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Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]

 R1A_CVMA5               Reviewed;        4468 AA.
P0C6V0; P16342;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
28-MAR-2018, entry version 67.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=p28;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=PL1-PRO/PL2-PRO;
AltName: Full=PL1/PL2;
AltName: Full=Papain-like proteinases 1/2;
AltName: Full=p210;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
AltName: Full=p44;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p27;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p10;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p22;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
AltName: Full=p12;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
AltName: Full=p15;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=11142;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8291254; DOI=10.1006/viro.1994.1088;
Bonilla P.J., Gorbalenya A.E., Weiss S.R.;
"Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a:
heterogeneity among MHV strains.";
Virology 198:736-740(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate C12 mutant;
PubMed=9426441; DOI=10.1006/viro.1997.8877;
Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E.,
Weiss S.R.;
"Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is
associated with a Q159L amino acid substitution in the spike
protein.";
Virology 239:1-10(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-597.
PubMed=2545027; DOI=10.1016/0042-6822(89)90520-5;
Pachuk C.J., Bredenbeek P.J., Zoltick P.W., Spaan W.J.M., Weiss S.R.;
"Molecular cloning of the gene encoding the putative polymerase of
mouse hepatitis coronavirus, strain A59.";
Virology 171:141-148(1989).
[4]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND CHARACTERIZATION OF NSP8.
PubMed=9499085;
Lu X.T., Sims A.C., Denison M.R.;
"Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton
protein from the open reading frame 1a polyprotein in virus-infected
cells and in vitro.";
J. Virol. 72:2265-2271(1998).
[5]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF PHE-3331;
LEU-3332; GLN-3333; SER-3334; GLY-3335; ILE-3336 AND CYS-3478.
PubMed=10544119; DOI=10.1006/viro.1999.9954;
Pinon J.D., Teng H., Weiss S.R.;
"Further requirements for cleavage by the murine coronavirus 3C-like
proteinase: identification of a cleavage site within ORF1b.";
Virology 263:471-484(1999).
[6]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND CHARACTERIZATION OF NSP7;
NSP9 AND NSP10.
PubMed=10708455; DOI=10.1128/JVI.74.7.3379-3387.2000;
Bost A.G., Carnahan R.H., Lu X.T., Denison M.R.;
"Four proteins processed from the replicase gene polyprotein of mouse
hepatitis virus colocalize in the cell periphery and adjacent to sites
of virion assembly.";
J. Virol. 74:3379-3387(2000).
-!- FUNCTION: The papain-like proteinase 1 (PL1-PRO) and papain-like
proteinase 2 (PL2-PRO) are responsible for the cleavages located
at the N-terminus of the replicase polyprotein. In addition, PLP2
possesses a deubiquitinating/deISGylating activity and processes
both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
cellular substrates. Antagonizes innate immune induction of type I
interferon by blocking the phosphorylation, dimerization and
subsequent nuclear translocation of host IRF-3 (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. Also contains an ADP-ribose-1''-
phosphate (ADRP)-binding function (By similarity).
{ECO:0000255|PROSITE-ProRule:PRU00772}.
-!- 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: Non-structural protein 1: binds to the 40S ribosomal
subunit and inhibits host translation. The nsp1-40S ribosome
complex further induces an endonucleolytic cleavage near the 5'UTR
of host mRNAs, targeting them for degradation. By suppressing host
gene expression, nsp1 facilitates efficient viral gene expression
in infected cells and evasion from host immune response (By
similarity). {ECO:0000250}.
-!- 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.
-!- 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).
-!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of
nsp7 and eight copies of nsp8 assemble to form a
heterohexadecamer. Nsp9 is a dimer. 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.
-!- 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.
-!- 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.
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6V0-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X9-1; 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}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; X73559; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AF029248; AAB86820.1; -; Genomic_RNA.
EMBL; M27198; AAA74011.1; -; Genomic_RNA.
PIR; A32440; A32440.
PIR; S15760; S15760.
RefSeq; NP_045298.1; NC_001846.1.
PDB; 2M0A; NMR; -; A=833-946.
PDBsum; 2M0A; -.
ProteinModelPortal; P0C6V0; -.
SMR; P0C6V0; -.
PRIDE; P0C6V0; -.
GeneID; 1489749; -.
KEGG; vg:1489749; -.
OrthoDB; VOG09000000; -.
BRENDA; 3.4.22.B14; 3442.
Proteomes; UP000007192; Genome.
GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
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:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0097264; P:self proteolysis; IMP:CACAO.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 1.10.150.420; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 3.10.20.350; -; 1.
InterPro; IPR022570; B-CoV_NSP1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR038123; NSP4_C_sf.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR002705; Pept_C30/C16_B_coronavir.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR038083; pp1a/1ab.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF11963; DUF3477; 2.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF01831; Peptidase_C16; 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; SSF159936; SSF159936; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus;
Complete proteome; Decay of host mRNAs by virus;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; 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 IRF3 by virus; Inhibition of host ISG15 by virus;
Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
Thiol protease; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 4468 Replicase polyprotein 1a.
/FTId=PRO_0000338278.
CHAIN 1 247 Non-structural protein 1. {ECO:0000305}.
/FTId=PRO_0000338279.
CHAIN 248 832 Non-structural protein 2. {ECO:0000305}.
/FTId=PRO_0000338280.
CHAIN 833 2837 Non-structural protein 3. {ECO:0000305}.
/FTId=PRO_0000338281.
CHAIN 2838 3333 Non-structural protein 4.
/FTId=PRO_0000338282.
CHAIN 3334 3635 3C-like proteinase.
/FTId=PRO_0000338283.
CHAIN 3636 3921 Non-structural protein 6. {ECO:0000305}.
/FTId=PRO_0000338284.
CHAIN 3922 4013 Non-structural protein 7.
/FTId=PRO_0000338285.
CHAIN 4014 4207 Non-structural protein 8.
/FTId=PRO_0000338286.
CHAIN 4208 4317 Non-structural protein 9.
/FTId=PRO_0000338287.
CHAIN 4318 4454 Non-structural protein 10.
/FTId=PRO_0000338288.
CHAIN 4455 4468 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338289.
TRANSMEM 2286 2306 Helical. {ECO:0000255}.
TRANSMEM 2314 2334 Helical. {ECO:0000255}.
TRANSMEM 2400 2420 Helical. {ECO:0000255}.
TRANSMEM 2442 2462 Helical. {ECO:0000255}.
TRANSMEM 2625 2645 Helical. {ECO:0000255}.
TRANSMEM 2847 2867 Helical. {ECO:0000255}.
TRANSMEM 3096 3116 Helical. {ECO:0000255}.
TRANSMEM 3118 3138 Helical. {ECO:0000255}.
TRANSMEM 3150 3170 Helical. {ECO:0000255}.
TRANSMEM 3177 3197 Helical. {ECO:0000255}.
TRANSMEM 3202 3222 Helical. {ECO:0000255}.
TRANSMEM 3644 3664 Helical. {ECO:0000255}.
TRANSMEM 3674 3694 Helical. {ECO:0000255}.
TRANSMEM 3699 3719 Helical. {ECO:0000255}.
TRANSMEM 3742 3762 Helical. {ECO:0000255}.
TRANSMEM 3769 3789 Helical. {ECO:0000255}.
TRANSMEM 3796 3816 Helical. {ECO:0000255}.
TRANSMEM 3840 3860 Helical. {ECO:0000255}.
DOMAIN 1084 1333 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1323 1482 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1678 1937 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3334 3635 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1198 1226 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1794 1830 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4391 4407 {ECO:0000250}.
ZN_FING 4433 4446 {ECO:0000250}.
REGION 2225 2645 HD1.
REGION 2847 3222 HD2.
REGION 3526 3860 HD3.
ACT_SITE 1121 1121 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1272 1272 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1716 1716 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1873 1873 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3374 3374 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3478 3478 For 3CL-PRO activity.
SITE 247 248 Cleavage; by PL1-PRO. {ECO:0000305}.
SITE 832 833 Cleavage; by PL1-PRO. {ECO:0000305}.
SITE 2837 2838 Cleavage; by PL2-PRO.
SITE 3333 3334 Cleavage; by 3CL-PRO.
SITE 3635 3636 Cleavage; by 3CL-PRO.
SITE 3921 3922 Cleavage; by 3CL-PRO.
SITE 4013 4014 Cleavage; by 3CL-PRO.
SITE 4207 4208 Cleavage; by 3CL-PRO.
SITE 4317 4318 Cleavage; by 3CL-PRO.
SITE 4454 4455 Cleavage; by 3CL-PRO.
VARIANT 1699 1699 P -> S (in strain: Isolate C12 mutant).
VARIANT 2196 2196 M -> K (in strain: Isolate C12 mutant).
MUTAGEN 3331 3331 F->A,H,W: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3332 3332 L->I,S: No processing between peptide HD2
and 3CL-PRO.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3333 3333 Q->A,K,R: No processing between peptide
HD2 and 3CL-PRO.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3334 3334 S->A: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3334 3334 S->C: No processing between peptide HD2
and 3CL-PRO.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3335 3335 G->A: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3335 3335 G->P: No processing between peptide HD2
and 3CL-PRO.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3336 3336 I->L: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3478 3478 C->A: Complete loss of 3CL-PRO activity.
{ECO:0000269|PubMed:10544119}.
CONFLICT 287 288 WR -> CA (in Ref. 3). {ECO:0000305}.
CONFLICT 311 311 L -> V (in Ref. 3). {ECO:0000305}.
CONFLICT 570 570 D -> G (in Ref. 3). {ECO:0000305}.
CONFLICT 3620 3620 E -> EL (in Ref. 2). {ECO:0000305}.
CONFLICT 3711 3711 T -> TL (in Ref. 2). {ECO:0000305}.
CONFLICT 3968 3968 M -> V (in Ref. 2). {ECO:0000305}.
STRAND 840 842 {ECO:0000244|PDB:2M0A}.
STRAND 849 853 {ECO:0000244|PDB:2M0A}.
STRAND 859 861 {ECO:0000244|PDB:2M0A}.
HELIX 862 870 {ECO:0000244|PDB:2M0A}.
STRAND 874 877 {ECO:0000244|PDB:2M0A}.
HELIX 882 896 {ECO:0000244|PDB:2M0A}.
HELIX 904 907 {ECO:0000244|PDB:2M0A}.
HELIX 909 918 {ECO:0000244|PDB:2M0A}.
STRAND 923 930 {ECO:0000244|PDB:2M0A}.
STRAND 935 942 {ECO:0000244|PDB:2M0A}.
SEQUENCE 4468 AA; 496341 MW; 53FB55E845B646A5 CRC64;
MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK GKTLVNHVRV
NCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG SAVLVKPSKR LSIQAWTNLG
VLPKTAAMGL FKRVCLCNTR ECSCDAHVAF HLFTVQPDGV CLGNGRFIGW FVPVTAIPEY
AKQWLQPWSI LLRKGGNKGS VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSCKAYA
LLKGYRGVKP ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELFPVWRDS LDSEVLVAWH
VDRDPRAAMR LQTLATVRCI DYVGQPTEDV VDGDVVVREP AHLLAANAIV KRLPRLVETM
LYTDSSVTEF CYKTKLCECG FITQFGYVDC CGDTCDFRGW VAGNMMDGFP CPGCTKNYMP
WELEAQSSGV IPEGGVLFTQ STDTVNRESF KLYGHAVVPF GSAVYWSPCP GMWLPVIWSS
VKSYSGLTYT GVVGCKAIVQ ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN
RGDYSLLLEN VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN
FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT EWFDLAVDIA
ASAAGWLCYQ LVNGLFAVAN GVITFVQEVP ELVKNFVDKF KAFFKVLIDS MSVSILSGLT
VVKTASNRVC LAGSKVYEVV QKSLSAYVMP VGCSEATCLV GEIEPAVFED DVVDVVKAPL
TYQGCCKPPT SFEKICIVDK LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVEFND
KPKVRKIPST RKIKITFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
KEHDVIGTKV CALLDRLAGD YVYLFDEGGD EVIAPRMYCS FSAPDDEDCV AADVVDADEN
QDDDAEDSAV LVADTQEEDG VAKGQVEADS EICVAHTGSQ EELAEPDAVG SQTPIASAEE
TEVGEASDRE GIAEAKATVC ADAVDACPDQ VEAFEIEKVE DSILDELQTE LNAPADKTYE
DVLAFDAVCS EALSAFYAVP SDETHFKVCG FYSPAIERTN CWLRSTLIVM QSLPLEFKDL
EMQKLWLSYK AGYDQCFVDK LVKSVPKSII LPQGGYVADF AYFFLSQCSF KAYANWRCLE
CDMELKLQGL DAMFFYGDVV SHMCKCGNSM TLLSADIPYT LHFGVRDDKF CAFYTPRKVF
RAACAVDVND CHSMAVVEGK QIDGKVVTKF IGDKFDFMVG YGMTFSMSPF ELAQLYGSCI
TPNVCFVKGD VIKVVRLVNA EVIVNPANGR MAHGAGVAGA IAEKAGSAFI KETSDMVKAQ
GVCQVGECYE SAGGKLCKKV LNIVGPDARG HGKQCYSLLE RAYQHINKCD NVVTTLISAG
IFSVPTDVSL TYLLGVVTKN VILVSNNQDD FDVIEKCQVT SVAGTKALSL QLAKNLCRDV
KFVTNACSSL FSESCFVSSY DVLQEVEALR HDIQLDDDAR VFVQANMDCL PTDWRLVNKF
DSVDGVRTIK YFECPGGIFV SSQGKKFGYV QNGSFKEASV SQIRALLANK VDVLCTVDGV
NFRSCCVAEG EVFGKTLGSV FCDGINVTKV RCSAIYKGKV FFQYSDLSEA DLVAVKDAFG
FDEPQLLKYY TMLGMCKWPV VVCGNYFAFK QSNNNCYINV ACLMLQHLSL KFPKWQWQEA
WNEFRSGKPL RFVSLVLAKG SFKFNEPSDS IDFMRVVLRE ADLSGATCNL EFVCKCGVKQ
EQRKGVDAVM HFGTLDKGDL VRGYNIACTC GSKLVHCTQF NVPFLICSNT PEGRKLPDDV
VAANIFTGGS VGHYTHVKCK PKYQLYDACN VNKVSEAKGN FTDCLYLKNL KQTFSSVLTT
FYLDDVKCVE YKPDLSQYYC ESGKYYTKPI IKAQFRTFEK VDGVYTNFKL VGHSIAEKLN
AKLGFDCNSP FVEYKITEWP TATGDVVLAS DDLYVSRYSS GCITFGKPVV WLGHEEASLK
SLTYFNRPSV VCENKFNVLP VDVSEPTDKG PVPAAVLVTG VPGADASAGA GIAKEQKACA
SASVEDQVVT EVRQEPSVSA ADVKEVKLNG VKKPVKVEGS VVVNDPTSET KVVKSLSIVD
VYDMFLTGCK YVVWTANELS RLVNSPTVRE YVKWGMGKIV TPAKLLLLRD EKQEFVAPKV
VKAKAIACYC AVKWFLLYCF SWIKFNTDNK VIYTTEVASK LTFKLCCLAF KNALQTFNWS
VVSRGFFLVA TVFLLWFNFL YANVILSDFY LPNIGPLPTF VGQIVAWFKT TFGVSTICDF
YQVTDLGYRS SFCNGSMVCE LCFSGFDMLD NYDAINVVQH VVDRRLSFDY ISLFKLVVEL
VIGYSLYTVC FYPLFVLIGM QLLTTWLPEF FMLETMHWSA RLFVFVANML PAFTLLRFYI
VVTAMYKVYC LCRHVMYGCS KPGCLFCYKR NRSVRVKCST VVGGSLRYYD VMANGGTGFC
TKHQWNCLNC NSWKPGNTFI THEAAADLSK ELKRPVNPTD SAYYSVTEVK QVGCSMRLFY
ERDGQRVYDD VNASLFVDMN GLLHSKVKGV PETHVVVVEN EADKAGFLGA AVFYAQSLYR
PMLMVEKKLI TTANTGLSVS RTMFDLYVDS LLNVLDVDRK SLTSFVNAAH NSLKEGVQLE
QVMDTFIGCA RRKCAIDSDV ETKSITKSVM SAVNAGVDFT DESCNNLVPT YVKSDTIVAA
DLGVLIQNNA KHVQANVAKA ANVACIWSVD AFNQLSADLQ HRLRKACSKT GLKIKLTYNK
QEANVPILTT PFSLKGGAVF SRMLQWLFVA NLICFIVLWA LMPTYAVHKS DMQLPLYASF
KVIDNGVLRD VSVTDACFAN KFNQFDQWYE STFGLAYYRN SKACPVVVAV IDQDIGHTLF
NVPTTVLRYG FHVLHFITHA FATDSVQCYT PHMQIPYDNF YASGCVLSSL CTMLAHADGT
PHPYCYTGGV MHNASLYSSL APHVRYNLAS SNGYIRFPEV VSEGIVRVVR TRSMTYCRVG
LCEEAEEGIC FNFNRSWVLN NPYYRAMPGT FCGRNAFDLI HQVLGGLVRP IDFFALTASS
VAGAILAIIV VLAFYYLIKL KRAFGDYTSV VVINVIVWCI NFLMLFVFQV YPTLSCLYAC
FYFYTTLYFP SEISVVMHLQ WLVMYGAIMP LWFCIIYVAV VVSNHALWLF SYCRKIGTEV
RSDGTFEEMA LTTFMITKES YCKLKNSVSD VAFNRYLSLY NKYRYFSGKM DTAAYREAAC
SQLAKAMETF NHNNGNDVLY QPPTASVTTS FLQSGIVKMV SPTSKVEPCI VSVTYGNMTL
NGLWLDDKVY CPRHVICSSA DMTDPDYPNL LCRVTSSDFC VMSGRMSLTV MSYQMQGCQL
VLTVTLQNPN TPKYSFGVVK PGETFTVLAA YNGRPQGAFH VTLRSSHTIK GSFLCGSCGS
VGYVLTGDSV RFVYMHQLEL STGCHTGTDF SGNFYGPYRD AQVVQLPVQD YTQTVNVVAW
LYAAIFNRCN WFVQSDSCSL EEFNVWAMTN GFSSIKADLV LDALASMTGV TVEQVLAAIK
RLHSGFQGKQ ILGSCVLEDE TPSDVYQQLA GVKLQSKRTR VIKGTCCWIL ASTFLFCSII
SAFVKWTMFM YVTTHMLGVT LCALCFVSFA MLLIKHKHLY LTMYIMPVLC TFYTNYLVVY
KQSFRGLAYA WLSHFVPAVD YTYMDEVLYG VVLLVAMVFV TMRSINHDVF SIMFLVGRLV
SLVSMWYFGA NLEEEVLLFL TSLFGTYTWT TMLSLATAKV IAKWLAVNVL YFTDVPQIKL
VLLSYLCIGY VCCCYWGILS LLNSIFRMPL GVYNYKISVQ ELRYMNANGL RPPRNSFEAL
MLNFKLLGIG GVPVIEVSQI QSRLTDVKCA NVVLLNCLQH LHIASNSKLW QYCSTLHNEI
LATSDLSMAF DKLAQLLVVL FANPAAVDSK CLASIEEVSD DYVRDNTVLQ ALQSEFVNMA
SFVEYELAKK NLDEAKASGS ANQQQIKQLE KACNIAKSAY ERDRAVARKL ERMADLALTN
MYKEARINDK KSKVVSALQT MLFSMVRKLD NQALNSILDN AVKGCVPLNA IPSLTSNTLT
IIVPDKQVFD QVVDNVYVTY AGNVWHIQFI QDADGAVKQL NEIDVNSTWP LVIAANRHNE
VSTVVLQNNE LMPQKLRTQV VNSGSDMNCN TPTQCYYNTT GTGKIVYAIL SDCDGLKYTK
IVKEDGNCVV LELDPPCKFS VQDVKGLKIK YLYFVKGCNT LARGWVVGTL SSTVRLQAGT
ATEYASNSAI LSLCAFSVDP KKTYLDYIKQ GGVPVTNCVK MLCDHAGTGM AITIKPEATT
NQDSYGGASV CIYCRSRVEH PDVDGLCKLR GKFVQVPLGI KDPVSYVLTH DVCQVCGFWR
DGSCSCVGTG SQFQSKDTNF LNGFGVQV


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