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 R1A_CVHN1               Reviewed;        4471 AA.
P0C6U3; Q5MQD2;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
28-MAR-2018, entry version 66.
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 N1) (HCoV-HKU1).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=443239;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15613317; DOI=10.1128/JVI.79.2.884-895.2005;
Woo P.C.Y., Lau S.K.P., Chu C.-M., Chan K.-H., Tsoi H.-W., Huang Y.,
Wong B.H.L., Poon R.W.S., Cai J.J., Luk W.-K., Poon L.L.M.,
Wong S.S.Y., Guan Y., Peiris J.S.M., Yuen K.-Y.;
"Characterization and complete genome sequence of a novel coronavirus,
coronavirus HKU1, from patients with pneumonia.";
J. Virol. 79:884-895(2005).
-!- 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=P0C6U3-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X2-1; 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 N1 belongs to genotype A.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; AY597011; -; NOT_ANNOTATED_CDS; Genomic_RNA.
PDB; 3D23; X-ray; 2.50 A; A/B/C/D=3335-3634.
PDBsum; 3D23; -.
ProteinModelPortal; P0C6U3; -.
SMR; P0C6U3; -.
OrthoDB; VOG09000000; -.
EvolutionaryTrace; P0C6U3; -.
Proteomes; UP000008170; 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.
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 4471 Replicase polyprotein 1a.
/FTId=PRO_0000338194.
CHAIN 1 222 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338195.
CHAIN 223 809 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338196.
CHAIN 810 2838 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338197.
CHAIN 2839 3334 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338198.
CHAIN 3335 3637 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338199.
CHAIN 3638 3924 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338200.
CHAIN 3925 4016 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338201.
CHAIN 4017 4210 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338202.
CHAIN 4211 4320 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338203.
CHAIN 4321 4457 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338204.
CHAIN 4458 4471 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338205.
TRANSMEM 2226 2246 Helical. {ECO:0000255}.
TRANSMEM 2287 2307 Helical. {ECO:0000255}.
TRANSMEM 2318 2338 Helical. {ECO:0000255}.
TRANSMEM 2401 2421 Helical. {ECO:0000255}.
TRANSMEM 2443 2463 Helical. {ECO:0000255}.
TRANSMEM 2844 2864 Helical. {ECO:0000255}.
TRANSMEM 3119 3139 Helical. {ECO:0000255}.
TRANSMEM 3151 3171 Helical. {ECO:0000255}.
TRANSMEM 3178 3198 Helical. {ECO:0000255}.
TRANSMEM 3203 3223 Helical. {ECO:0000255}.
TRANSMEM 3651 3671 Helical. {ECO:0000255}.
TRANSMEM 3676 3696 Helical. {ECO:0000255}.
TRANSMEM 3701 3721 Helical. {ECO:0000255}.
TRANSMEM 3744 3764 Helical. {ECO:0000255}.
TRANSMEM 3772 3792 Helical. {ECO:0000255}.
TRANSMEM 3800 3820 Helical. {ECO:0000255}.
TRANSMEM 3843 3863 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.
REPEAT 1055 1064 12.
REPEAT 1065 1074 13.
REPEAT 1075 1084 14.
DOMAIN 1123 1373 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1351 1522 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1718 1978 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3335 3637 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1238 1266 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1835 1871 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4394 4410 {ECO:0000250}.
ZN_FING 4436 4449 {ECO:0000250}.
REGION 945 1084 14 X 10 AA tandem repeat of N-[DN]-D-E-D-
V-V-T-G-D.
REGION 2226 2463 HD1. {ECO:0000250}.
REGION 2844 3223 HD2. {ECO:0000250}.
REGION 3651 3863 HD3. {ECO:0000250}.
COMPBIAS 934 1116 Asp-rich.
COMPBIAS 2229 2321 Phe-rich.
COMPBIAS 2616 2619 Poly-Val.
ACT_SITE 1161 1161 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1312 1312 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1757 1757 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1914 1914 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3375 3375 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3479 3479 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 2838 2839 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3334 3335 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3637 3638 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3924 3925 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4016 4017 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4210 4211 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4320 4321 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4457 4458 Cleavage; by 3CL-PRO. {ECO:0000250}.
TURN 3345 3347 {ECO:0000244|PDB:3D23}.
HELIX 3348 3350 {ECO:0000244|PDB:3D23}.
STRAND 3351 3356 {ECO:0000244|PDB:3D23}.
STRAND 3359 3366 {ECO:0000244|PDB:3D23}.
STRAND 3369 3373 {ECO:0000244|PDB:3D23}.
HELIX 3374 3377 {ECO:0000244|PDB:3D23}.
STRAND 3380 3382 {ECO:0000244|PDB:3D23}.
HELIX 3388 3394 {ECO:0000244|PDB:3D23}.
HELIX 3397 3399 {ECO:0000244|PDB:3D23}.
STRAND 3400 3404 {ECO:0000244|PDB:3D23}.
STRAND 3407 3409 {ECO:0000244|PDB:3D23}.
STRAND 3411 3417 {ECO:0000244|PDB:3D23}.
STRAND 3420 3427 {ECO:0000244|PDB:3D23}.
STRAND 3434 3437 {ECO:0000244|PDB:3D23}.
STRAND 3445 3452 {ECO:0000244|PDB:3D23}.
STRAND 3455 3463 {ECO:0000244|PDB:3D23}.
STRAND 3482 3485 {ECO:0000244|PDB:3D23}.
STRAND 3491 3502 {ECO:0000244|PDB:3D23}.
STRAND 3505 3509 {ECO:0000244|PDB:3D23}.
STRAND 3521 3524 {ECO:0000244|PDB:3D23}.
HELIX 3535 3547 {ECO:0000244|PDB:3D23}.
HELIX 3561 3571 {ECO:0000244|PDB:3D23}.
HELIX 3580 3589 {ECO:0000244|PDB:3D23}.
HELIX 3593 3604 {ECO:0000244|PDB:3D23}.
STRAND 3615 3617 {ECO:0000244|PDB:3D23}.
HELIX 3624 3632 {ECO:0000244|PDB:3D23}.
SEQUENCE 4471 AA; 502589 MW; 6A17587F5DF95C46 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
PTEDVVDGDV VIREPVHLLS ADAIVLKLPS LMKVMTHMDD FSIKSIYNVD LCDCGFVMQY
GYVDCFNDNC DFYGWVSGNM MDGFSCPLCC TVYDSSEVKA QSSGVIPENP VLFTNSTDTV
NHDSFNLYGY 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 ENALNSCKEH PVVGYQVRAF LNKLNENVVY
LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
VTGDNNDEEI VTGDNDDQIV VTGDDVDDIE SIYDFDTYKA LLVFNDVYND ALFVSYGSSV
ETETYFKVNG LWSPTITHTN CWLRSVLLVM QKLPFKFKDL AIENMWLSYK VGYNQSFVDY
LLTTIPKAIV LPQGGFVADF AYWFLNQFDI NAYANWCCLK CGFSFDLNGL DALFFYGDIV
SHVCKCGHNM TLIAADLPCT LHFSLFDDNF CAFCTPKKIF IAACAVDVNV CHSVAVIGDE
QIDGKFVTKF SGDKFDFIVG YGMSFSMSSF ELPQLYGLCI 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 TQTMFDVYVD TFMSHFDVDR KSFNNFVNIA HASLREGVQL
EKVLDTFVGC VRKCCSIDSD VETRFITKSM ISAVAAGLEF TDENYNNLVP TYLKSDNIVA
ADLGVLIQNG AKHVQGNVAK AANISCIWFI DAFNQLTADL QHKLKKACVK TGLKLKLTFN
KQEASVPILT TPFSLKGGVV LSNLLYILFF VSLICFILLW ALLPTYSVYK SDIHLPAYAS
FKVIDNGVVR DISVNDLCFA NKFFQFDQWY ESTFGSVYYH NSMDCPIVVA VMDEDIGSTM
FNVPTKVLRH GFHVLHFLTY AFASDSVQCY TPHIQISYND FYASGCVLSS LCTMFKRGDG
TPHPYCYSDG VMKNASLYTS LVPHTRYSLA NSNGFIRFPD VISEGIVRIV RTRSMTYCRV
GACEYAEEGI CFNFNSSWVL NNDYYRSMPG TFCGRDLFDL FYQFFSSLIR PIDFFSLTAS
SIFGAILAIV VVLVFYYLIK LKRAFGDYTS VVVINVVVWC INFLMLFVFQ VYPICACVYA
CFYFYVTLYF PSEISVIMHL QWIVMYGAIM PFWFCVTYVA MVIANHVLWL FSYCRKIGVN
VCSDSTFEET SLTTFMITKD SYCRLKNSVS DVAYNRYLSL YNKYRYYSGK MDTAAYREAA
CSQLAKAMET FNHNNGNDVL YQPPTASVST SFLQSGIVKM VSPTSKIEPC IVSVTYGSMT
LNGLWLDDKV YCPRHVICSS SNMNEPDYSA LLCRVTLGDF TIMSGRMSLT VVSYQMQGCQ
LVLTVSLQNP YTPKYTFGNV KPGETFTVLA AYNGRPQGAF HVTMRSSYTI KGSFLCGSCG
SVGYVLTGDS VKFVYMHQLE LSTGCHTGTD FTGNFYGPYR DAQVVQLPVK DYVQTVNVIA
WLYAAILNNC AWFVQNDVCS TEDFNVWAMA NGFSQVKADL VLDALASMTG VSIETLLAAI
KRLYMGFQGR QILGSCTFED ELAPSDVYQQ LAGVKLQSKT KRFIKETIYW ILISTFLFSC
IISAFVKWTI FMYINTHMIG VTLCVLCFVS FMMLLVKHKH FYLTMYIIPV LCTLFYVNYL
VVYKEGFRGF TYVWLSYFVP AVNFTYVYEV FYGCILCVFA IFITMHSINH DIFSLMFLVG
RIVTLISMWY FGSNLEEDVL LFITAFLGTY TWTTILSLAI AKIVANWLSV NIFYFTDVPY
IKLILLSYLF IGYILSCYWG FFSLLNSVFR MPMGVYNYKI SVQELRYMNA NGLRPPRNSF
EAILLNLKLL GIGGVPVIEV SQIQSKLTDV KCANVVLLNC LQHLHVASNS KLWQYCSVLH
NEILSTSDLS VAFDKLAQLL IVLFANPAAV DTKCLASIDE VSDDYVQDST VLQALQSEFV
NMASFVEYEV AKKNLADAKN SGSVNQQQIK QLEKACNIAK SVYERDKAVA RKLERMADLA
LTNMYKEARI NDKKSKVVSA LQTMLFSMVR KLDNQALNSI LDNAVKGCVP LSAIPALAAN
TLTIVIPDKQ VFDKVVDNVY VTYAGSVWHI QTVQDADGIN KQLTDISVDS NWPLVIIANR
YNEVANAVMQ NNELMPHKLK IQVVNSGSDM NCNIPTQCYY NNGSSGRIVY AVLSDVDGLK
YTKIMKDDGN CVVLELDPPC KFSIQDVKGL KIKYLYFIKG CNTLARGWVV GTLSSTIRLQ
AGVATEYAAN SSILSLCAFS VDPKKTYLDY IQQGGVPIIN CVKMLCDHAG TGMAITIKPE
ATINQDSYGG ASVCIYCRAR VEHPDVDGIC KLRGKFVQVP LGIKDPILYV LTHDVCQVCG
FWRDGSCSCV GSSVAVQSKD LNFLNGFGVL V


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