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 R1A_IBVB                Reviewed;        3951 AA.
P0C6V3; P27920;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 56.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a 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=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
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 AND GLN-3928.
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.
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]
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).
-!- 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: 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}.
-!- 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).
{ECO:0000250}.
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6V3-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6Y1-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
-!- 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}.
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EMBL; M94356; AAA46223.1; -; Genomic_RNA.
EMBL; M95169; AAA70233.1; -; Genomic_RNA.
EMBL; DQ001339; AAY24431.1; -; Genomic_RNA.
PIR; A33094; VFIHB1.
PIR; B33094; VFIHB2.
RefSeq; NP_040829.1; NC_001451.1.
ProteinModelPortal; P0C6V3; -.
SMR; P0C6V3; -.
GeneID; 1489740; -.
KEGG; vg:1489740; -.
OrthoDB; VOG09000000; -.
BRENDA; 3.4.22.B14; 8728.
Proteomes; UP000006717; Genome.
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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF08715; Viral_protease; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 1.
1: Evidence at protein level;
Activation of host autophagy by virus; Complete proteome;
Host cytoplasm; Host membrane; Host-virus interaction; Hydrolase;
Membrane; Metal-binding; Protease; Reference proteome; Repeat;
Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
Transmembrane helix; Zinc; Zinc-finger.
CHAIN 1 3951 Replicase polyprotein 1a.
/FTId=PRO_0000338314.
CHAIN 1 673 Non-structural protein 2.
/FTId=PRO_0000338315.
CHAIN 674 2265 Non-structural protein 3.
/FTId=PRO_0000338316.
CHAIN 2266 2779 Non-structural protein 4.
/FTId=PRO_0000338317.
CHAIN 2780 3086 3C-like proteinase.
/FTId=PRO_0000338318.
CHAIN 3087 3379 Non-structural protein 6.
/FTId=PRO_0000338319.
CHAIN 3380 3462 Non-structural protein 7.
/FTId=PRO_0000338320.
CHAIN 3463 3672 Non-structural protein 8.
/FTId=PRO_0000338321.
CHAIN 3673 3783 Non-structural protein 9.
/FTId=PRO_0000338322.
CHAIN 3784 3928 Non-structural protein 10.
/FTId=PRO_0000338323.
CHAIN 3929 3951 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338324.
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}.
ZN_FING 1353 1390 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 3858 3878 {ECO:0000250}.
ZN_FING 3904 3917 {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.
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.
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).
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.
{ECO:0000269|PubMed:10644337}.
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}.
SEQUENCE 3951 AA; 441126 MW; 9B8B2E7E2545F50C 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 LNGYGVAVRL G


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