STRAND 6137 6140 {ECO:0000244|PDB:5C8T}.
STRAND 6142 6145 {ECO:0000244|PDB:5C8T}.
HELIX 6146 6149 {ECO:0000244|PDB:5C8T}.
HELIX 6155 6162 {ECO:0000244|PDB:5C8T}.
STRAND 6164 6166 {ECO:0000244|PDB:5C8U}.
HELIX 6172 6188 {ECO:0000244|PDB:5C8T}.
HELIX 6204 6226 {ECO:0000244|PDB:5C8T}.
STRAND 6229 6235 {ECO:0000244|PDB:5C8T}.
STRAND 6242 6245 {ECO:0000244|PDB:5C8T}.
STRAND 6247 6256 {ECO:0000244|PDB:5C8T}.
STRAND 6263 6267 {ECO:0000244|PDB:5C8S}.
HELIX 6272 6275 {ECO:0000244|PDB:5C8T}.
TURN 6276 6278 {ECO:0000244|PDB:5C8T}.
STRAND 6281 6288 {ECO:0000244|PDB:5C8T}.
STRAND 6296 6303 {ECO:0000244|PDB:5C8T}.
STRAND 6312 6314 {ECO:0000244|PDB:5C8T}.
STRAND 6320 6322 {ECO:0000244|PDB:5C8T}.
STRAND 6324 6326 {ECO:0000244|PDB:5C8T}.
STRAND 6328 6330 {ECO:0000244|PDB:5C8T}.
HELIX 6335 6338 {ECO:0000244|PDB:5C8T}.
STRAND 6341 6343 {ECO:0000244|PDB:5C8T}.
STRAND 6373 6376 {ECO:0000244|PDB:5C8T}.
STRAND 6381 6383 {ECO:0000244|PDB:5C8T}.
HELIX 6387 6405 {ECO:0000244|PDB:5C8T}.
STRAND 6408 6412 {ECO:0000244|PDB:5C8T}.
HELIX 6419 6425 {ECO:0000244|PDB:5C8T}.
HELIX 6431 6441 {ECO:0000244|PDB:2H85}.
STRAND 6453 6456 {ECO:0000244|PDB:2H85}.
STRAND 6459 6464 {ECO:0000244|PDB:2H85}.
STRAND 6467 6473 {ECO:0000244|PDB:2H85}.
STRAND 6476 6478 {ECO:0000244|PDB:2H85}.
HELIX 6480 6488 {ECO:0000244|PDB:2H85}.
STRAND 6493 6495 {ECO:0000244|PDB:2OZK}.
HELIX 6498 6503 {ECO:0000244|PDB:2H85}.
STRAND 6508 6513 {ECO:0000244|PDB:2H85}.
TURN 6517 6520 {ECO:0000244|PDB:2H85}.
STRAND 6521 6530 {ECO:0000244|PDB:2H85}.
TURN 6532 6534 {ECO:0000244|PDB:2H85}.
STRAND 6535 6539 {ECO:0000244|PDB:2H85}.
HELIX 6543 6545 {ECO:0000244|PDB:2H85}.
STRAND 6550 6553 {ECO:0000244|PDB:2H85}.
HELIX 6559 6565 {ECO:0000244|PDB:2H85}.
STRAND 6567 6575 {ECO:0000244|PDB:2H85}.
STRAND 6589 6591 {ECO:0000244|PDB:2H85}.
STRAND 6594 6596 {ECO:0000244|PDB:2H85}.
STRAND 6599 6601 {ECO:0000244|PDB:2H85}.
STRAND 6606 6611 {ECO:0000244|PDB:2H85}.
STRAND 6614 6616 {ECO:0000244|PDB:2RHB}.
HELIX 6629 6631 {ECO:0000244|PDB:2H85}.
HELIX 6637 6644 {ECO:0000244|PDB:2H85}.
HELIX 6647 6653 {ECO:0000244|PDB:2H85}.
HELIX 6661 6664 {ECO:0000244|PDB:2H85}.
STRAND 6670 6673 {ECO:0000244|PDB:2H85}.
STRAND 6677 6679 {ECO:0000244|PDB:2OZK}.
HELIX 6680 6689 {ECO:0000244|PDB:2H85}.
STRAND 6692 6698 {ECO:0000244|PDB:2H85}.
STRAND 6703 6711 {ECO:0000244|PDB:2H85}.
TURN 6712 6714 {ECO:0000244|PDB:2H85}.
STRAND 6717 6724 {ECO:0000244|PDB:2H85}.
HELIX 6728 6736 {ECO:0000244|PDB:2H85}.
STRAND 6741 6751 {ECO:0000244|PDB:2H85}.
STRAND 6754 6763 {ECO:0000244|PDB:2H85}.
STRAND 6766 6772 {ECO:0000244|PDB:2H85}.
HELIX 6777 6780 {ECO:0000244|PDB:2XYQ}.
STRAND 6781 6785 {ECO:0000244|PDB:2XYQ}.
HELIX 6788 6791 {ECO:0000244|PDB:2XYQ}.
HELIX 6817 6829 {ECO:0000244|PDB:2XYQ}.
STRAND 6841 6846 {ECO:0000244|PDB:2XYQ}.
HELIX 6855 6863 {ECO:0000244|PDB:2XYQ}.
STRAND 6869 6876 {ECO:0000244|PDB:2XYQ}.
STRAND 6881 6888 {ECO:0000244|PDB:2XYQ}.
HELIX 6890 6892 {ECO:0000244|PDB:2XYQ}.
STRAND 6893 6897 {ECO:0000244|PDB:3R24}.
STRAND 6899 6904 {ECO:0000244|PDB:2XYQ}.
HELIX 6924 6935 {ECO:0000244|PDB:2XYQ}.
STRAND 6936 6946 {ECO:0000244|PDB:2XYQ}.
STRAND 6948 6950 {ECO:0000244|PDB:2XYQ}.
HELIX 6953 6959 {ECO:0000244|PDB:2XYQ}.
STRAND 6962 6970 {ECO:0000244|PDB:2XYQ}.
HELIX 6971 6973 {ECO:0000244|PDB:2XYQ}.
STRAND 6979 6986 {ECO:0000244|PDB:2XYQ}.
HELIX 6996 7009 {ECO:0000244|PDB:2XYQ}.
HELIX 7017 7020 {ECO:0000244|PDB:2XYQ}.
STRAND 7033 7035 {ECO:0000244|PDB:2XYQ}.
HELIX 7039 7041 {ECO:0000244|PDB:2XYQ}.
HELIX 7044 7051 {ECO:0000244|PDB:2XYQ}.
STRAND 7055 7057 {ECO:0000244|PDB:2XYQ}.
STRAND 7065 7067 {ECO:0000244|PDB:3R24}.
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


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