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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_CVMJH               Reviewed;        4474 AA.
P0C6V1; P19751;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
23-MAY-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 JHM) (MHV-JHM) (Murine hepatitis virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=11144;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1846489; DOI=10.1016/0042-6822(91)90071-I;
Lee H.-J., Shieh C.-K., Gorbalenya A.E., Koonin E.V., la Monica N.,
Tuler J., Bagdzhardzhyan A., Lai M.M.C.;
"The complete sequence (22 kilobases) of murine coronavirus gene 1
encoding the putative proteases and RNA polymerase.";
Virology 180:567-582(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-595.
PubMed=2824826;
Soe L.H., Shieh C.-K., Baker S.C., Chang M.F., Lai M.M.C.;
"Sequence and translation of the murine coronavirus 5'-end genomic RNA
reveals the N-terminal structure of the putative RNA polymerase.";
J. Virol. 61:3968-3976(1987).
[3]
SEQUENCE REVISION.
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1021-1326.
PubMed=1966414;
Baker S.C., La Monica N., Shieh C.K., Lai M.M.;
"Murine coronavirus gene 1 polyprotein contains an autoproteolytic
activity.";
Adv. Exp. Med. Biol. 276:283-289(1990).
[5]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF PHE-2835;
SER-2836; LEU-2837; LYS-2838; GLY-2839; GLY-2840; ALA-2841; VAL-2842
AND VAL-2846.
PubMed=12805436; DOI=10.1128/JVI.77.13.7376-7382.2003;
Kanjanahaluethai A., Jukneliene D., Baker S.C.;
"Identification of the murine coronavirus MP1 cleavage site recognized
by papain-like proteinase 2.";
J. Virol. 77:7376-7382(2003).
[6]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND SUBCELLULAR LOCATION.
PubMed=9514967; DOI=10.1006/viro.1997.9010;
Schiller J.J., Kanjanahaluethai A., Baker S.C.;
"Processing of the coronavirus MHV-JHM polymerase polyprotein:
identification of precursors and proteolytic products spanning 400
kilodaltons of ORF1a.";
Virology 242:288-302(1998).
[7]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=11842254;
Hegyi A., Ziebuhr J.;
"Conservation of substrate specificities among coronavirus main
proteases.";
J. Gen. Virol. 83:595-599(2002).
-!- 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 (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=P0C6V1-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6Y0-1; 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; M55148; AAA46457.1; -; Genomic_RNA.
EMBL; M18040; AAA46466.1; -; Genomic_RNA.
EMBL; S51684; AAB19566.1; -; Genomic_RNA.
PIR; A36815; RRIHM2.
PIR; B36815; VFIHJH.
RefSeq; YP_209230.1; AC_000192.1. [P0C6V1-1]
ProteinModelPortal; P0C6V1; -.
SMR; P0C6V1; -.
PRIDE; P0C6V1; -.
OrthoDB; VOG09000000; -.
BRENDA; 3.4.22.B14; 3467.
Proteomes; UP000007193; 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; IMP:CACAO.
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; IDA: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;
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; Repeat;
Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion;
Zinc; Zinc-finger.
CHAIN 1 4474 Replicase polyprotein 1a.
/FTId=PRO_0000338290.
CHAIN 1 247 Non-structural protein 1. {ECO:0000305}.
/FTId=PRO_0000338291.
CHAIN 248 832 Non-structural protein 2. {ECO:0000305}.
/FTId=PRO_0000338292.
CHAIN 833 2840 Non-structural protein 3. {ECO:0000305}.
/FTId=PRO_0000338293.
CHAIN 2841 3336 Non-structural protein 4. {ECO:0000305}.
/FTId=PRO_0000338294.
CHAIN 3337 3639 3C-like proteinase. {ECO:0000305}.
/FTId=PRO_0000338295.
CHAIN 3640 3927 Non-structural protein 6. {ECO:0000305}.
/FTId=PRO_0000338296.
CHAIN 3928 4019 Non-structural protein 7. {ECO:0000305}.
/FTId=PRO_0000338297.
CHAIN 4020 4213 Non-structural protein 8.
/FTId=PRO_0000338298.
CHAIN 4214 4323 Non-structural protein 9. {ECO:0000305}.
/FTId=PRO_0000338299.
CHAIN 4323 4474 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338301.
CHAIN 4324 4460 Non-structural protein 10. {ECO:0000305}.
/FTId=PRO_0000338300.
TRANSMEM 2289 2309 Helical. {ECO:0000255}.
TRANSMEM 2320 2340 Helical. {ECO:0000255}.
TRANSMEM 2403 2423 Helical. {ECO:0000255}.
TRANSMEM 2445 2465 Helical. {ECO:0000255}.
TRANSMEM 2846 2866 Helical. {ECO:0000255}.
TRANSMEM 3099 3119 Helical. {ECO:0000255}.
TRANSMEM 3121 3141 Helical. {ECO:0000255}.
TRANSMEM 3153 3173 Helical. {ECO:0000255}.
TRANSMEM 3180 3200 Helical. {ECO:0000255}.
TRANSMEM 3205 3225 Helical. {ECO:0000255}.
TRANSMEM 3648 3668 Helical. {ECO:0000255}.
TRANSMEM 3678 3698 Helical. {ECO:0000255}.
TRANSMEM 3705 3725 Helical. {ECO:0000255}.
TRANSMEM 3748 3768 Helical. {ECO:0000255}.
TRANSMEM 3775 3795 Helical. {ECO:0000255}.
TRANSMEM 3802 3822 Helical. {ECO:0000255}.
TRANSMEM 3846 3866 Helical. {ECO:0000255}.
DOMAIN 1083 1320 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1321 1481 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1677 1936 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3337 3639 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1197 1225 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1793 1829 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4397 4413 {ECO:0000250}.
ZN_FING 4439 4452 {ECO:0000250}.
REGION 2228 2465 HD1.
REGION 2846 3225 HD2.
REGION 3648 3866 HD3.
ACT_SITE 1120 1120 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1271 1271 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1715 1715 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1872 1872 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3377 3377 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3481 3481 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 247 248 Cleavage; by PL1-PRO. {ECO:0000305}.
SITE 832 833 Cleavage; by PL1-PRO. {ECO:0000305}.
SITE 2840 2841 Cleavage; by PL2-PRO. {ECO:0000305}.
SITE 3336 3337 Cleavage; by 3CL-PRO. {ECO:0000305}.
SITE 3639 3640 Cleavage; by 3CL-PRO. {ECO:0000305}.
SITE 3927 3928 Cleavage; by 3CL-PRO. {ECO:0000305}.
SITE 4019 4020 Cleavage; by 3CL-PRO. {ECO:0000305}.
SITE 4213 4214 Cleavage; by 3CL-PRO. {ECO:0000305}.
SITE 4323 4324 Cleavage; by 3CL-PRO. {ECO:0000305}.
SITE 4460 4461 Cleavage; by 3CL-PRO. {ECO:0000305}.
MUTAGEN 2835 2835 F->A: No processing between p210 and
peptide HD2.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2836 2836 S->A: No effect.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2837 2837 L->A: No effect.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2838 2838 K->A: No effect.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2838 2838 K->N: No effect.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2839 2839 G->A: Partial processing between p210 and
peptide HD2.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2839 2839 G->N: No processing between p210 and
peptide HD2.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2839 2839 G->V: No processing between p210 and
peptide HD2.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2840 2840 G->A: No processing between p210 and
peptide HD2.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2840 2840 G->N: No processing between p210 and
peptide HD2.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2840 2840 G->V: No processing between p210 and
peptide HD2.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2841 2841 A->N: No effect.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2842 2842 V->N,M: No effect.
{ECO:0000269|PubMed:12805436}.
MUTAGEN 2846 2846 V->M: No effect.
{ECO:0000269|PubMed:12805436}.
SEQUENCE 4474 AA; 497595 MW; 7F09A6BF0E052D83 CRC64;
MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK GKTLVNHVRV
DCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG SAVLVKPSKR LSVQAWAKLG
VLPKTPAMGL FKRFCLCNTR ECVCDAHVAF QLFTVQPDGV CLGNGRFIGW FVPVTAIPEY
AKQWLQPWSI LLRKGGNKGS VTSGHFRRAV TMPVYDFNVE DACEEVHLNP RGKYSCKAYA
LLRGYRGVKP ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELSPVWRDS LDNEVVVAWH
VDRDPRAVMR LQTLATVRSI EYVGQPIEDM VDGDVVMREP AHLLAPNAIV KRLPRLVETM
LYTDSSVTEF CYKTKLCDCG FITQFGYVDC CGDTCGFRGW VPGNMMDGFP CPGCCKSYMP
WELEAQSSGV IPEGGVLFTQ STDTVNRESF KLYGHAVVPF GGAAYWSPYP GMWLPVIWSS
VKSYSYLTYT GVVGCKAIVQ ETDAICRFLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN
RGDYSLLLEN VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSLMVN
FSREVVDMCM DMALLFMHDV KVATKYVKKV TGKVAVRFKA LGIAVVRKIT EWFDLAVDTA
ASAAGWLCYQ LVNGLFAVAN GVITFIQEVP ELVKNFVDKF KTFFKVLIDS MSVSILSGLT
VVKTASNRVC LAGSKVYEVV QKSLPAYIMP VGCSEATCLV GEIEPAVFED DVVDVVKAPL
TYQGCCKPPS SFEKICIVDK LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVVFND
KPKVKEVPST RKIKIIFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
KEHGVIGTKV CALLERLVDD YVYLFDEGGE EVIASRMYCS FSAPDEDCVA TDVVYADENQ
DDDADDPVVL VADTQEEDGV AREQVDSADS EICVAHTGGQ EMTEPDVVGS QTPIASAEET
EVGEACDREG IAEVKATVCA DALDACPDQV EAFDIEKVED SILSELQTEL NAPADKTYED
VLAFDAIYSE TLSAFYAVPS DETHFKVCGF YSPAIERTNC WLRSTLIVMQ SLPLEFKDLG
MQKLWLSYKA GYDQCFVDKL VKSAPKSIIL PQGGYVADFA YFFLSQCSFK VHANWRCLKC
GMELKLQGLD AVFFYGDVVS HMCKCGNSMT LLSADIPYTF DFGVRDDKFC AFYTPRKVFR
AACAVDVNDC HSMAVVDGKQ IDGKVVTKFN GDKFDFMVGH GMTFSMSPFE IAQLYGSCIT
PNVCFVKGDV IKVLRRVGAE VIVNPANGRM AHGAGVAGAI AKAAGKAFIN ETADMVKAQG
VCQVGGCYES TGGKLCKKVL NIVGPDARGH GNECYSLLER AYQHINKCDN VVTTLISAGI
FSVPTDVSLT YLLGVVTKNV ILVSNNQDDF DVIEKCQVTS VAGTKALSFQ LAKNLCRDVK
FVTNACSSLF SESSFVSSYD VLQEVEALRH DIQLDDDARV FVQANMDCLP TDWRLVNKFD
SVDGVRTIKY FECPGEVFVS SQGKKFGYVQ NGSFKEASVS QIRALLANKV DVLCTVDGVN
FRSCCVAEGE VFGKTLGSVF CDGINVTKVR CSAIHKGKVF FQYSGLSAAD LAAVKDAFGF
DEPQLLQYYS MLGMCKWPVV VCGNYFAFKQ SNNNCYINVA CLMLQHLSLK FPKWQWRRPG
NEFRSGKPLR FVSLVLAKGS FKFNEPSDST DFIRVELREA DLSGATCDLE FICKCGVKQE
QRKGVDAVMH FGTLDKSGLV KGYNIACTCG DKLVHCTQFN VPFLICSNTP EGKKLPDDVV
AANIFTGGSV GHYTHVKCKP KYQLYDACNV SKVSEAKGNF TDCLYLKNLK QTFSSVLTTY
YLDDVKCVAY KPDLSQYYCE SGKYYTKPII KAQFRTFEKV EGVYTNFKLV GHDIAEKLNA
KLGFDCNSPF MEYKITEWPT ATGDVVLASD DLYVSRYSGG CVTFGKPVIW RGHEEASLKS
LTYFNRPSVV CENKFNVLPV DVSEPTDRRP VPSAVLVTGA ASGADASAIS TEPGTAKEQK
ACASDSVEDQ IVMEAQKKSS VTTVAVKEVK LNGVKKPVKW NCSVVVNDPT SETKVVKSLS
IVDVYDMFLT GCRYVVWTAN ELSRLINSPT VREYVKWGMS KLIIPANLLL LRDEKQEFVA
PKVVKAKAIA CYGAVKWFLL YCFSWIKFNT DNKVIYTTEV ASKLTFKLCC LAFKNALQTF
NWSVVSRGFF LVATVFLLWF NFLYANVILS DFYLPNIGPL PMFVGQIVAW VKTTFGVLTI
CDFYQVTDLG YRSSFCNGSM VCELCFSGFD MLDNYESINV VQHVVDRRVS FDYISLFKLV
VELVIGYSLY TVCFYPLFVL VGMQLLTTWL PEFFMLGTMH WSARLFVFVA NMLPAFTLLR
FYIVVTAMYK VYCLCRHVMY GCSKPGCLFC YKRNRSVRVK CSTVVGGSLR YYDVMANGGT
GFCTKHQWNC LNCNSWKPGN TFITHEAAAD LSKELKRPVN PTDSAYYSVI EVKQVGCSMR
LFYERDGQRV YDDVSASLFV DMNGLLHSKV KGVPETHVVV VENEADKAGF LNAAVFYAQS
LYRPMLMVEK KLITTANTGL SVSRTMFDLY VYSLLRHLDV DRKSLTSFVN AAHNSLKEGV
QLEQVMDTFV GCARRKCAID SDVETKSITK SVMAAVNAGV EVTDESCNNL VPTYVKSDTI
VAADLGVLIQ NNAKHVQSNV AKAANVACIW SVDAFNQLSA DLQHRLRKAC VKTGLKIKLT
YNKQEANVPI LTTPFSLKGG AVFSRVLQWL FVANLICFIV LWALMPTYAV HKSDMQLPLY
ASFKVIDNGV LRDVSVTDAC FANKFNQFDQ WYESTFGLVY YRNSKACPVV VAVIDQDIGH
TLFNVPTKVL RYGFHVLHFI THAFATDRVQ CYTPHMQIPY DNFYASGCVL SSLCTMLAHA
DGTPHPYCYT EGVMHNASLY SSLVPHVRYN LASSNGYIRF PEVVSEGIVR VVRTRSMTYC
RVGLCEEAEE GICFNFNSSW VLNNPYYRAM PGTFCGRNAF DLIHQVLGGL VQPIDFFALT
ASSVAGAILA IIVVLAFYYL IKLKRAFGDY TSVVVINVIV WCINFLMLFV FQVYPTLSCL
YACFYFYTTL YFPSEISVVM HLQWLVMYGA IMPLWFCITY VAVVVSNHAL WLFSYCRKIG
TDVRSDGTFE EMALTTFMIT KESYCKLKNS VSDVAFNRYL SLYNKYRYFS GKMDTATYRE
AACSQLAKAM ETFNHNNGND VLYQPPTASV TTSFLQSGIV KMVSPTSKVE PCVVSVTYGN
MTLNGLWLDD KVYCPRHVIC SSADMTDPDY PNLLCRVTSS DFCVMSDRMS LTVMSYQMQG
SLLVLTVTLQ NPNTPKYSFG VVKPGETFTV LAAYNGRPQG AFHVVMRSSH TIKGSFLCGS
CGSVGYVLTG DSVRFVYMHQ LELSTGCHTG TDFSGNFYGP YRDAQVVQLP VQDYTQTVNV
VAWLYAAILN RCNWFVQSDS CSLEEFNVWA MTNGFSSIKA DLVLDALASM TGVTVEQVLA
AIKRLHSGFQ GKQILGSCVL EDELTPSDVY QQLAGVKLQS KRTRVIKGTC CWILASTFLF
CSIISAFVKW TMFMYVTTHM LGVTLCALCF VIFAMLLIKH KHLYLTMYIM PVLCTLFYTN
YLVVGYKQSF RGLAYAWLSY FVPAVDYTYM DEVLYGVVLL VAMVFVTMRS INHDVFSTMF
LVGRLVSLVS MWYFGANLEE EVLLFLTSLF GTYTWTTMLS LATAKVIAKW LAVNVLYFTD
IPQIKLVLLS YLCIGYVCCC YWGVLSLLNS IFRMPLGVYN YKISVQELRY MNANGLRPPR
NSFEALMLNF KLLGIGGVPV IEVSQIQSRL TDVKCANVVL LNCLQHLHIA SNSKLWQYCS
TLHNEILATS DLSVAFDKLA QLLVVLFANP AAVDSKCLAS IEEVSDDYVR DNTVLQALQS
EFVNMASFVE YELAKKNLDE AKASGSANQQ QIKQLEKACN IAKSAYERDR AVARKLERMA
DLALTNMYKE ARINDKKSKV VSALQTMLFS MVRKLDNQAL NSILDNAVKG CVPLNAIPPL
TSNTLTIIVP DKQVFDQVVD NVYVTYAPNV WHIQSIQDAD GAVKQLNEID VNSTWPLVIS
ANRHNEVSTV VLQNNELMPQ KLRTQVVNSG SDMNCNIPTQ CYYNTTGTGK IVYAILSDCD
GLKYTKIVKE DGNCVVLELD PPCKFSVQDV KGLKIKYLYF VKGCNTLARG WVVGTLSSTV
RLQAGTATEY ASNSAILSLC AFSVDPKKTY LDYIQQGGVP VTNCVKMLCD HAGTGMAITI
KPEATTNQDS YGGASVCIYC RSRVEHPDVD GLCKLRGKFV QVPLGIKDPV SYVLTHDVCQ
VCGFWRDGSC SCVGTGSQFQ SKDTNFLNGF GVQV


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