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 R1A_CVPPU               Reviewed;        4017 AA.
P0C6V2; Q9IW06;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 65.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a 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=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Porcine transmissible gastroenteritis coronavirus (strain Purdue)
(TGEV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=11151;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Isolate Purdue-115;
PubMed=7856095; DOI=10.1006/viro.1995.1004;
Eleouet J., Rasschaert D., Lambert P., Levy L., Vende P., Laude H.;
"Complete sequence (20 kilobases) of the polyprotein-encoding gene 1
of transmissible gastroenteritis virus.";
Virology 206:817-822(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate PUR46-MAD;
PubMed=10805807; DOI=10.1073/pnas.97.10.5516;
Almazan F., Gonzalez J.M., Penzes Z., Izeta A., Calvo E.,
Plana-Duran J., Enjuanes L.;
"Engineering the largest RNA virus genome as an infectious bacterial
artificial chromosome.";
Proc. Natl. Acad. Sci. U.S.A. 97:5516-5521(2000).
[3]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
STRAIN=Isolate Purdue-115;
PubMed=11842254;
Hegyi A., Ziebuhr J.;
"Conservation of substrate specificities among coronavirus main
proteases.";
J. Gen. Virol. 83:595-599(2002).
[4]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 2879-3180.
PubMed=12093723; DOI=10.1093/emboj/cdf327;
Anand K., Palm G.J., Mesters J.R., Siddell S.G., Ziebuhr J.,
Hilgenfeld R.;
"Structure of coronavirus main proteinase reveals combination of a
chymotrypsin fold with an extra alpha-helical domain.";
EMBO J. 21:3213-3224(2002).
[5]
X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 2879-3180 COMPLEXED WITH THE
SUBSTRATE-ANALOG HEXAPEPTIDYL CMK.
PubMed=12746549; DOI=10.1126/science.1085658;
Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.;
"Coronavirus main proteinase (3CLpro) structure: basis for design of
anti-SARS drugs.";
Science 300:1763-1767(2003).
-!- 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-|-[SAGC]. Inhibited by the substrate-analog
Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK.
-!- 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}.
-!- 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=P0C6V2-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6Y5-1; 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 is autocatalytically processed.
{ECO:0000269|PubMed:11842254}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; Z34093; CAA83979.1; -; mRNA.
EMBL; AJ271965; CAB91144.1; -; Genomic_RNA.
PDB; 1LVO; X-ray; 1.96 A; A/B/C/D/E/F=2879-3180.
PDB; 1P9U; X-ray; 2.37 A; A/B/C/D/E/F=2879-3180.
PDB; 2AMP; X-ray; 2.70 A; A/B=2879-3180.
PDB; 3MP2; X-ray; 2.50 A; A=1071-1281.
PDB; 3ZBD; X-ray; 1.49 A; A/B=1-105.
PDB; 4F49; X-ray; 2.25 A; A/B/C/D=2879-3181.
PDBsum; 1LVO; -.
PDBsum; 1P9U; -.
PDBsum; 2AMP; -.
PDBsum; 3MP2; -.
PDBsum; 3ZBD; -.
PDBsum; 4F49; -.
ProteinModelPortal; P0C6V2; -.
SMR; P0C6V2; -.
OrthoDB; VOG09000000; -.
BRENDA; 3.4.22.B14; 4985.
EvolutionaryTrace; P0C6V2; -.
Proteomes; UP000001440; 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: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:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR032039; A-CoV_nsp1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR014827; Viral_protease.
Pfam; PF16688; CNV-Replicase_N; 1.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF09401; NSP10; 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; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 2.
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; 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;
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 4017 Replicase polyprotein 1a.
/FTId=PRO_0000338302.
CHAIN 1 110 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338303.
CHAIN 111 879 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338304.
CHAIN 880 2388 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338305.
CHAIN 2389 2878 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338306.
CHAIN 2879 3180 3C-like proteinase.
/FTId=PRO_0000338307.
CHAIN 3181 3474 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338308.
CHAIN 3475 3557 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338309.
CHAIN 3558 3752 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338310.
CHAIN 3753 3863 Non-structural protein 9.
/FTId=PRO_0000338311.
CHAIN 3864 3998 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338312.
CHAIN 3999 4017 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338313.
TRANSMEM 1896 1916 Helical. {ECO:0000255}.
TRANSMEM 1995 2015 Helical. {ECO:0000255}.
TRANSMEM 2033 2053 Helical. {ECO:0000255}.
TRANSMEM 2401 2421 Helical. {ECO:0000255}.
TRANSMEM 2467 2487 Helical. {ECO:0000255}.
TRANSMEM 2497 2517 Helical. {ECO:0000255}.
TRANSMEM 2538 2558 Helical. {ECO:0000255}.
TRANSMEM 2666 2686 Helical. {ECO:0000255}.
TRANSMEM 2695 2715 Helical. {ECO:0000255}.
TRANSMEM 2721 2741 Helical. {ECO:0000255}.
TRANSMEM 2746 2766 Helical. {ECO:0000255}.
TRANSMEM 3187 3207 Helical. {ECO:0000255}.
TRANSMEM 3217 3237 Helical. {ECO:0000255}.
TRANSMEM 3242 3262 Helical. {ECO:0000255}.
TRANSMEM 3280 3300 Helical. {ECO:0000255}.
TRANSMEM 3313 3333 Helical. {ECO:0000255}.
TRANSMEM 3347 3367 Helical. {ECO:0000255}.
TRANSMEM 3371 3391 Helical. {ECO:0000255}.
TRANSMEM 3394 3414 Helical. {ECO:0000255}.
DOMAIN 1055 1299 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1318 1489 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1550 1803 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2879 3180 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1164 1195 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 3937 3953 {ECO:0000250}.
ZN_FING 3979 3992 {ECO:0000250}.
REGION 1896 2053 HD1.
REGION 2401 2766 HD2.
REGION 3187 3414 HD3.
COMPBIAS 932 1042 Glu-rich.
ACT_SITE 1093 1093 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1244 1244 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1588 1588 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1741 1741 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 2919 2919 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3022 3022 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 110 111 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 879 880 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2388 2389 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 2878 2879 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3180 3181 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3474 3475 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3557 3558 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3752 3753 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3863 3864 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3998 3999 Cleavage; by 3CL-PRO. {ECO:0000250}.
VARIANT 572 572 F -> S (in strain: Isolate Purdue-115).
VARIANT 1041 1041 E -> D (in strain: Isolate Purdue-115).
VARIANT 2375 2375 P -> T (in strain: Isolate Purdue-115).
VARIANT 2381 2381 E -> Q (in strain: Isolate Purdue-115).
STRAND 4 10 {ECO:0000244|PDB:3ZBD}.
HELIX 23 36 {ECO:0000244|PDB:3ZBD}.
STRAND 41 45 {ECO:0000244|PDB:3ZBD}.
HELIX 46 51 {ECO:0000244|PDB:3ZBD}.
STRAND 59 75 {ECO:0000244|PDB:3ZBD}.
STRAND 84 90 {ECO:0000244|PDB:3ZBD}.
STRAND 96 104 {ECO:0000244|PDB:3ZBD}.
STRAND 1077 1080 {ECO:0000244|PDB:3MP2}.
STRAND 1083 1086 {ECO:0000244|PDB:3MP2}.
HELIX 1093 1102 {ECO:0000244|PDB:3MP2}.
HELIX 1111 1116 {ECO:0000244|PDB:3MP2}.
TURN 1117 1119 {ECO:0000244|PDB:3MP2}.
HELIX 1122 1132 {ECO:0000244|PDB:3MP2}.
HELIX 1142 1150 {ECO:0000244|PDB:3MP2}.
STRAND 1156 1164 {ECO:0000244|PDB:3MP2}.
STRAND 1167 1180 {ECO:0000244|PDB:3MP2}.
STRAND 1183 1185 {ECO:0000244|PDB:3MP2}.
STRAND 1187 1191 {ECO:0000244|PDB:3MP2}.
TURN 1193 1195 {ECO:0000244|PDB:3MP2}.
STRAND 1198 1217 {ECO:0000244|PDB:3MP2}.
HELIX 1223 1225 {ECO:0000244|PDB:3MP2}.
STRAND 1226 1228 {ECO:0000244|PDB:3MP2}.
STRAND 1231 1238 {ECO:0000244|PDB:3MP2}.
TURN 1240 1242 {ECO:0000244|PDB:3MP2}.
STRAND 1244 1249 {ECO:0000244|PDB:3MP2}.
TURN 1250 1253 {ECO:0000244|PDB:3MP2}.
STRAND 1254 1257 {ECO:0000244|PDB:3MP2}.
STRAND 1260 1262 {ECO:0000244|PDB:3MP2}.
STRAND 1269 1280 {ECO:0000244|PDB:3MP2}.
TURN 2889 2891 {ECO:0000244|PDB:4F49}.
HELIX 2892 2894 {ECO:0000244|PDB:4F49}.
STRAND 2895 2900 {ECO:0000244|PDB:4F49}.
STRAND 2903 2910 {ECO:0000244|PDB:4F49}.
STRAND 2913 2917 {ECO:0000244|PDB:4F49}.
HELIX 2918 2921 {ECO:0000244|PDB:4F49}.
HELIX 2931 2936 {ECO:0000244|PDB:4F49}.
HELIX 2940 2942 {ECO:0000244|PDB:4F49}.
STRAND 2943 2948 {ECO:0000244|PDB:4F49}.
STRAND 2950 2952 {ECO:0000244|PDB:4F49}.
STRAND 2954 2960 {ECO:0000244|PDB:4F49}.
STRAND 2963 2970 {ECO:0000244|PDB:4F49}.
STRAND 2988 2995 {ECO:0000244|PDB:4F49}.
STRAND 2998 3006 {ECO:0000244|PDB:4F49}.
STRAND 3025 3030 {ECO:0000244|PDB:4F49}.
STRAND 3033 3043 {ECO:0000244|PDB:4F49}.
STRAND 3049 3052 {ECO:0000244|PDB:4F49}.
HELIX 3059 3061 {ECO:0000244|PDB:4F49}.
HELIX 3078 3090 {ECO:0000244|PDB:4F49}.
HELIX 3104 3111 {ECO:0000244|PDB:4F49}.
TURN 3112 3115 {ECO:0000244|PDB:4F49}.
HELIX 3123 3125 {ECO:0000244|PDB:4F49}.
HELIX 3126 3132 {ECO:0000244|PDB:4F49}.
HELIX 3136 3146 {ECO:0000244|PDB:4F49}.
STRAND 3158 3160 {ECO:0000244|PDB:4F49}.
HELIX 3167 3175 {ECO:0000244|PDB:4F49}.
SEQUENCE 4017 AA; 447352 MW; 97ED2B170C4FD248 CRC64;
MSSKQFKILV NEDYQVNVPS LPIRDVLQEI KYCYRNGFEG YVFVPEYCRD LVDCDRKDHY
VIGVLGNGVS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF DLKIARTGRG AIYVDQYMCG
ADGKPVIEGD FKDYFGDEDI IEFEGEEYHC AWTTVRDEKP LNQQTLFTIQ EIQYNLDIPH
KLPNCATRHV APPVKKNSKI VLSEDYKKLY DIFGSPFMGN GDCLSKCFDT LHFIAATLRC
PCGSESSGVG DWTGFKTACC GLSGKVKGVT LGDIKPGDAV VTSMSAGKGV KFFANCVLQY
AGDVEGVSIW KVIKTFTVDE TVCTPGFEGE LNDFIKPESK SLVACSVKRA FITGDIDDAV
HDCIITGKLD LSTNLFGNVG LLFKKTPWFV QKCGALFVDA WKVVEELCGS LTLTYKQIYE
VVASLCTSAF TIVNYKPTFV VPDNRVKDLV DKCVKVLVKA FDVFTQIITI AGIEAKCFVL
GAKYLLFNNA LVKLVSVKIL GKKQKGLECA FFATSLVGAT VNVTPKRTET ATISLNKVDD
VVAPGEGYIV IVGDMAFYKS GEYYFMMSSP NFVLTNNVFK AVKVPSYDIV YDVDNDTKSK
MIAKLGSSFE YDGDIDAAIV KVNELLIEFR QQSLCFRAFK DDKSIFVEAY FKKYKMPACL
AKHIGLWNII KKDSCKRGFL NLFNHLNELE DIKETNIQAI KNILCPDPLL DLDYGAIWYN
CMPGCSDPSV LGSVQLLIGN GVKVVCDGCK GFANQLSKGY NKLCNAARND IEIGGIPFST
FKTPTNTFIE MTDAIYSVIE QGKALSFRDA DVPVVDNGTI STADWSEPIL LEPAEYVKPK
NNGNVIVIAG YTFYKDEDEH FYPYGFGKIV QRMYNKMGGG DKTVSFSEEV DVQEIAPVTR
VKLEFEFDNE IVTGVLERAI GTRYKFTGTT WEEFEESISE ELDAIFDTLA NQGVELEGYF
IYDTCGGFDI KNPDGIMISQ YDINITADEK SEVSASSEEE EVESVEEDPE NEIVEASEGA
EGTSSQEEVE TVEVADITST EEDVDIVEVS AKDDPWAAAV DVQEAEQFNP SLPPFKTTNL
NGKIILKQGD NNCWINACCY QLQAFDFFNN EAWEKFKKGD VMDFVNLCYA ATTLARGHSG
DAEYLLELML NDYSTAKIVL AAKCGCGEKE IVLERAVFKL TPLKESFNYG VCGDCMQVNT
CRFLSVEGSG VFVHDILSKQ TPEAMFVVKP VMHAVYTGTT QNGHYMVDDI EHGYCVDGMG
IKPLKKRCYT STLFINANVM TRAEKPKQEF KVEKVEQQPI VEENKSSIEK EEIQSPKNDD
LILPFYKAGK LSFYQGALDV LINFLEPDVI VNAANGDLKH MGGVARAIDV FTGGKLTERS
KDYLKKNKSI APGNAVFFEN VIEHLSVLNA VGPRNGDSRV EAKLCNVYKA IAKCEGKILT
PLISVGIFNV RLETSLQCLL KTVNDRGLNV FVYTDQERQT IENFFSCSIP VNVTEDNVNH
ERVSVSFDKT YGEQLKGTVV IKDKDVTNQL PSAFDVGQKV IKAIDIDWQA HYGFRDAAAF
SASSHDAYKF EVVTHSNFIV HKQTDNNCWI NAICLALQRL KPQWKFPGVR GLWNEFLERK
TQGFVHMLYH ISGVKKGEPG DAELMLHKLG DLMDNDCEII VTHTTACDKC AKVEKFVGPV
VAAPLAIHGT DETCVHGVSV NVKVTQIKGT VAITSLIGPI IGEVLEATGY ICYSGSNRNG
HYTYYDNRNG LVVDAEKAYH FNRDLLQVTT AIASNFVVKK PQAEERPKNC AFNKVAASPK
IVQEQKLLAI ESGANYALTE FGRYADMFFM AGDKILRLLL EVFKYLLVLF MCLRSTKMPK
VKVKPPLAFK DFGAKVRTLN YMRQLNKPSV WRYAKLVLLL IAIYNFFYLF VSIPVVHKLT
CNGAVQAYKN SSFIKSAVCG NSILCKACLA SYDELADFQH LQVTWDFKSD PLWNRLVQLS
YFAFLAVFGN NYVRCFLMYF VSQYLNLWLS YFGYVEYSWF LHVVNFESIS AEFVIVVIVV
KAVLALKHIV FACSNPSCKT CSRTARQTRI PIQVVVNGSM KTVYVHANGT GKFCKKHNFY
CKNCDSYGFE NTFICDEIVR DLSNSVKQTV YATDRSHQEV TKVECSDGFY RFYVGDEFTS
YDYDVKHKKY SSQEVLKSML LLDDFIVYSP SGSALANVRN ACVYFSQLIG KPIKIVNSDL
LEDLSVDFKG ALFNAKKNVI KNSFNVDVSE CKNLDECYRA CNLNVSFSTF EMAVNNAHRF
GILITDRSFN NFWPSKVKPG SSGVSAMDIG KCMTSDAKIV NAKVLTQRGK SVVWLSQDFA
ALSSTAQKVL VKTFVEEGVN FSLTFNAVGS DDDLPYERFT ESVSPKSGSG FFDVITQLKQ
IVILVFVFIF ICGLCSVYSV ATQSYIESAE GYDYMVIKNG IVQPFDDTIS CVHNTYKGFG
DWFKAKYGFI PTFGKSCPIV VGTVFDLENM RPIPDVPAYV SIVGRSLVFA INAAFGVTNM
CYDHTGNAVS KDSYFDTCVF NTACTTLTGL GGTIVYCAKQ GLVEGAKLYS DLMPDYYYEH
ASGNMVKLPA IIRGLGLRFV KTQATTYCRV GECIDSKAGF CFGGDNWFVY DNEFGNGYIC
GNSVLGFFKN VFKLFNSNMS VVATSGAMLV NIIIACLAIA MCYGVLKFKK IFGDCTFLIV
MIIVTLVVNN VSYFVTQNTF FMIIYAIVYY FITRKLAYPG ILDAGFIIAY INMAPWYVIT
AYILVFLYDS LPSLFKLKVS TNLFEGDKFV GNFESAAMGT FVIDMRSYET IVNSTSIARI
KSYANSFNKY KYYTGSMGEA DYRMACYAHL GKALMDYSVN RTDMLYTPPT VSVNSTLQSG
LRKMAQPSGL VEPCIVRVSY GNNVLNGLWL GDEVICPRHV IASDTTRVIN YENEMSSVRL
HNFSVSKNNV FLGVVSARYK GVNLVLKVNQ VNPNTPEHKF KSIKAGESFN ILACYEGCPG
SVYGVNMRSQ GTIKGSFIAG TCGSVGYVLE NGILYFVYMH HLELGNGSHV GSNFEGEMYG
GYEDQPSMQL EGTNVMSSDN VVAFLYAALI NGERWFVTNT SMSLESYNTW AKTNSFTELS
STDAFSMLAA KTGQSVEKLL DSIVRLNKGF GGRTILSYGS LCDEFTPTEV IRQMYGVNLQ
AGKVKSFFYP IMTAMTILFA FWLEFFMYTP FTWINPTFVS IVLAVTTLIS TVFVSGIKHK
MLFFMSFVLP SVILVTAHNL FWDFSYYESL QSIVENTNTM FLPVDMQGVM LTVFCFIVFV
TYSVRFFTCK QSWFSLAVTT ILVIFNMVKI FGTSDEPWTE NQIAFCFVNM LTMIVSLTTK
DWMVVIASYR IAYYIVVCVM PSAFVSDFGF MKCISIVYMA CGYLFCCYYG ILYWVNRFTC
MTCGVYQFTV SAAELKYMTA NNLSAPKNAY DAMILSAKLI GVGGKRNIKI STVQSKLTEM
KCTNVVLLGL LSKMHVESNS KEWNYCVGLH NEINLCDDPE IVLEKLLALI AFFLSKHNTC
DLSELIESYF ENTTILQSVA SAYAALPSWI ALEKARADLE EAKKNDVSPQ ILKQLTKAFN
IAKSDFEREA SVQKKLDKMA EQAAASMYKE ARAVDRKSKI VSAMHSLLFG MLKKLDMSSV
NTIIDQARNG VLPLSIIPAA SATRLVVITP SLEVFSKIRQ ENNVHYAGAI WTIVEVKDAN
GSHVHLKEVT AANELNLTWP LSITCERTTK LQNNEIMPGK LKERAVRASA TLDGEAFGSG
KALMASESGK SFMYAFIASD NNLKYVKWES NNDIIPIELE APLRFYVDGA NGPEVKYLYF
VKNLNTLRRG AVLGYIGATV RLQAGKPTEH PSNSSLLTLC AFSPDPAKAY VDAVKRGMQP
VNNCVKMLSN GAGNGMAVTN GVEANTQQDS YGGASVCIYC RCHVEHPAID GLCRYKGKFV
QIPTGTQDPI RFCIENEVCV VCGCWLNNGC MCDRTSMQSF TVDQSYLNEC GVLVQLD


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