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 R1AB_IBVB               Reviewed;        6629 AA.
P0C6Y1; P26314; P27920; Q4ZJT1; Q4ZJT2;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 73.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p87;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.22.-;
AltName: Full=Papain-like proteinase;
Short=PL-PRO;
AltName: Full=p195;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
AltName: Full=p41;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p33;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
AltName: Full=p34;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p9;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p24;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
AltName: Full=p10;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
AltName: Full=p16;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
AltName: Full=p100;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
AltName: Full=p68;
Contains:
RecName: Full=Exoribonuclease;
Short=ExoN;
EC=3.1.13.-;
AltName: Full=nsp14;
AltName: Full=p58;
Contains:
RecName: Full=Uridylate-specific endoribonuclease;
EC=3.1.-.-;
AltName: Full=NendoU;
AltName: Full=nsp15;
AltName: Full=p39;
Contains:
RecName: Full=Putative 2'-O-methyl transferase;
EC=2.1.1.-;
AltName: Full=nsp16;
AltName: Full=p35;
Name=rep; ORFNames=1a-1b;
Avian infectious bronchitis virus (strain Beaudette) (IBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Gammacoronavirus.
NCBI_TaxID=11122;
NCBI_TaxID=9031; Gallus gallus (Chicken).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3027249; DOI=10.1099/0022-1317-68-1-57;
Boursnell M.E.G., Brown T.D.K., Foulds I.J., Green P.F., Tomley F.M.,
Binns M.M.;
"Completion of the sequence of the genome of the coronavirus avian
infectious bronchitis virus.";
J. Gen. Virol. 68:57-77(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Vero cell-adapted p65;
PubMed=16137658; DOI=10.1016/j.bbrc.2005.08.105;
Fang S.G., Shen S., Tay F.P., Liu D.X.;
"Selection of and recombination between minor variants lead to the
adaptation of an avian coronavirus to primate cells.";
Biochem. Biophys. Res. Commun. 336:417-423(2005).
[3]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=11831730; DOI=10.1006/viro.1995.1128;
Liu D.X., Tibbles K.W., Cavanagh D., Brown T.D.K., Brierley I.;
"Identification, expression, and processing of an 87-kDa polypeptide
encoded by ORF 1a of the coronavirus infectious bronchitis virus.";
Virology 208:48-57(1995).
[4]
CHARACTERIZATION OF 3CL-PRO, AND MUTAGENESIS OF HIS-2820; GLU-2841;
GLU-2843; CYS-2922; GLN-3928; GLN-4868 AND SER-4869.
PubMed=7778277; DOI=10.1006/viro.1995.1274;
Liu D.X., Brown T.D.K.;
"Characterisation and mutational analysis of an ORF 1a-encoding
proteinase domain responsible for proteolytic processing of the
infectious bronchitis virus 1a/1b polyprotein.";
Virology 209:420-427(1995).
[5]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF GLN-3672 AND
GLN-3783.
PubMed=9032311;
Liu D.X., Xu H.Y., Brown T.D.K.;
"Proteolytic processing of the coronavirus infectious bronchitis virus
1a polyprotein: identification of a 10-kilodalton polypeptide and
determination of its cleavage sites.";
J. Virol. 71:1814-1820(1997).
[6]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF GLN-3462;
GLN-3672 AND GLN-3783.
PubMed=9568037; DOI=10.1006/viro.1998.9058;
Ng L.F.P., Liu D.X.;
"Identification of a 24-kDa polypeptide processed from the coronavirus
infectious bronchitis virus 1a polyprotein by the 3C-like proteinase
and determination of its cleavage sites.";
Virology 243:388-395(1998).
[7]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, CHARACTERIZATION OF PAPAIN-LIKE
PROTEINASE DOMAINS, AND MUTAGENESIS OF GLY-673; THR-676; CYS-1274 AND
HIS-1437.
PubMed=9636369; DOI=10.1006/viro.1998.9164;
Lim K.P., Liu D.X.;
"Characterization of the two overlapping papain-like proteinase
domains encoded in gene 1 of the coronavirus infectious bronchitis
virus and determination of the C-terminal cleavage site of an 87-kDa
protein.";
Virology 245:303-312(1998).
[8]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF GLN-4868;
GLN-5468; GLN-5989 AND GLN-6327.
PubMed=9657947; DOI=10.1006/viro.1998.9199;
Liu D.X., Shen S., Xu H.Y., Wang S.F.;
"Proteolytic mapping of the coronavirus infectious bronchitis virus 1b
polyprotein: evidence for the presence of four cleavage sites of the
3C-like proteinase and identification of two novel cleavage
products.";
Virology 246:288-297(1998).
[9]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, GLYCOSYLATION OF NSP4, AND
MUTAGENESIS OF ALA-2264; GLY-2265 AND GLY-2266.
PubMed=10644337; DOI=10.1128/JVI.74.4.1674-1685.2000;
Lim K.P., Ng L.F.P., Liu D.X.;
"Identification of a novel cleavage activity of the first papain-like
proteinase domain encoded by open reading frame 1a of the coronavirus
avian infectious bronchitis virus and characterization of the cleavage
products.";
J. Virol. 74:1674-1685(2000).
[10]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF GLN-3086;
GLN-3365 AND GLN-3379.
PubMed=10873746; DOI=10.1006/viro.2000.0330;
Ng L.F.P., Liu D.X.;
"Further characterization of the coronavirus infectious bronchitis
virus 3C-like proteinase and determination of a new cleavage site.";
Virology 272:27-39(2000).
[11]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND SUBCELLULAR LOCATION.
PubMed=11601893; DOI=10.1006/viro.2001.1098;
Xu H.Y., Lim K.P., Shen S., Liu D.X.;
"Further identification and characterization of novel intermediate and
mature cleavage products released from the ORF 1b region of the avian
coronavirus infectious bronchitis virus 1a/1b polyprotein.";
Virology 288:212-222(2001).
[12]
APOPTOTIC FUNCTION OF NSP14.
PubMed=11413307; DOI=10.1128/JVI.75.14.6402-6409.2001;
Liu C., Xu H.Y., Liu D.X.;
"Induction of caspase-dependent apoptosis in cultured cells by the
avian coronavirus infectious bronchitis virus.";
J. Virol. 75:6402-6409(2001).
[13]
CHARACTERIZATION OF NSP10, AND MUTAGENESIS.
PubMed=12021359; DOI=10.1128/JVI.76.12.6257-6267.2002;
Ng L.F.P., Liu D.X.;
"Membrane association and dimerization of a cysteine-rich, 16-
kilodalton polypeptide released from the C-terminal region of the
coronavirus infectious bronchitis virus 1a polyprotein.";
J. Virol. 76:6257-6267(2002).
[14]
INTERACTION 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).
-!- FUNCTION: The replicase polyprotein of coronaviruses is a
multifunctional protein: it contains the activities necessary for
the transcription of negative stranded RNA, leader RNA, subgenomic
mRNAs and progeny virion RNA as well as proteinases responsible
for the cleavage of the polyprotein into functional products.
-!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for
the cleavages located at the N-terminus of replicase polyprotein.
Activity of PL-PRO is dependent on zinc (By similarity).
{ECO:0000250}.
-!- FUNCTION: The main proteinase 3CL-PRO is responsible for the
majority of cleavages as it cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog
Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
-!- FUNCTION: The peptide p16 might be involved in the EGF signaling
pathway.
-!- FUNCTION: The helicase which contains a zinc finger structure
displays RNA and DNA duplex-unwinding activities with 5' to 3'
polarity. Its ATPase activity is strongly stimulated by poly(U),
poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity).
{ECO:0000250}.
-!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3'
to 5' direction. {ECO:0000250}.
-!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity
to the polymerase, maybe by binding to dsRNA or by producing
primers utilized by the latter. {ECO:0000250}.
-!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
-!- FUNCTION: NendoU is a Mn(2+)-dependent, uridylate-specific enzyme,
which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. The three
peptides nsp2, nsp3 and nsp4 may form a complex. Nsp9 is a dimer.
Eight copies of nsp7 and eight copies of nsp8 assemble to form a
heterohexadecamer. Nsp10 forms a dodecamer (By similarity).
Interacts with DDX1 (via C-terminus). {ECO:0000250,
ECO:0000269|PubMed:20573827}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- 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=P0C6Y1-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6V3-1; 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}.
-!- PTM: P41 is N-glycosylated. {ECO:0000269|PubMed:10644337}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA46223.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAA46224.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAA70233.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAA70234.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAY24431.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAY24432.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; M94356; AAA46223.1; ALT_SEQ; Genomic_RNA.
EMBL; M94356; AAA46224.1; ALT_SEQ; Genomic_RNA.
EMBL; M95169; AAA70233.1; ALT_SEQ; Genomic_RNA.
EMBL; M95169; AAA70234.1; ALT_SEQ; Genomic_RNA.
EMBL; DQ001339; AAY24431.1; ALT_SEQ; Genomic_RNA.
EMBL; DQ001339; AAY24432.1; ALT_SEQ; Genomic_RNA.
PIR; A33094; VFIHB1.
PIR; B33094; VFIHB2.
PDB; 3EJF; X-ray; 1.60 A; A=1005-1176.
PDB; 3EKE; X-ray; 2.10 A; A=1005-1176.
PDB; 4X2Z; X-ray; 2.15 A; A=1174-1483.
PDB; 5BZ0; X-ray; 2.10 A; A=1174-1483.
PDBsum; 3EJF; -.
PDBsum; 3EKE; -.
PDBsum; 4X2Z; -.
PDBsum; 5BZ0; -.
ProteinModelPortal; P0C6Y1; -.
SMR; P0C6Y1; -.
MEROPS; C16.005; -.
OrthoDB; VOG09000000; -.
EvolutionaryTrace; P0C6Y1; -.
Proteomes; UP000006717; Genome.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR009461; Coronavirus_NSP16.
InterPro; IPR027352; CV_ZBD.
InterPro; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR009466; NSP11.
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; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF06478; Corona_RPol_N; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF06471; NSP11; 1.
Pfam; PF06460; NSP13; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF01443; Viral_helicase1; 1.
Pfam; PF08715; Viral_protease; 1.
SMART; SM00506; A1pp; 1.
SMART; SM00382; AAA; 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; Endonuclease; Exonuclease; Helicase;
Host cytoplasm; Host membrane; Host-virus interaction; Hydrolase;
Membrane; Metal-binding; Methyltransferase; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Transmembrane; Transmembrane helix; Viral RNA replication; Zinc;
Zinc-finger.
CHAIN 1 673 Non-structural protein 2.
/FTId=PRO_0000037404.
CHAIN 674 2265 Non-structural protein 3.
/FTId=PRO_0000037405.
CHAIN 2266 2779 Non-structural protein 4.
/FTId=PRO_0000037406.
CHAIN 2780 3086 3C-like proteinase.
/FTId=PRO_0000037407.
CHAIN 3087 3379 Non-structural protein 6.
/FTId=PRO_0000037408.
CHAIN 3380 3462 Non-structural protein 7.
/FTId=PRO_0000037409.
CHAIN 3463 3672 Non-structural protein 8.
/FTId=PRO_0000037410.
CHAIN 3673 3783 Non-structural protein 9.
/FTId=PRO_0000037411.
CHAIN 3784 3928 Non-structural protein 10.
/FTId=PRO_0000037412.
CHAIN 3929 4868 RNA-directed RNA polymerase.
/FTId=PRO_0000037413.
CHAIN 4869 5468 Helicase.
/FTId=PRO_0000037414.
CHAIN 5469 5989 Exoribonuclease. {ECO:0000250}.
/FTId=PRO_0000037415.
CHAIN 5990 6327 Uridylate-specific endoribonuclease.
{ECO:0000250}.
/FTId=PRO_0000037416.
CHAIN 6328 6629 Putative 2'-O-methyl transferase.
{ECO:0000250}.
/FTId=PRO_0000037417.
TRANSMEM 1721 1741 Helical. {ECO:0000255}.
TRANSMEM 1751 1771 Helical. {ECO:0000255}.
TRANSMEM 1844 1864 Helical. {ECO:0000255}.
TRANSMEM 1887 1907 Helical. {ECO:0000255}.
TRANSMEM 2281 2301 Helical. {ECO:0000255}.
TRANSMEM 2560 2580 Helical. {ECO:0000255}.
TRANSMEM 2589 2609 Helical. {ECO:0000255}.
TRANSMEM 2612 2632 Helical. {ECO:0000255}.
TRANSMEM 2644 2664 Helical. {ECO:0000255}.
TRANSMEM 3101 3121 Helical. {ECO:0000255}.
TRANSMEM 3122 3142 Helical. {ECO:0000255}.
TRANSMEM 3152 3172 Helical. {ECO:0000255}.
TRANSMEM 3189 3209 Helical. {ECO:0000255}.
TRANSMEM 3220 3240 Helical. {ECO:0000255}.
TRANSMEM 3258 3278 Helical. {ECO:0000255}.
TRANSMEM 3297 3317 Helical. {ECO:0000255}.
DOMAIN 1003 1179 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1236 1497 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2780 3086 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 4548 4710 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 4869 4952 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5125 5305 (+)RNA virus helicase ATP-binding.
DOMAIN 5306 5477 (+)RNA virus helicase C-terminal.
ZN_FING 1353 1390 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 3858 3878 {ECO:0000250}.
ZN_FING 3904 3917 {ECO:0000250}.
NP_BIND 5150 5157 ATP. {ECO:0000250}.
REGION 1721 1907 HD1.
REGION 2281 2664 HD2.
REGION 3101 3317 HD3.
COMPBIAS 226 229 Poly-Val.
COMPBIAS 2570 2573 Poly-Val.
ACT_SITE 1274 1274 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1437 1437 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 2820 2820 For 3CL-PRO activity.
ACT_SITE 2922 2922 For 3CL-PRO activity.
METAL 4873 4873 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4876 4876 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4884 4884 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4887 4887 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4894 4894 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4897 4897 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4901 4901 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4907 4907 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4918 4918 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4923 4923 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4940 4940 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4943 4943 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 673 674 Cleavage; by PL-PRO.
SITE 2265 2266 Cleavage; by PL-PRO.
SITE 2779 2780 Cleavage; by 3CL-PRO.
SITE 3086 3087 Cleavage; by 3CL-PRO.
SITE 3379 3380 Cleavage; by 3CL-PRO.
SITE 3462 3463 Cleavage; by 3CL-PRO.
SITE 3672 3673 Cleavage; by 3CL-PRO.
SITE 3783 3784 Cleavage; by 3CL-PRO.
SITE 3928 3929 Cleavage; by 3CL-PRO.
SITE 4868 4869 Cleavage; by 3CL-PRO.
SITE 5468 5469 Cleavage; by 3CL-PRO.
SITE 5989 5990 Cleavage; by 3CL-PRO.
SITE 6327 6328 Cleavage; by 3CL-PRO.
VARIANT 105 105 P -> S (in strain: Isolate Vero cell-
adapted p65).
VARIANT 919 919 K -> E (in strain: Isolate Vero cell-
adapted p65).
VARIANT 932 932 L -> I (in strain: Isolate Vero cell-
adapted p65).
VARIANT 948 948 D -> G (in strain: Isolate Vero cell-
adapted p65).
VARIANT 967 967 A -> D (in strain: Isolate Vero cell-
adapted p65).
VARIANT 1133 1133 L -> S (in strain: Isolate Vero cell-
adapted p65).
VARIANT 1388 1388 P -> S (in strain: Isolate Vero cell-
adapted p65).
VARIANT 1753 1753 L -> F (in strain: Isolate Vero cell-
adapted p65).
VARIANT 2561 2561 Q -> H (in strain: Isolate Vero cell-
adapted p65).
VARIANT 3058 3058 Missing (in strain: Isolate Vero cell-
adapted p65).
VARIANT 3242 3242 N -> S (in strain: Isolate Vero cell-
adapted p65).
VARIANT 3409 3409 V -> A (in strain: Isolate Vero cell-
adapted p65).
VARIANT 3418 3418 I -> T (in strain: Isolate Vero cell-
adapted p65).
VARIANT 3471 3472 IP -> MT (in strain: Isolate Vero cell-
adapted p65).
VARIANT 3751 3751 V -> D (in strain: Isolate Vero cell-
adapted p65).
VARIANT 3870 3870 S -> G (in strain: Isolate Vero cell-
adapted p65).
VARIANT 3935 3935 D -> G (in strain: Isolate Vero cell-
adapted p65).
VARIANT 5085 5085 A -> V (in strain: Isolate Vero cell-
adapted p65).
VARIANT 5968 5968 F -> S (in strain: Isolate Vero cell-
adapted p65).
VARIANT 6221 6221 P -> L (in strain: Isolate Vero cell-
adapted p65).
MUTAGEN 673 673 G->A: No processing between p87 and p195.
{ECO:0000269|PubMed:9636369}.
MUTAGEN 676 676 T->S: No effect.
{ECO:0000269|PubMed:9636369}.
MUTAGEN 1274 1274 C->S: Complete loss of PL-PRO activity.
{ECO:0000269|PubMed:9636369}.
MUTAGEN 1437 1437 H->K: Complete loss of PL-PRO activity.
{ECO:0000269|PubMed:9636369}.
MUTAGEN 2264 2264 A->N: Almost no processing between p195
and peptide HD2.
{ECO:0000269|PubMed:10644337}.
MUTAGEN 2265 2266 Missing: No processing between p195 and
peptide HD2.
MUTAGEN 2265 2265 G->A: No effect.
{ECO:0000269|PubMed:10644337}.
MUTAGEN 2265 2265 G->N: Almost no processing between p195
and peptide HD2.
{ECO:0000269|PubMed:10644337}.
MUTAGEN 2266 2266 G->N: No effect.
{ECO:0000269|PubMed:10644337}.
MUTAGEN 2820 2820 H->K,G: Complete loss of 3CL-PRO
activity. {ECO:0000269|PubMed:7778277}.
MUTAGEN 2841 2841 E->Q: No effect.
{ECO:0000269|PubMed:7778277}.
MUTAGEN 2843 2843 E->D,N,Q: No effect.
{ECO:0000269|PubMed:7778277}.
MUTAGEN 2922 2922 C->A: Complete loss of 3CL-PRO activity.
{ECO:0000269|PubMed:7778277}.
MUTAGEN 2922 2922 C->S: Partial loss of 3CL-PRO activity.
{ECO:0000269|PubMed:7778277}.
MUTAGEN 3086 3086 Q->E: No processing between 3CL-PRO and
p34. {ECO:0000269|PubMed:10873746}.
MUTAGEN 3365 3365 Q->E: No effect.
{ECO:0000269|PubMed:10873746}.
MUTAGEN 3379 3379 Q->E: No processing between p34 and p9.
{ECO:0000269|PubMed:10873746}.
MUTAGEN 3462 3462 Q->E: No processing between p9 and p24.
{ECO:0000269|PubMed:9568037}.
MUTAGEN 3672 3672 Q->E: No processing between p24 and p10.
{ECO:0000269|PubMed:9032311,
ECO:0000269|PubMed:9568037}.
MUTAGEN 3783 3783 Q->E: No processing between p10 and p16.
{ECO:0000269|PubMed:9032311,
ECO:0000269|PubMed:9568037}.
MUTAGEN 3928 3928 Q->E: No processing between p16 and p100.
{ECO:0000269|PubMed:7778277}.
MUTAGEN 4868 4868 Q->E: No processing between p100 and p68.
{ECO:0000269|PubMed:7778277,
ECO:0000269|PubMed:9657947}.
MUTAGEN 4869 4869 S->A,G: No effect.
{ECO:0000269|PubMed:7778277}.
MUTAGEN 5468 5468 Q->M: No processing between p68 and p58.
{ECO:0000269|PubMed:9657947}.
MUTAGEN 5989 5989 Q->E: No processing between p58 and p39.
{ECO:0000269|PubMed:9657947}.
MUTAGEN 6327 6327 Q->E: No processing between p39 and p35.
{ECO:0000269|PubMed:9657947}.
STRAND 1015 1021 {ECO:0000244|PDB:3EJF}.
HELIX 1023 1034 {ECO:0000244|PDB:3EJF}.
STRAND 1035 1042 {ECO:0000244|PDB:3EJF}.
HELIX 1052 1061 {ECO:0000244|PDB:3EJF}.
HELIX 1063 1076 {ECO:0000244|PDB:3EJF}.
STRAND 1080 1084 {ECO:0000244|PDB:3EJF}.
STRAND 1091 1097 {ECO:0000244|PDB:3EJF}.
HELIX 1107 1116 {ECO:0000244|PDB:3EJF}.
STRAND 1125 1129 {ECO:0000244|PDB:3EJF}.
STRAND 1133 1135 {ECO:0000244|PDB:3EKE}.
TURN 1136 1139 {ECO:0000244|PDB:3EKE}.
HELIX 1140 1151 {ECO:0000244|PDB:3EJF}.
STRAND 1157 1163 {ECO:0000244|PDB:3EJF}.
HELIX 1165 1173 {ECO:0000244|PDB:3EJF}.
STRAND 1178 1188 {ECO:0000244|PDB:4X2Z}.
STRAND 1190 1194 {ECO:0000244|PDB:4X2Z}.
HELIX 1200 1203 {ECO:0000244|PDB:4X2Z}.
STRAND 1209 1211 {ECO:0000244|PDB:4X2Z}.
HELIX 1216 1218 {ECO:0000244|PDB:4X2Z}.
STRAND 1224 1226 {ECO:0000244|PDB:4X2Z}.
HELIX 1232 1235 {ECO:0000244|PDB:5BZ0}.
TURN 1236 1239 {ECO:0000244|PDB:5BZ0}.
HELIX 1242 1251 {ECO:0000244|PDB:5BZ0}.
STRAND 1258 1261 {ECO:0000244|PDB:5BZ0}.
STRAND 1264 1267 {ECO:0000244|PDB:5BZ0}.
TURN 1271 1273 {ECO:0000244|PDB:5BZ0}.
HELIX 1274 1285 {ECO:0000244|PDB:5BZ0}.
HELIX 1294 1302 {ECO:0000244|PDB:5BZ0}.
HELIX 1307 1316 {ECO:0000244|PDB:5BZ0}.
HELIX 1327 1335 {ECO:0000244|PDB:5BZ0}.
TURN 1342 1344 {ECO:0000244|PDB:5BZ0}.
STRAND 1346 1353 {ECO:0000244|PDB:5BZ0}.
STRAND 1356 1363 {ECO:0000244|PDB:5BZ0}.
HELIX 1364 1368 {ECO:0000244|PDB:5BZ0}.
STRAND 1369 1376 {ECO:0000244|PDB:5BZ0}.
HELIX 1377 1381 {ECO:0000244|PDB:5BZ0}.
STRAND 1382 1386 {ECO:0000244|PDB:5BZ0}.
TURN 1388 1390 {ECO:0000244|PDB:5BZ0}.
STRAND 1393 1413 {ECO:0000244|PDB:5BZ0}.
STRAND 1415 1418 {ECO:0000244|PDB:5BZ0}.
STRAND 1424 1431 {ECO:0000244|PDB:5BZ0}.
STRAND 1435 1442 {ECO:0000244|PDB:5BZ0}.
STRAND 1445 1447 {ECO:0000244|PDB:5BZ0}.
STRAND 1458 1473 {ECO:0000244|PDB:5BZ0}.
SEQUENCE 6629 AA; 744540 MW; 887FCAF7EA68A270 CRC64;
MASSLKQGVS PKPRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAVRQ KFDRSLQTGK
QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI FGVSPLARKY RELLKTACQW
SLTVEALDVR AQTLDEIFDP TEILWLQVAA KIHVSSMAMR RLVGEVTAKV MDALGSNLSA
LFQIVKQQIA RIFQKALAIF ENVNELPQRI AALKMAFAKC ARSITVVVVE RTLVVKEFAG
TCLASINGAV AKFFEELPNG FMGSKIFTTL AFFKEAAVRV VENIPNAPRG TKGFEVVGNA
KGTQVVVRGM RNDLTLLDQK ADIPVEPEGW SAILDGHLCY VFRSGDRFYA APLSGNFALS
DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVSELVTA LKKGEPFKFL GHKFVYAKDA
AVSFTLAKAA TIADVLRLFQ SARVIAEDVW SSFTEKSFEF WKLAYGKVRN LEEFVKTYVC
KAQMSIVILA AVLGEDIWHL VSQVIYKLGV LFTKVVDFCD KHWKGFCVQL KRAKLIVTET
FCVLKGVAQH CFQLLLDAIH SLYKSFKKCA LGRIHGDLLF WKGGVHKIVQ DGDEIWFDAI
DSVDVEDLGV VQEKSIDFEV CDDVTLPENQ PGHMVQIEDD GKNYMFFRFK KDENIYYTPM
SQLGAINVVC KAGGKTVTFG ETTVQEIPPP DVVPIKVSIE CCGEPWNTIF KKAYKEPIEV
DTDLTVEQLL SVIYEKMCDD LKLFPEAPEP PPFENVALVD KNGKDLDCIK SCHLIYRDYE
SDDDIEEEDA EECDTDSGEA EECDTNSECE EEDEDTKVLA LIQDPASIKY PLPLDEDYSV
YNGCIVHKDA LDVVNLPSGE ETFVVNNCFE GAVKPLPQKV VDVLGDWGEA VDAQEQLCQQ
EPLQHTFEEP VENSTGSSKT MTEQVVVEDQ ELPVVEQDQD VVVYTPTDLE VAKETAEEVD
EFILIFAVPK EEVVSQKDGA QIKQEPIQVV KPQREKKAKK FKVKPATCEK PKFLEYKTCV
GDLTVVIAKA LDEFKEFCIV NAANEHMTHG SGVAKAIADF CGLDFVEYCE DYVKKHGPQQ
RLVTPSFVKG IQCVNNVVGP RHGDNNLHEK LVAAYKNVLV DGVVNYVVPV LSLGIFGVDF
KMSIDAMREA FEGCTIRVLL FSLSQEHIDY FDVTCKQKTI YLTEDGVKYR SIVLKPGDSL
GQFGQVYAKN KIVFTADDVE DKEILYVPTT DKSILEYYGL DAQKYVIYLQ TLAQKWNVQY
RDNFLILEWR DGNCWISSAI VLLQAAKIRF KGFLTEAWAK LLGGDPTDFV AWCYASCTAK
VGDFSDANWL LANLAEHFDA DYTNAFLKKR VSCNCGIKSY ELRGLEACIQ PVRATNLLHF
KTQYSNCPTC GANNTDEVIE ASLPYLLLFA TDGPATVDCD EDAVGTVVFV GSTNSGHCYT
QAAGQAFDNL AKDRKFGKKS PYITAMYTRF AFKNETSLPV AKQSKGKSKS VKEDVSNLAT
SSKASFDNLT DFEQWYDSNI YESLKVQESP DNFDKYVSFT TKEDSKLPLT LKVRGIKSVV
DFRSKDGFIY KLTPDTDENS KAPVYYPVLD AISLKAIWVE GNANFVVGHP NYYSKSLHIP
TFWENAENFV KMGDKIGGVT MGLWRAEHLN KPNLERIFNI AKKAIVGSSV VTTQCGKLIG
KAATFIADKV GGGVVRNITD SIKGLCGITR GHFERKMSPQ FLKTLMFFLF YFLKASVKSV
VASYKTVLCK VVLATLLIVW FVYTSNPVMF TGIRVLDFLF EGSLCGPYKD YGKDSFDVLR
YCADDFICRV CLHDKDSLHL YKHAYSVEQV YKDAASGFIF NWNWLYLVFL ILFVKPVAGF
VIICYCVKYL VLNSTVLQTG VCFLDWFVQT VFSHFNFMGA GFYFWLFYKI YIQVHHILYC
KDVTCEVCKR VARSNRQEVS VVVGGRKQIV HVYTNSGYNF CKRHNWYCRN CDDYGHQNTF
MSPEVAGELS EKLKRHVKPT AYAYHVVDEA CLVDDFVNLK YKAATPGKDS ASSAVKCFSV
TDFLKKAVFL KEALKCEQIS NDGFIVCNTQ SAHALEEAKN AAIYYAQYLC KPILILDQAL
YEQLVVEPVS KSVIDKVCSI LSSIISVDTA ALNYKAGTLR DALLSITKDE EAVDMAIFCH
NHDVDYTGDG FTNVIPSYGI DTGKLTPRDR GFLINADASI ANLRVKNAPP VVWKFSELIK
LSDSCLKYLI SATVKSGVRF FITKSGAKQV IACHTQKLLV EKKAGGIVSG TFKCFKSYFK
WLLIFYILFT ACCSGYYYME VSKSFVHPMY DVNSTLHVEG FKVIDKGVLR EIVPEDTCFS
NKFVNFDAFW GRPYDNSRNC PIVTAVIDGD GTVATGVPGF VSWVMDGVMF IHMTQTERKP
WYIPTWFNRE IVGYTQDSII TEGSFYTSIA LFSARCLYLT ASNTPQLYCF NGDNDAPGAL
PFGSIIPHRV YFQPNGVRLI VPQQILHTPY VVKFVSDSYC RGSVCEYTRP GYCVSLNPQW
VLFNDEYTSK PGVFCGSTVR ELMFSMVSTF FTGVNPNIYM QLATMFLILV VVVLIFAMVI
KFQGVFKAYA TTVFITMLVW VINAFILCVH SYNSVLAVIL LVLYCYASLV TSRNTVIIMH
CWLVFTFGLI VPTWLACCYL GFIIYMYTPL FLWCYGTTKN TRKLYDGNEF VGNYDLAAKS
TFVIRGSEFV KLTNEIGDKF EAYLSAYARL KYYSGTGSEQ DYLQACRAWL AYALDQYRNS
GVEIVYTPPR YSIGVSRLQS GFKKLVSPSS AVEKCIVSVS YRGNNLNGLW LGDTIYCPRH
VLGKFSGDQW NDVLNLANNH EFEVTTQHGV TLNVVSRRLK GAVLILQTAV ANAETPKYKF
IKANCGDSFT IACAYGGTVV GLYPVTMRSN GTIRASFLAG ACGSVGFNIE KGVVNFFYMH
HLELPNALHT GTDLMGEFYG GYVDEEVAQR VPPDNLVTNN IVAWLYAAII SVKESSFSLP
KWLESTTVSV DDYNKWAGDN GFTPFSTSTA ITKLSAITGV DVCKLLRTIM VKNSQWGGDP
ILGQYNFEDE LTPESVFNQI GGVRLQSSFV RKATSWFWSR CVLACFLFVL CAIVLFTAVP
LKFYVYAAVI LLMAVLFISF TVKHVMAYMD TFLLPTLITV IIGVCAEVPF IYNTLISQVV
IFLSQWYDPV VFDTMVPWMF LPLVLYTAFK CVQGCYMNSF NTSLLMLYQF VKLGFVIYTS
SNTLTAYTEG NWELFFELVH TTVLANVSSN SLIGLFVFKC AKWMLYYCNA TYLNNYVLMA
VMVNCIGWLC TCYFGLYWWV NKVFGLTLGK YNFKVSVDQY RYMCLHKINP PKTVWEVFST
NILIQGIGGD RVLPIATVQA KLSDVKCTTV VLMQLLTKLN VEANSKMHVY LVELHNKILA
SDDVGECMDN LLGMLITLFC IDSTIDLSEY CDDILKRSTV LQSVTQEFSH IPSYAEYERA
KNLYEKVLVD SKNGGVTQQE LAAYRKAANI AKSVFDRDLA VQKKLDSMAE RAMTTMYKEA
RVTDRRAKLV SSLHALLFSM LKKIDSEKLN VLFDQASSGV VPLATVPIVC SNKLTLVIPD
PETWVKCVEG VHVTYSTVVW NIDTVIDADG TELHPTSTGS GLTYCISGAN IAWPLKVNLT
RNGHNKVDVV LQNNELMPHG VKTKACVAGV DQAHCSVESK CYYTNISGNS VVAAITSSNP
NLKVASFLNE AGNQIYVDLD PPCKFGMKVG VKVEVVYLYF IKNTRSIVRG MVLGAISNVV
VLQSKGHETE EVDAVGILSL CSFAVDPADT YCKYVAAGNQ PLGNCVKMLT VHNGSGFAIT
SKPSPTPDQD SYGGASVCLY CRAHIAHPGS VGNLDGRCQF KGSFVQIPTT EKDPVGFCLR
NKVCTVCQCW IGYGCQCDSL RQPKSSVQSV AGASDFDKNY LNRVRGSSEA RLIPLASGCD
PDVVKRAFDV CNKESAGMFQ NLKRNCARFQ ELRDTEDGNL EYLDSYFVVK QTTPSNYEHE
KSCYEDLKSE VTADHDFFVF NKNIYNISRQ RLTKYTMMDF CYALRHFDPK DCEVLKEILV
TYGCIEDYHP KWFEENKDWY DPIENSKYYV MLAKMGPIVR RALLNAIEFG NLMVEKGYVG
VITLDNQDLN GKFYDFGDFQ KTAPGAGVPV FDTYYSYMMP IIAMTDALAP ERYFEYDVHK
GYKSYDLLKY DYTEEKQELF QKYFKYWDQE YHPNCRDCSD DRCLIHCANF NILFSTLIPQ
TSFGNLCRKV FVDGVPFIAT CGYHSKELGV IMNQDNTMSF SKMGLSQLMQ FVGDPALLVG
TSNNLVDLRT SCFSVCALTS GITHQTVKPG HFNKDFYDFA EKAGMFKEGS SIPLKHFFYP
QTGNAAINDY DYYRYNRPTM FDICQLLFCL EVTSKYFECY EGGCIPASQV VVNNLDKSAG
YPFNKFGKAR LYYEMSLEEQ DQLFEITKKN VLPTITQMNL KYAISAKNRA RTVAGVSILS
TMTNRQFHQK ILKSIVNTRN ASVVIGTTKF YGGWDNMLRN LIQGVEDPIL MGWDYPKCDR
AMPNLLRIAA SLVLARKHTN CCSWSERIYR LYNECAQVLS ETVLATGGIY VKPGGTSSGD
ATTAYANSVF NIIQATSANV ARLLSVITRD IVYDNIKSLQ YELYQQVYRR VNFDPAFVEK
FYSYLCKNFS LMILSDDGVV CYNNTLAKQG LVADISGFRE VLYYQNNVFM ADSKCWVEPD
LEKGPHEFCS QHTMLVEVDG EPKYLPYPDP SRILGACVFV DDVDKTEPVA VMERYIALAI
DAYPLVHHEN EEYKKVFFVL LAYIRKLYQE LSQNMLMDYS FVMDIDKGSK FWEQEFYENM
YRAPTTLQSC GVCVVCNSQT ILRCGNCIRK PFLCCKCCYD HVMHTDHKNV LSINPYICSQ
LGCGEADVTK LYLGGMSYFC GNHKPKLSIP LVSNGTVFGI YRANCAGSEN VDDFNQLATT
NWSIVEPYIL ANRCSDSLRR FAAETVKATE ELHKQQFASA EVREVFSDRE LILSWEPGKT
RPPLNRNYVF TGYHFTRTSK VQLGDFTFEK GEGKDVVYYK ATSTAKLSVG DIFVLTSHNV
VSLVAPTLCP QQTFSRFVNL RPNVMVPECF VNNIPLYHLV GKQKRTTVQG PPGSGKSHFA
IGLAVYFSSA RVVFTACSHA AVDALCEKAF KFLKVDDCTR IVPQRTTVDC FSKFKANDTG
KKYIFSTINA LPEVSCDILL VDEVSMLTNY ELSFINGKIN YQYVVYVGDP AQLPAPRTLL
NGSLSPKDYN VVTNLMVCVK PDIFLAKCYR CPKEIVDTVS TLVYDGKFIA NNPESRECFK
VIVNNGNSDV GHESGSAYNT TQLEFVKDFV CRNKQWREAI FISPYNAMNQ RAYRMLGLNV
QTVDSSQGSE YDYVIFCVTA DSQHALNINR FNVALTRAKR GILVVMRQRD ELYSALKFTE
LDSETSLQGT GLFKICNKEF SGVHPAYAVT TKALAATYKV NDELAALVNV EAGSEITYKH
LISLLGFKMS VNVEGCHNMF ITRDEAIRNV RGWVGFDVEA THACGTNIGT NLPFQVGFST
GADFVVTPEG LVDTSIGNNF EPVNSKAPPG EQFNHLRVLF KSAKPWHVIR PRIVQMLADN
LCNVSDCVVF VTWCHGLELT TLRYFVKIGK EQVCSCGSRA TTFNSHTQAY ACWKHCLGFD
FVYNPLLVDI QQWGYSGNLQ FNHDLHCNVH GHAHVASVDA IMTRCLAINN AFCQDVNWDL
TYPHIANEDE VNSSCRYLQR MYLNACVDAL KVNVVYDIGN PKGIKCVRRG DVNFRFYDKN
PIVRNVKQFE YDYNQHKDKF ADGLCMFWNC NVDCYPDNSL VCRYDTRNLS VFNLPGCNGG
SLYVNKHAFY TPKFDRISFR NLKAMPFFFY DSSPCETIQV DGVAQDLVSL ATKDCITKCN
IGGAVCKKHA QMYAEFVTSY NAAVTAGFTF WVTNKLNPYN LWKSFSALQS IDNIAYNMYK
GGHYDAIAGE MPTVITGDKV FVIDQGVEKA VFVNQTTLPT SVAFELYAKR NIRTLPNNRI
LKGLGVDVTN GFVIWDYANQ TPLYRNTVKV CAYTDIEPNG LVVLYDDRYG DYQSFLAADN
AVLVSTQCYK RYSYVEIPSN LLVQNGMPLK DGANLYVYKR VNGAFVTLPN TINTQGRSYE
TFEPRSDIER DFLAMSEESF VERYGKDLGL QHILYGEVDK PQLGGLHTVI GMYRLLRANK
LNAKSVTNSD SDVMQNYFVL SDNGSYKQVC TVVDLLLDDF LELLRNILKE YGTNKSKVVT
VSIDYHSINF MTWFEDGSIK TCYPQLQSAW TCGYNMPELY KVQNCVMEPC NIPNYGVGIT
LPSGILMNVA KYTQLCQYLS KTTICVPHNM RVMHFGAGSD KGVAPGSTVL KQWLPEGTLL
VDNDIVDYVS DAHVSVLSDC NKYNTEHKFD LVISDMYTDN DSKRKHEGVI ANNGNDDVFI
YLSSFLRNNL ALGGSFAVKV TETSWHEVLY DIAQDCAWWT MFCTAVNASS SEAFLIGVNY
LGASEKVKVS GKTLHANYIF WRNCNYLQTS AYSIFDVAKF DLRLKATPVV NLKTEQKTDL
VFNLIKCGKL LVRDVGNTSF TSDSFVCTM


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