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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_CVHN2               Reviewed;        4441 AA.
P0C6U4; Q14EB2;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
23-MAY-2018, entry version 61.
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 N2) (HCoV-HKU1).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=443240;
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=P0C6U4-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X3-1; 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 N2 belongs to genotype B.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; AY884001; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; P0C6U4; -.
SMR; P0C6U4; -.
PRIDE; P0C6U4; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006551; 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 4441 Replicase polyprotein 1a.
/FTId=PRO_0000338206.
CHAIN 1 222 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338207.
CHAIN 223 809 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338208.
CHAIN 810 2808 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338209.
CHAIN 2809 3304 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338210.
CHAIN 3305 3607 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338211.
CHAIN 3608 3894 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338212.
CHAIN 3895 3986 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338213.
CHAIN 3987 4180 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338214.
CHAIN 4181 4290 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338215.
CHAIN 4291 4427 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338216.
CHAIN 4428 4441 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338217.
TRANSMEM 2196 2216 Helical. {ECO:0000255}.
TRANSMEM 2257 2277 Helical. {ECO:0000255}.
TRANSMEM 2288 2308 Helical. {ECO:0000255}.
TRANSMEM 2371 2391 Helical. {ECO:0000255}.
TRANSMEM 2413 2433 Helical. {ECO:0000255}.
TRANSMEM 2814 2834 Helical. {ECO:0000255}.
TRANSMEM 3089 3109 Helical. {ECO:0000255}.
TRANSMEM 3121 3141 Helical. {ECO:0000255}.
TRANSMEM 3148 3168 Helical. {ECO:0000255}.
TRANSMEM 3173 3193 Helical. {ECO:0000255}.
TRANSMEM 3621 3641 Helical. {ECO:0000255}.
TRANSMEM 3646 3666 Helical. {ECO:0000255}.
TRANSMEM 3671 3691 Helical. {ECO:0000255}.
TRANSMEM 3714 3734 Helical. {ECO:0000255}.
TRANSMEM 3742 3762 Helical. {ECO:0000255}.
TRANSMEM 3770 3790 Helical. {ECO:0000255}.
TRANSMEM 3813 3833 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.
REPEAT 1035 1044 10.
REPEAT 1045 1054 11.
DOMAIN 1093 1343 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1321 1492 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1688 1948 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3305 3607 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1208 1236 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1805 1841 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4364 4380 {ECO:0000250}.
ZN_FING 4406 4419 {ECO:0000250}.
REGION 945 1054 11 X 10 AA tandem repeat of N-[DN]-D-E-D-
V-V-T-G-D.
REGION 2196 2433 HD1. {ECO:0000250}.
REGION 2814 3193 HD2. {ECO:0000250}.
REGION 3621 3833 HD3. {ECO:0000250}.
COMPBIAS 934 1086 Asp-rich.
COMPBIAS 2199 2291 Phe-rich.
COMPBIAS 2586 2589 Poly-Val.
ACT_SITE 1131 1131 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1282 1282 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1727 1727 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1884 1884 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3345 3345 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3449 3449 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 2808 2809 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3304 3305 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3607 3608 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3894 3895 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3986 3987 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4180 4181 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4290 4291 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4427 4428 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 4441 AA; 499423 MW; 9BED41AF10453162 CRC64;
MIKTSKYGLG FKWAPEFRWL LPDAAEELAS PMKSDEGGLC PSTGQAMESV GFVYDNHVKI
DCRCILGQEW HVQSNLIRDI FVHEDLHVVE VLTKTAVKSG TAILIKSPLH SLGGFPKGYV
MGLFRSYKTK RYVVHHLSMT TSTTNFGEDF LGWIVPFGFM PSYVHKWFQF CRLYIEESDL
IISNFKFDDY DFSVEDAYAE VHAEPKGKYS QKAYALLRQY RGIKPVLFVD QYGCDYSGKL
ADCLQAYGHY SLQDMRQKQS VWLANCDFDI VVAWHVVRDS RFVMRLQTIA TICGIKYVAQ
PTEDVVDGAV 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 WLLYQLLNGL FVVSQANFNF
VALIPDYAKI LVNKFYTFFK LLLECVTVDV LKDMPVLKTI NGLVCIVGNK FYNVSTGLIP
GFVLPCNAQE QQIYFFEGVA ESVIVEDDVI ENVKSSLSSY EYCQPPKSVE KICIIDNMYM
GKCGDKFFPI VMNDKNICLL DQAWRFPCAG RKVNFNEKPV VMEIPSLMTV KVMFDLDSTF
DDILGKVCSE FEVEKGVTVD DFVAVVCDAI ENALNSCKDH PVVGYQVRAF LNKLNENVVY
LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEEI VTGDNDDQIV VTGDDVDDIE
SVYDFDTYKA 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
IWLCHDEASL 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 ELCYSGFDML
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 TQTMFDVYVD
TFMSHFDVDR KSFNNFVNIA HASLREGVQL EKVLDTFVGC VRKCCSIDSD VETRFITKSM
ISAVAAGLEF TDENYNNLVP TYLKSDNIVA ADLGVLIQNG AKHVQGNVAK AANISCIWFI
DTFNQLTADL QHKLKKACVK TGLKLKLTFN KQEASVPILT TPFSLKGGVV LSNLLYILFF
ISLICFILLW ALLPTYSVYK SDIHLPAYAS FKVIDNGVVR DISVNDLCFA NKFFQFDQWY
ESTFGSFYYH NSMDCPIVVA VMDEDIGSTM FNVPTKVLRH GFHVLHFLTY AFASDSVQCY
TPHIQISYND FYASGCVLSS LCTMFKRGDG TPHPYCYSDG VMKNASLYTS LVPHTRYSLA
NSNGFIRFPD VISEGIVRIV RTRSMTYCRV GACEYAEEGI CFNFNSSWVL NNDYYRSMPG
TFCGRDLFDL FYQFFSSLIR PIDFFSLTAS SIFGAILAIV VVLVFYYLIK LKRAFGDYTS
VVVINVIVWC INFLMLFVFQ VYPICACVYA CFYFYVTLYF PSEISVIMHL QWIVMYGAIM
PFWFCVTYVA MVIANHVLWL FSYCRKIGVN VCNDSTFEET SLTTFMITKD SYCRLKNSVS
DVAYNRYLSL YNKYRYYSGK MDTAAYREAA CSQLAKAMET FNHNNGNDVL YQPPTASVST
SFLQSGIVKM VSPTSKIEPC IVSVTYGSMT LNGLWLDDKV YCPRHVICLS SNMNEPDYSA
LLCRVTLGDF TIMSGRMSLT VVSYQMQGCQ LVLTVSLQNP YTPKYTFGVV KPGETFTVLA
AYNGRPQGAF HVTMRSSYTI KGSFLCGSCG SVGYVLTGDS VKFVYMHQLE LSTGCHTGTD
FTGNFYGPYR DAQVVQLPVK DYVQTVNVIA WLYAAILNNC AWFVQNDVCS IEDFNVWAMT
NGFSQVKADL VLDALASMTG VSIETLLAAI KRLYMGFQGR QILGSCTFED ELAPSDVYQQ
LAGVKLQSKT KRFIKETIYW ILISTFLFSC IISAFVKWTI FMYINTHMIG VTLCVLCFVS
FMMLLVKHKH FYLTMYIIPV LCTLFYVNYL VVYKEGFRGL TYVWLSYFVP AVNFTYVYEV
FYGCILCVFA IFITMHSINH DIFSLMFLVG RIVTLISMWY FGSNLEEDVL LFITAFLGTY
TWTTILSLAI AKIVANWLSV NIFYFTDVPY IKLILLSYLF IGYILSCYWG FFSLLNSVFR
MPMGVYNYKI SVQELRYMNA NGLRPPRNSF EAILLNLKLL GIGGVPVIEV SQIQSKLTDV
KCANVVLLNC LQHLHVASNS RLWQYCSILH NEILSTSDLS VAFDKLAQLL IVLFANPAAV
DTKCLASIDE VSDDYVQDST VLQALQSEFV NMASFVEYEV AKKNLADAKN SGSVNQQQIK
QLEKACNIAK SVYERDKAVA RKLERMADLA LTNMYKEARI NDKKSKVVSA LQTMLFSMVR
KLDNQALNSI LDNAVKGCVP LNAIPALAAN TLTIIIPDKQ VFDKVVDNVY VAYAGSVWHI
QTVQDADGIN KQLTDISVDS NWPLVIIANR YNEVANAVMQ NNELMPHKLK IQVVNSGSDM
NCNIPTQCYY NNGSSGRIVY AVLSDVDGLK YTKIIKDDGN CVVLELDPPC KFSIQDVKGL
KIKYLYFIKG CNTLARGWVV GTLSSTIRLQ AGVATEYAAN SSILSLCAFS VDPKKTYLDY
IQQGGVPIIN CVKMLCDHAG TGMAITIKPE ATINQDSYGG ASVCIYCRAR VEHPDVDGLC
KLRGKFVQVP LGIKDPILYV LTHDVCQVCG FWRDGSCSCV GSGVAVQSKD LNFLNGFGVL
V


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