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 R1AB_PEDV7              Reviewed;        6781 AA.
P0C6Y4; Q91AV2;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 68.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=p9;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p87;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.-;
AltName: Full=PL1-PRO/PL2-PRO;
AltName: Full=PLP1/PLP2;
AltName: Full=Papain-like proteinases 1/2;
AltName: Full=p195;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p34;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p5;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p23;
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=p14;
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=p66;
AltName: Full=p66-HEL;
Contains:
RecName: Full=Exoribonuclease;
Short=ExoN;
EC=3.1.13.-;
AltName: Full=nsp14;
Contains:
RecName: Full=Uridylate-specific endoribonuclease;
EC=3.1.-.-;
AltName: Full=NendoU;
AltName: Full=nsp15;
Contains:
RecName: Full=Putative 2'-O-methyl transferase;
EC=2.1.1.-;
AltName: Full=nsp16;
Name=rep; ORFNames=1a-1b;
Porcine epidemic diarrhea virus (strain CV777) (PEDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=229032;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=9782358;
Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.;
"Further analysis of the genome of porcine epidemic diarrhea virus.";
Adv. Exp. Med. Biol. 440:781-786(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11724265; DOI=10.1023/A:1011831902219;
Kocherhans R., Bridgen A., Ackermann M., Tobler K.;
"Completion of the porcine epidemic diarrhoea coronavirus (PEDV)
genome sequence.";
Virus Genes 23:137-144(2001).
-!- 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 1 (PLP1) and papain-like
proteinase 2 (PLP2) 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. PLP2 also antagonizes innate immune induction
of type I interferon by blocking the 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: The helicase which contains a zinc finger structure
displays RNA and DNA duplex-unwinding activities with 5' to 3'
polarity. 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: 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).
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1).
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- 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}.
-!- 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=P0C6Y4-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6V6-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. 3CL-PRO and PL-PRO proteinases are
autocatalytically processed (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK38661.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF353511; AAK38661.1; ALT_SEQ; Genomic_RNA.
RefSeq; NP_598309.2; NC_003436.1.
PDB; 5HIY; X-ray; 3.00 A; A/B/C=3858-3965.
PDB; 5HIZ; X-ray; 2.90 A; A/B=3858-3965.
PDBsum; 5HIY; -.
PDBsum; 5HIZ; -.
ProteinModelPortal; P0C6Y4; -.
SMR; P0C6Y4; -.
GeneID; 935181; -.
KEGG; vg:935181; -.
OrthoDB; VOG09000000; -.
BRENDA; 3.4.22.B14; 8727.
Proteomes; UP000008159; 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:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR009461; Coronavirus_NSP16.
InterPro; IPR027352; CV_ZBD.
InterPro; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; 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; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
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; PF08715; Viral_protease; 2.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF142877; SSF142877; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF51126; SSF51126; 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; 2.
PROSITE; PS51657; PSRV_HELICASE; 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;
Inhibition of host innate immune response by virus;
Inhibition of host IRF3 by virus;
Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
Methyltransferase;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway;
Viral immunoevasion; Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 110 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000037369.
CHAIN 111 895 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000037370.
CHAIN 896 2516 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000037371.
CHAIN 2517 2997 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000037372.
CHAIN 2998 3299 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000037373.
CHAIN 3300 3579 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000037374.
CHAIN 3580 3662 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000037375.
CHAIN 3663 3857 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000037376.
CHAIN 3858 3965 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000037377.
CHAIN 3966 4100 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000037378.
CHAIN 4101 5027 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000037379.
CHAIN 5028 5546 Helicase.
/FTId=PRO_0000037380.
CHAIN 5547 6141 Exoribonuclease. {ECO:0000250}.
/FTId=PRO_0000037381.
CHAIN 6142 6480 Uridylate-specific endoribonuclease.
{ECO:0000250}.
/FTId=PRO_0000037382.
CHAIN 6481 6781 Putative 2'-O-methyl transferase.
{ECO:0000250}.
/FTId=PRO_0000037383.
TRANSMEM 1959 1979 Helical. {ECO:0000255}.
TRANSMEM 2022 2042 Helical. {ECO:0000255}.
TRANSMEM 2105 2125 Helical. {ECO:0000255}.
TRANSMEM 2127 2147 Helical. {ECO:0000255}.
TRANSMEM 2150 2170 Helical. {ECO:0000255}.
TRANSMEM 2528 2548 Helical. {ECO:0000255}.
TRANSMEM 2619 2639 Helical. {ECO:0000255}.
TRANSMEM 2654 2674 Helical. {ECO:0000255}.
TRANSMEM 2754 2774 Helical. {ECO:0000255}.
TRANSMEM 2787 2807 Helical. {ECO:0000255}.
TRANSMEM 2814 2834 Helical. {ECO:0000255}.
TRANSMEM 2863 2883 Helical. {ECO:0000255}.
TRANSMEM 3336 3356 Helical. {ECO:0000255}.
TRANSMEM 3361 3381 Helical. {ECO:0000255}.
TRANSMEM 3399 3419 Helical. {ECO:0000255}.
TRANSMEM 3431 3451 Helical. {ECO:0000255}.
TRANSMEM 3454 3474 Helical. {ECO:0000255}.
TRANSMEM 3476 3496 Helical. {ECO:0000255}.
TRANSMEM 3500 3520 Helical. {ECO:0000255}.
DOMAIN 1057 1296 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1297 1465 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1691 1951 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2998 3299 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 4707 4869 RdRp catalytic.
DOMAIN 5028 5111 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5275 5466 (+)RNA virus helicase ATP-binding.
DOMAIN 5467 5636 (+)RNA virus helicase C-terminal.
ZN_FING 1162 1193 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4039 4055 {ECO:0000250}.
ZN_FING 4081 4094 {ECO:0000250}.
NP_BIND 5310 5317 ATP. {ECO:0000250}.
REGION 1959 2170 HD1.
REGION 2528 2883 HD2.
REGION 3336 3520 HD3.
COMPBIAS 1816 1932 Val-rich.
ACT_SITE 1091 1091 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1239 1239 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1729 1729 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1888 1888 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3038 3038 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3141 3141 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 5032 5032 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5035 5035 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5043 5043 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5046 5046 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5053 5053 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5056 5056 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5060 5060 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5066 5066 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5077 5077 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5082 5082 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5099 5099 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5102 5102 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 110 111 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 895 896 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2516 2517 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 2997 2998 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3299 3300 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3579 3580 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3662 3663 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3857 3858 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3965 3966 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4100 4101 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5027 5028 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5546 5547 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6141 6142 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6480 6481 Cleavage; by 3CL-PRO. {ECO:0000250}.
STRAND 3867 3874 {ECO:0000244|PDB:5HIZ}.
STRAND 3879 3888 {ECO:0000244|PDB:5HIZ}.
STRAND 3893 3903 {ECO:0000244|PDB:5HIZ}.
STRAND 3907 3910 {ECO:0000244|PDB:5HIZ}.
STRAND 3917 3921 {ECO:0000244|PDB:5HIZ}.
STRAND 3925 3930 {ECO:0000244|PDB:5HIZ}.
STRAND 3932 3943 {ECO:0000244|PDB:5HIZ}.
HELIX 3948 3958 {ECO:0000244|PDB:5HIZ}.
SEQUENCE 6781 AA; 753158 MW; C5E29CBA752AD5BB CRC64;
MASNHVTLAF ANDAEISAFG FCTASEAVSY YSEAAASGFM QCRFVSLDLA DTVEGLLPED
YVMVVIGTTK LSAYVDTFGS RPRNICGWLL FSNCNYFLEE LELTFGRRGG NIVPVDQYMC
GADGKPVLQE SEWEYTDFFA DSEDGQLNIA GITYVKAWIV ERSDVSYASQ NLTSIKSITY
CSTYEHTFLD GTAMKVARTP KIKKNVVLSE PLATIYREIG SPFVDNGSDA RSIIRRPVFL
HAFVKCKCGS YHWTVGDWTS YVSTCCGFKC KPVLVASCSA MPGSVVVTRA GAGTGVKYYN
NMFLRHVADI DGLAFWRILK VQSKDDLACS GKFLEHHEEG FTDPCYFLND SSLATKLKFD
ILSGKFSDEV KQAIIAGHVV VGSALVDIVD DALGQPWFIR KLGDLASAPW EQLKAVVRGL
GLLSDEVVLF GKRLSCATLS IVNGVFEFLA DVPEKLAAAV TVFVNFLNEF FESACDCLKV
GGKTFNKVGS YVLFDNALVK LVKAKARGPR QAGICEVRYT SLVVGSTTKV VSKRVENANV
NLVVVDEDVT LNTTGRTVVV DGLAFFESDG FYRHLADADV VIEHPVYKSA CELKPVFECD
PIPDFPLPVA ASVAELCVQT DLLLKNYNTP YKTYSCVVRG DKCCITCTLQ FKAPSYVEDA
VNFVDLCTKN IGTAGFHEFY ITAHEQQDLQ GFLTTCCTMS GFECFMPTIP QCPAVLEEID
GGSIWRSFIT GLNTMWDFCK RLKVSFGLDG IVVTVARKFK RLGALLAEMY NTYLSTVVEN
LVLAGVSFKY YATSVPKIVL GGCFHSVKSV FASVFQIPVQ AGIEKFKVFL NCVHPVVPRV
IETSFVELEE TTFKPPALNG GIAIVDGFAF YYDGTLYYPT DGNSVVPICF KKKGGGDVKF
SDEVSVKTID PVYKVSLEFE FESETIMAVL NKAVGNRIKV TGGWDDVVEY INVAIEVLKD
HVEVPKYYIY DEEGGTDPNL PVMVSQWPLN DDTISQDLLD VEVVTDAPID SEGDEVDSSA
PEKVADVANS EPGDDGLPVA PETNVESEVE EVAATLSFIK DTPSTVTKDP FAFDFVSYGG
LKVLRQSHNN CWVTSTLVQL QLLGIVDDPA MELFSAGRVG PMVRKCYESQ KAILGSLGDV
SACLESLTKD LHTLKITCSV VCGCGTGERI YEGCAFRMTP TLEPFPYGAC AQCAQVLMHT
FKSIVGTGIF CRDTTALSLD SLVVKPLCAA AFIGKDSGHY VTNFYDAAMA IDGYGRHQIK
YDTLNTICVK DVNWTAPLVP AVDSVVEPVV KPFYSYKNVD FYQGDFSDLV KLPCDFVVNA
ANEKLSHGGG IAKAIDVYTK GMLQKCSNDY IKAHGPIKVG RGVMLEALGL KVFNVVGPRK
GKHAPELLVK AYKSVFANSG VALTPLISVG IFSVPLEESL SAFLACVGDR HCKCFCYGDK
EREAIIKYMD GLVDAIFKEA LVDTTPVQED VQQVSQKPVL PNFEPFRIEG AHAFYECNPE
GLMSLGADKL VLFTNSNLDF CSVGKCLNDV TSGALLEAIN VFKKSNKTVP AGNCVTLDCA
NMISITMVVL PFDGDANYDK NYARAVVKVS KLKGKLVLAV DDATLYSKLS HLSVLGFVST
PDDVERFYAN KSVVIKVTED TRSVKAVKVE STATYGQQIG PCLVNDTVVT DNKPVVADVV
AKVVPNANWD SHYGFDKAGE FHMLDHTGFT FPSEVVNGRR VIKTTDNNCW VNVTCLQLQF
ARFRFKSAGL QAMWESYCTG DVAMFVHWLY WLTGVDKGQP SDSENALNML SKYIVPAGSV
TIERVTHDGC CCSKRVVTAP VVNASVLKLG VEDGLCPHGL NYIGKVVVVK GTTIVVNVGK
PVVAPSHLFL KGVSYTTFLD NGNGVVGHYT VFDHGTGMVH DGDAFVPGDL NVSPVTNVVV
SEQTAVVIKD PVKKAELDAT KLLDTMNYAS ERFFSFGDFM SRNLITVFLY ILSILGLCFR
AFRKRDVKVL AGVPQRTGII LRKSMRYNAK ALGVFFKLKL YWFKVLGKFS LGIYALYALL
FMTIRFTPIG SPVCDDVVAG YANSSFDKNE YCNSVICKVC LYGYQELSDF SHTQVVWQHL
RDPLIGNVMP FFYLAFLAIF GGVYVKAITL YFIFQYLNSL GVFLGLQQSI WFLQLVPFDV
FGDEIVVFFI VTRVLMFIKH VCLGCDKASC VACSKSARLK RVPVQTIFQG TSKSFYVHAN
GGSKFCKKHN FFCLNCDSYG PGCTFINDVI ATEVGNVVKL NVQPTGPATI LIDKVEFSNG
FYYLYSGDTF WKYNFDITDS KYTCKEALKN CSIITDFIVF NNNGSNVNQV KNACVYFSQM
LCKPVKLVDS ALLASLSVDF GASLHSAFVS VLSNSFGKDL SSCNDMQDCK STLGFDDVPL
DTFNAAVAEA HRYDVLLTDM SFNNFTTSYA KPEEKFPVHD IATCMRVGAK IVNHNVLVKD
SIPVVWLVRD FIALSEETRK YIIRTTKVKG ITFMLTFNDC RMHTTIPTVC IANKKGAGLP
SFSKVKKFFW FLCLFIVAAF FALSFLDFST QVSSDSDYDF KYIESGQLKT FDNPLSCVHN
VFINFDQWHD AKFGFTPVNN PSCPIVVGVS DEARTVPGIP AGVYLAGKTL VFAINTIFGT
SGLCFDASGV ADKGACIFNS ACTTLSGLGG TAVYCYKNGL VEGAKLYSEL APHSYYKMVD
GNAVSLPEII SRGFGIRTIR TKAMTYCRVG QCVQSAEGVC FGADRFFVYN AESGSDFVCG
TGLFTLLMNV ISVFSKTVPV TVLSGQILFN CIIAFVAVAV CFLFTKFKRM FGDMSVGVFT
VGACTLLNNV SYIVTQNTLG MLGYATLYFL CTKGVRYMWI WHLGFLISYI LIAPWWVLMV
YAFSAIFEFM PNLFKLKVST QLFEGDKFVG SFENAAAGTF VLDMHAYERL ANSISTEKLR
QYASTYNKYK YYSGSASEAD YRLACFAHLA KAMMDYASNH NDTLYTPPTV SYNSTLQAGL
RKMAQPSGVV EKCIVRVCYG NMALNGLWLG DIVMCPRHVI ASSTTSTIDY DYALSVLRLH
NFSISSGNVF LGVVSATMRG ALLQIKVNQN NVHTPKYTYR TVRPGESFNI LACYDGAAAG
VYGVNMRSNY TIRGSFINGA CGSPGYNINN GTVEFCYLHQ LELGSGCHVG SDLDGVMYGG
YEDQPTLQVE GASSLFTENV LAFLYAALIN GSTWWLSSSR IAVDRFNEWA VHNGMTTVGN
TDCFSILAAK TGVDVQRLLA SIQSLHKNFG GKQILGHTSL TDEFTTGEVV RQMYGVNLQG
GYVSRACRNV LLVGSFLTFF WSELVSYTKF FWVNPGYVTP MFACLSLLSS LLMFTLKHKT
LFFQVFLIPA LIVTSCINLA FDVEVYNYLA EHFDYHVSLM GFNAQGLVNI FVCFVVTILH
GTYTWRFFNT PASSVTYVVA LLTAAYNYFY ASDILSCAMT LFASVTGNWF VGAVCYKVAV
YMALRFPTFV AIFGDIKSVM FCYLVLGYFT CCFYGILYWF NRFFKVSVGV YDYTVSAAEF
KYMVANGLRA PTGTLDSLLL SAKLIGIGGE RNIKISSVQS KLTDIKCSNV VLLGCLSSMN
VSANSTEWAY CVDLHNKINL CNDPEKAQEM LLALLAFFLS KNSAFGLDDL LESYFNDNSM
LQSVASTYVG LPSYVIYENA RQQYEDAVNN GSPPQLVKQL RHAMNVAKSE FDREASTQRK
LDRMAEQAAA QMYKEARAVN RKSKVVSAMH SLLFGMLRRL DMSSVDTILN LAKDGVVPLS
VIPAVSATKL NIVTSDIDSY NRIQREGCVH YAGTIWNIID IKDNDGKVVH VKEVTAQNAE
SLSWPLVLGC ERIVKLQNNE IIPGKLKQRS IKAEGDGIVG EGKALYNNEG GRTFMYAFIS
DKPDLRVVKW EFDGGCNTIE LEPPRKFLVD SPNGAQIKYL YFVRNLNTLR RGAVLGYIGA
TVRLQAGKQT EQAINSSLLT LCAFAVDPAK TYIDAVKSGH KPVGNCVKML ANGSGNGQAV
TNGVEASTNQ DSYGGASVCL YCRAHVEHPS MDGFCRLKGK YVQVPLGTVD PIRFVLENDV
CKVCGCWLSN GCTCDRSIMQ STDMAYLNRV RGSSAARLEP CNGTDTQHVY RAFDIYNKDV
ACLGKFLKVN CVRLKNLDKH DAFYVVKRCT KSAMEHEQSI YSRLEKCGAI AEHDFFTWKD
GRAIYGNVCR KDLTEYTMMD LCYALRNFDE NNCDVLKSIL IKVGACEESY FNNKVWFDPV
ENEDIHRVYA LLGTIVARAM LKCVKFCDAM VEQGIVGVVT LDNQDLNGDF YDFGDFTCSI
KGMGVPICTS YYSYMMPVMG MTNCLASECF VKSDIFGEDF KSYDLLEYDF TEHKTALFNK
YFKYWGLQYH PNCVDCSDEQ CIVHCANFNT LFSTTIPITA FGPLCRKCWI DGVPLVTTAG
YHFKQLGIVW NNDLNLHSSR LSINELLQFC SDPALLIASS PALVDQRTVC FSVAALGTGM
TNQTVKPGHF NKEFYDFLLE QGFFSEGSEL TLKHFFFAQK VDAAVKDFDY YRYNRPTVLD
ICQARVVYQI VQRYFDIYEG GCITAKEVVV TNLNKSAGYP LNKFGKAGLY YESLSYEEQD
ELYAYTKRNI LPTMTQLNLK YAISGKERAR TVGGVSLLST MTTRQYHQKH LKSIVNTRGA
SVVIGTTKFY GGWDNMLKNL IDGVENPCLM GWDYPKCDRA LPNMIRMISA MILGSKHTTC
CSSTDRFFRL CNELAQVLTE VVYSNGGFYL KPGGTTSGDA TTAYANSVFN IFQAVSANVN
KLLSVDSNVC HNLEVKQLQR KLYECCYRST IVDDQFVVEY YGYLRKHFSM MILSDDGVVC
YNNDYASLGY VADLNAFKAV LYYQNNVFMS ASKCWIEPDI NKGPHEFCSQ HTMQIVDKEG
TYYLPYPDPS RILSAGVFVD DVVKTDAVVL LERYVSLAID AYPLSKHENP EYKKVFYVLL
DWVKHLYKTL NAGVLESFSV TLLEDSTAKF WDESFYANMY EKSAVLQSAG LCVVCGSQTV
LRCGDCLRRP MLCTKCAYDH VIGTTHKFIL AITPYVCCAS DCGVNDVTKL YLGGLSYWCH
EHKPRLAFPL CSAGNVFGLY KNSATGSPDV EDFNRIATSD WTDVSDYRLA NDVKDSLRLF
AAETIKAKEE SVKSSYACAT LHEVVGPKEL LLKWEVGRPK PPLNRNSVFT CYHITKNTKF
QIGEFVFEKA EYDNDAVTYK TTATTKLVPG MVFVLTSHNV QPLRAPTIAN QERYSTIHKL
HPAFNIPEAY SSLVPYYQLI GKQKITTIQG PPGSGKSHCV IGLGLYYPGA RIVFTACSHA
AVDSLCVKAS TAYSNDKCSR IIPQRARVEC YDGFKSNNTS AQYLFSTVNA LPECNADIVV
VDEVSMCTNY DLSVINQRIS YRHVVYVGDP QQLPAPRVMI SRGTLEPKDY NVVTQRMCAL
KPDVFLHKCY RCPAEIVRTV SEMVYENQFI PVHPDSKQCF KIFCKGNVQV DNGSSINRRQ
LDVVRMFLAK NPRWSKAVFI SPYNSQNYVA SRLLGLQIQT VDSSQGSEYD YVIYAQTSDT
AHASNVNRFN VAITRAKKGI LCIMCDRSLF DLLKFFELKL SDLQANEGCG LFKDCSRGDD
LLPPSHANTF MSLADNFKTD QYLAVQIGVN GPIKYEHVIS FMGFRFDINI PNHHTLFCTR
DFAMRNVRGW LGFDVEGAHV VGSNVGTNVP LQLGFSNGVD FVVRPEGCVV TESGDYIKPV
RARAPPGEQF AHLLPLLKRG QPWDVVRKRI VQMCSDYLAN LSDILIFVLW AGGLELTTMR
YFVKIGPSKS CDCGKVATCY NSALHTYCCF KHALGCDYLY NPYCIDIQQW GYKGSLSLNH
HEHCNVHRNE HVASGDAIMT RCLAIHDCFV KNVDWSITYP FIGNEAVINK SGRIVQSHTM
RSVLKLYNPK AIYDIGNPKG IRCAVTDAKW FCFDKNPTNS NVKTLEYDYI THGQFDGLCL
FWNCNVDMYP EFSVVCRFDT RCRSPLNLEG CNGGSLYVNN HAFHTPAFDK RAFAKLKPMP
FFFYDDTECD KLQDSINYVP LRASNCITKC NVGGAVCSKH CAMYHSYVNA YNTFTSAGFT
IWVPTSFDTY NLWQTFSNNL QGLENIAFNV LKKGSFVGDE GELPVAVVND KVLVRDGTVD
TLVFTNKTSL PTNVAFELYA KRKVGLTPPI TILRNLGVVC TSKCVIWDYE AERPLTTFTK
DVCKYTDFEG DVCTLFDNSI VGSLERFSMT QNAVLMSLTA VKKLTGIKLT YGYLNGVPVN
THEDKPFTWY IYTRKNGKFE DYPDGYFTQG RTTADFSPRS DMEKDFLSMD MGLFINKYGL
EDYGFEHVVY GDVSKTTLGG LHLLISQVRL ACMGVLKIDE FVSSNDSTLK SCTVTYADNP
SSKMVCTYMD LLLDDFVSIL KSLDLSVVSK VHEVMVDCKM WRWMLWCKDH KLQTFYPQLQ
ASEWKCGYSM PSIYKIQRMC LEPCNLYNYG AGVKLPDGIM FNVVKYTQLC QYLNSTTMCV
PHHMRVLHLG AGSDKGVAPG TAVLRRWLPL DAIIVDNDSV DYVSDADYSV TGDCSTLYLS
DKFDLVISDM YDGKIKSCDG ENVSKEGFFP YINGVITEKL ALGGTVAIKV TEFSWNKKLY
ELIQKFEYWT MFCTSVNTSS SEAFLIGVHY LGDFASGAVI DGNTMHANYI FWRNSTIMTM
SYNSVLDLSK FNCKHKATVV VNLKDSSISD VVLGLLKNGK LLVRNNDAIC GFSNHLVNVN
K


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