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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_CVHN5               Reviewed;        4421 AA.
P0C6U5; Q0ZME9;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
10-OCT-2018, entry version 69.
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;
Human coronavirus HKU1 (isolate N5) (HCoV-HKU1).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=443241;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16809319; DOI=10.1128/JVI.00509-06;
Woo P.C.Y., Lau S.K.P., Yip C.C.Y., Huang Y., Tsoi H.-W., Chan K.-H.,
Yuen K.-Y.;
"Comparative analysis of 22 coronavirus HKU1 genomes reveals a novel
genotype and evidence of natural recombination in coronavirus HKU1.";
J. Virol. 80:7136-7145(2006).
-!- 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=P0C6U5-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X4-1; 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}.
-!- MISCELLANEOUS: Isolate N5 belongs to genotype C. Genotype C
probably arose from recombination between genotypes A and B.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; DQ339101; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; P0C6U5; -.
SMR; P0C6U5; -.
PRIDE; P0C6U5; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000001985; 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: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: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; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF11963; DUF3477; 1.
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.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
3: Inferred from homology;
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 4421 Replicase polyprotein 1a.
/FTId=PRO_0000338218.
CHAIN 1 222 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338219.
CHAIN 223 809 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338220.
CHAIN 810 2788 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338221.
CHAIN 2789 3284 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338222.
CHAIN 3285 3587 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338223.
CHAIN 3588 3874 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338224.
CHAIN 3875 3966 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338225.
CHAIN 3967 4160 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338226.
CHAIN 4161 4270 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338227.
CHAIN 4271 4407 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338228.
CHAIN 4408 4421 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338229.
TRANSMEM 2176 2196 Helical. {ECO:0000255}.
TRANSMEM 2237 2257 Helical. {ECO:0000255}.
TRANSMEM 2268 2288 Helical. {ECO:0000255}.
TRANSMEM 2351 2371 Helical. {ECO:0000255}.
TRANSMEM 2393 2413 Helical. {ECO:0000255}.
TRANSMEM 2794 2814 Helical. {ECO:0000255}.
TRANSMEM 3069 3089 Helical. {ECO:0000255}.
TRANSMEM 3101 3121 Helical. {ECO:0000255}.
TRANSMEM 3128 3148 Helical. {ECO:0000255}.
TRANSMEM 3153 3173 Helical. {ECO:0000255}.
TRANSMEM 3601 3621 Helical. {ECO:0000255}.
TRANSMEM 3626 3646 Helical. {ECO:0000255}.
TRANSMEM 3651 3671 Helical. {ECO:0000255}.
TRANSMEM 3694 3714 Helical. {ECO:0000255}.
TRANSMEM 3722 3742 Helical. {ECO:0000255}.
TRANSMEM 3750 3770 Helical. {ECO:0000255}.
TRANSMEM 3793 3813 Helical. {ECO:0000255}.
REPEAT 945 954 1.
REPEAT 955 964 2.
REPEAT 965 974 3.
REPEAT 975 984 4.
REPEAT 985 994 5.
REPEAT 995 1004 6.
REPEAT 1005 1014 7.
REPEAT 1015 1024 8.
REPEAT 1025 1034 9.
DOMAIN 1073 1323 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1301 1472 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1668 1928 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3285 3587 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1188 1216 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1785 1821 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4344 4360 {ECO:0000250}.
ZN_FING 4386 4399 {ECO:0000250}.
REGION 945 1034 9 X 10 AA tandem repeat of N-[DN]-D-E-D-
V-V-T-G-D.
REGION 2176 2413 HD1. {ECO:0000250}.
REGION 2794 3173 HD2. {ECO:0000250}.
REGION 3601 3813 HD3. {ECO:0000250}.
COMPBIAS 934 1066 Asp-rich.
COMPBIAS 2179 2271 Phe-rich.
COMPBIAS 2566 2569 Poly-Val.
ACT_SITE 1111 1111 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1262 1262 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1707 1707 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1864 1864 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3325 3325 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3429 3429 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 222 223 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 809 810 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2788 2789 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3284 3285 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3587 3588 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3874 3875 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3966 3967 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4160 4161 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4270 4271 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4407 4408 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 4421 AA; 497400 MW; 19FFC89AAA1E43AB CRC64;
MIKTSKYGLG FKWAPEFRWL LPDAAEELAS PMKSDEGGLC PSTGQAMESV GFVYDNHVKI
DCRCILGQEW HVQSNLIRDI FVHEDLHVVE VLTKTAVKSG TAILIKSPLH SLGGFPKGYV
MGLFRSYKTK RYVVHHLSMT TSTTNFGEDF FGWIVPFGFM PSYVHKWFQF CRLYIEESDL
IISNFKFDDY DFSVEAAYAE VHAEPKGKYS QKAYALLRQY RGIKPVLFVD QYGCDYSGKL
ADCLQAYGHY SLQDMRQKQS VWLANCDFDI VVAWHVVRDS RFVMRLQTIA TICGIKYVAQ
PTEDVVDGDV VIREPVHLLS ADAIVLKLPS LMKVMTHMDD FSIKSIYNVD LCDCGFVMQY
GYVDCFNDNC DFYGWVSGNM MDGFSCPLCC TVYDSSEVKA QSSGVIPENP VLFTNSTDTV
NPDSFNLYGY SVTPFGSCIY WSPRPGLWIP IIKSSVKSYD DLVYSGVVGC KSIVKETALI
THALYLDYVQ CKCGNLEQNH ILGVNNSWCR QLLLNRGDYN MLLKNIDLFV KRRADFACKF
AVCGDGFVPF LLDGLIPRSY YLIQSGIFFT SLMSQFSQEV SDMCLKMCIL FMDRVSVATF
YIEHYVNRLV TQFKLLGTTL VNKMVNWFNT MLDASAPATG WLLYQLLNGF FVVSQANLNF
VALIPDYAKI LVNKFYTFFK LLLECVTVDV LKDMPVLKTI NGLVCIVGNK FYNVSTGLIP
GFVLPCNAQE QQIYFFEGVA ESVIVEDDVI ENVKSSLSSY EYCQPPKSVE KICIIDNMYM
GKCGDKFFPI VMNDKNICLL DHAWRFPCAG RKVNFNEKPV VMEIPSLMTV KVMFDLDSTF
DDILGKVCSE FEVEKGVTVD DFVAVVCDAI ENALNSCKEH PVVGYQVRAF LNKLNENVVY
LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
VTGDNNDEDV VTGDNNDEES VTGDNDDQIV VTGDDVDDIE SIYDFDTYKA LLVFNDVYND
ALFVSYGSSV ETETYFKVNG LWSPTITHTN CWLRSVLLVM QKLPFKFKDL AIENMWLSYK
VGYNQSFVDY LLTTIPKAIV LPQGGYVADF AYWFLNQFDI NAYANWCCLK CGFSFDLNGL
DAVFFYGDIV SHVCKCGHNM TLIAADLPCT LHFSLFDDNF CAFCTPKKIF IAACAVDVNV
CHSVAVIGDE QIDGKFVTKF SGDKFDFIVG YGMSFSMSSF ELAQLYGLCI TPNVCFVKGD
IINVARLVKA DVIVNPANGH MLHGGGVAKA IAVAAGKKFS KETAAMVKSK GVCQVGDCYV
STGGKLCKTI LNIVGPDARQ DGRQSYVLLA RAYKHLNNYD CCLSTLISAG IFSVPADVSL
TYLLGVVDKQ VILVSNNKED FDIIQKCQIT SVVGTKALAV RLTANVGRVI KFETDAYKLF
LSGDDCFVSN SSVIQEVLLL RHDIQLNNDV RDYLLSKMTS LPKDWRLINK FDVINGVKTV
KYFECPNSIY ICSQGKDFGY VCDGSFYKAT VNQVCVLLAK KIDVLLTVDG VNFKSISLTV
GEVFGKILGN VFCDGIDVTK LKCSDFYADK ILYQYENLSL ADISAVQSSF GFDQQQLLAY
YNFLTVCKWS VVVNGPFFSF EQSHNNCYVN VACLMLQHIN LKFNKWQWQE AWYEFRAGRP
HRLVALVLAK GHFKFDEPSD ATDFIRVVLK QADLSGAICE LELICDCGIK QESRVGVDAV
MHFGTLAKTD LFNGYKIGCN CAGRIVHCTK LNVPFLICSN TPLSKDLPDD VVAANMFMGV
GVGHYTHLKC GSPYQHYDAC SVKKYTGVSG CLTDCLYLKN LTQTFTSMLT NYFLDDVEMV
AYNPDLSQYY CDNGKYYTKP IIKAQFKPFA KVDGVYTNFK LVGHDICAQL NDKLGFNVDL
PFVEYKVTVW PVATGDVVLA SDDLYVKRYF KGCETFGKPV IWFCHDEASL NSLTYFNKPS
FKSENRYSVL SVDSVSEESQ GNVVTSVMES QISTKEVKLK GVRKTVKIED AIIVNDENSS
IKVVKSLSLV DVWDMYLTGC DYVVWVANEL SRLVKSPTVR EYIRYGIKPI TIPIDLLCLR
DDNQTLLVPK IFKARAIEFY GFLKWLFIYV FSLLHFTNDK TIFYTTEIAS KFTFNLFCLA
LKNAFQTFRW SIFIKGFLVV ATVFLFWFNF LYINVIFSDF YLPNISVFPI FVGRIVMWIK
ATFGLVTICD FYSKLGVGFT SHFCNGSFIC ELCHSGFDML DTYAAIDFVQ YEVDRRVLFD
YVSLVKLIVE LVIGYSLYTV WFYPLFCLIG LQLFTTWLPD LFMLETMHWL IRFIVFVANM
LPAFVLLRFY IVVTAMYKVV GFIRHIVYGC NKAGCLFCYK RNCSVRVKCS TIVGGVIRYY
DITANGGTGF CVKHQWNCFN CHSFKPGNTF ITVEAAIELS KELKRPVNPT DASHYVVTDI
KQVGCMMRLF YDRDGQRVYD DVDASLFVDI NNLLHSKVKV VPNLYVVVVE SDADRANFLN
AVVFYAQSLY RPILLVDKKL ITTACNGISV TQIMFDVYVD TFMSHFDVDR KSFNNFVNIA
HASLREGVQL EKVLDTFVGC VRKCCSIDSD VETRFITKSM ISAVAAGLEF TDENYNNLVP
TYLKSDNIVA ADLGVLIQNG AKHVQGNVAK VANISCIWFI DAFNQLTADL QHKLKKACVK
TGLKLKLTFN KQEASVPILT TPFSLKGGVV LSNLLYILFF ISLICFILLW ALLPTYSVYK
SDIHLPAYAS FKVIDNGVVR DISVNDLCFA NKFFQFDQWY ESTFGSVYYH NSMDCPIVVA
VMDEDIGSTM FNVPTKVLRY GFHVLHFLTY AFASDSVQCY TPHIQISYND FYASGCVLSS
LCTMFKRGDG TPHPYCYTDG VMKNASLYTS LVPHTRYSLA NSNGFIRFPD VISEGIVRIV
RTRSMTYCRV GACEYAEEGI CFNFNSSWVL NNDYYRSMPG TFCGRDFFDL FYQFFSSLIR
PIDFFSLTAS SIFGAILAIV VVLVFYYLIK LKRAFGDYTS VVVINVIVWC INFLMLFVFQ
VYPICACVYA CFYFYVTLYF PSEISVIMHL QWIVMYGAIM PFWFCVTYVA MVIANHVLWL
FSYCRKIGVN VCSDSTFEET SLTTFMITKD SYCRLKNSVS DVAYNRYLSL YNKYRYYSGK
MDTAAYREAA CSQLAKAMET FNHNNGNDVL YQPPTASVST SFLQSGIVKM VSPTSKIEPC
LVSVTYGSMT LNGLWLDDKV YCPRHVICLS SNMNEPDYSA LLCRVTLGDF TIMSGRMSLT
VVSYQMQGCQ LVLTVSLQNP YTPKYTFGVV KPGETFTVLA AYNGRPQGAF HVTMRSSYTI
KGSFLCGSCG SVGYVLTGDS VKFVYMHQLE LSTGCHTGTD FNGNFYGPYR DAQVVQLPVK
DYVQTVNVIA WLYAAILNNC AWFVQNDVCS IEDFNVWAMT NGFSQVKADL VLDALASMTG
VSIETLLAAI KRLYMGFQGR QILGSCTFED ELAPSDVYQQ LAGVKLQSKT KRFIKETIYW
ILISTFLFSC IISAFVKWTI FMYINTHMIG VTLCVLCFVS FMMLLVKHKH FYLTMYIIPV
LCTLFYVNYL VVYKEGFRGF TYVWLSHFVP AVNFTYVYEV FYGCILCVFA IFITMHSINH
DIFSLMFLVG RIVTLISMWY FGSNLEEDVL LFITAFLGTY TWTTILSLAI AKIVANWLSV
NIFYFTDVPY IKLILLSYLF IGYILSCYWG FFSLLNSVFR MPMGVYNYKI SVQELRYMNA
NGLRPPRNSF EAILLNLKLL GIGGVPVIEV SQIQSKLTDV KCANVVLLNC LQHLHVASNS
KLWQYCSVLH NEILSTSDLS VAFDKLAQLL IVLFSNPAAV DTKCLASIDE VSDDYVQDST
VLQALQSEFV NMASFVEYEV AKKNLADAKN SGSVNQQQIK QLEKACNIAK SVYERDKAVA
RKLERMADLA LTNMYKEARI NDKKSKVVSA LQTMLFSMVR KLDNQALNSI LDNAVKGCVP
LSAIPALAAN TLTIIIPDKQ VFDKVVDNVY VTYAGSVWHI QTVQDADGIN KQLTDISVDS
NWPLVIIANR YNEVANAVMQ NNELMPHKLK IQVVNSGSDI NCNIPTQCYY NNVSSGRIVY
AVLSDVDGLK YTKIMKDDGN CVVLELDPPC KFSIQDVKGL KIKYLYFIKG CNTLARGWVV
GTLSSTIRLQ AGVATEYAAN SSILSLCAFS VDPKKTYLDY IQQGGVPIIN CVKMLCDHAG
TGMAITIKPE ATINQDSYGG ASVCIYCRAR VEHPDVDGIC KLRGKFVQVP LGIKDPILYV
LTHDVCQVCG FWRDGSCSCV GSSVAVQSKD LNFLNGLGVL V


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