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Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]

 R1A_BC133               Reviewed;        4441 AA.
P0C6F7; Q0Q4F3;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
18-JUL-2018, entry version 68.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=Leader protein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65 homolog;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=PL2-PRO;
AltName: Full=Papain-like proteinase;
Short=PL-PRO;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Bat coronavirus 133/2005 (BtCoV) (BtCoV/133/2005).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=389230;
NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16840328; DOI=10.1128/JVI.00697-06;
Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
"Prevalence and genetic diversity of coronaviruses in bats from
China.";
J. Virol. 80:7481-7490(2006).
[2]
FUNCTION OF NSP1.
PubMed=19264783; DOI=10.1128/JVI.02485-08;
Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K.,
Makino S.;
"Suppression of host gene expression by nsp1 proteins of group 2 bat
coronaviruses.";
J. Virol. 83:5282-5288(2009).
-!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for
the cleavages located at the N-terminus of replicase polyprotein.
In addition, PL-PRO 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. {ECO:0000269|PubMed:19264783}.
-!- 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.
{ECO:0000269|PubMed:19264783}.
-!- 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 (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=P0C6F7-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W1-1; 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. {ECO:0000250}.
-!- 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}.
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EMBL; DQ648794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; P0C6F7; -.
SMR; P0C6F7; -.
PRIDE; P0C6F7; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000007449; 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.
Gene3D; 3.40.220.20; -; 1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR038400; Nsp3_coronavir_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; 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; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF11633; SUD-M; 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; 1.
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_0000338062.
CHAIN 1 195 Non-structural protein 1. {ECO:0000255}.
/FTId=PRO_0000338063.
CHAIN 196 847 Non-structural protein 2. {ECO:0000255}.
/FTId=PRO_0000338064.
CHAIN 848 2791 Non-structural protein 3. {ECO:0000255}.
/FTId=PRO_0000338065.
CHAIN 2792 3298 Non-structural protein 4. {ECO:0000255}.
/FTId=PRO_0000338066.
CHAIN 3299 3604 3C-like proteinase. {ECO:0000255}.
/FTId=PRO_0000338067.
CHAIN 3605 3896 Non-structural protein 6. {ECO:0000255}.
/FTId=PRO_0000338068.
CHAIN 3897 3979 Non-structural protein 7. {ECO:0000255}.
/FTId=PRO_0000338069.
CHAIN 3980 4178 Non-structural protein 8. {ECO:0000255}.
/FTId=PRO_0000338070.
CHAIN 4179 4288 Non-structural protein 9. {ECO:0000255}.
/FTId=PRO_0000338071.
CHAIN 4288 4441 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338073.
CHAIN 4289 4427 Non-structural protein 10. {ECO:0000255}.
/FTId=PRO_0000338072.
TRANSMEM 2152 2172 Helical. {ECO:0000255}.
TRANSMEM 2229 2249 Helical. {ECO:0000255}.
TRANSMEM 2333 2353 Helical. {ECO:0000255}.
TRANSMEM 2357 2377 Helical. {ECO:0000255}.
TRANSMEM 2382 2402 Helical. {ECO:0000255}.
TRANSMEM 2807 2827 Helical. {ECO:0000255}.
TRANSMEM 3079 3099 Helical. {ECO:0000255}.
TRANSMEM 3112 3132 Helical. {ECO:0000255}.
TRANSMEM 3156 3176 Helical. {ECO:0000255}.
TRANSMEM 3610 3630 Helical. {ECO:0000255}.
TRANSMEM 3644 3664 Helical. {ECO:0000255}.
TRANSMEM 3669 3689 Helical. {ECO:0000255}.
TRANSMEM 3714 3734 Helical. {ECO:0000255}.
TRANSMEM 3742 3762 Helical. {ECO:0000255}.
TRANSMEM 3791 3811 Helical. {ECO:0000255}.
TRANSMEM 3815 3835 Helical. {ECO:0000255}.
DOMAIN 1159 1328 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1600 1871 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3299 3604 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1721 1758 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4362 4378 {ECO:0000250}.
ZN_FING 4404 4417 {ECO:0000250}.
REGION 2119 2402 HD1. {ECO:0000250}.
REGION 2807 3176 HD2. {ECO:0000250}.
REGION 3610 3835 HD3. {ECO:0000250}.
COMPBIAS 960 1059 Glu-rich.
ACT_SITE 1641 1641 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1807 1807 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3339 3339 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3446 3446 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 195 196 Cleavage. {ECO:0000255}.
SITE 847 848 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 2791 2792 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 3298 3299 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3604 3605 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3896 3897 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3979 3980 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4178 4179 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4288 4289 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4427 4428 Cleavage; by 3CL-PRO. {ECO:0000255}.
SEQUENCE 4441 AA; 492464 MW; A6E0DB4CDDA40AC7 CRC64;
MLSKAGVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTED MASKLTPWFE DGETAFNQVS
SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS KHFLVNQLAY KDHVGAAMMR
TTLNVKPLGM FFPYDSSLET GEHTFLLRKN GLGGQLFRER PWDRKETPYV EILDDLEADP
TGKYSQNLLK KLIGGDCIPV DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS
DRFIVLNKKL YRVVWNVTRR NVPYSKQTAF TVVSVIQCDD KESVPEHTFT IGSQILMVSP
LKATNNKNFN LKQRLLHTFY GKEAVQQPGY IYHSAYVDCN ACGRGTWCTG NAIQGFACDC
GANYSANDVD LQSSGLVPKN ALFLANCPCA NNGACSHNAA QVYSILDGKA CVEVGGKSFT
LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR IGDAIFTGCT GTWDKVVETA NLFLEKAQHS
LNFCQQFALT EVVLAILSGT TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI
NIGANGVCNA TINAPFIAFT GLGESFKKVA AIPWKICSNL KSALDYYCSN IMFRVFPYDI
PCDVNDFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SNACQTALSS FLNACVAASR
ATAGFISDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ QVLDIMSKAM KLLHTNVSWA
GTKLSAIIYE GREALLFNSG TYFCLSTKAK TLQDQMNLVL PGDYNKKTLG ILDPVPNADT
IDVTANSTVV DVVHGQLEPT NEHGPSMIVG NYVLVSDKLF VRTDDEEFYP LCINGKVVST
LFRLKGGMPS KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN MTFSINPVED
VEEVEEFIED DYLSDELPIA DDEEAWTRAV EEVMPLDDIL VAEIELEEDL PLETALESVE
AEVGESISDE LCVVETAKAQ EPSVESTDST PSTSTVVSEN DLSVKPMSRV AETGDVLEVE
TAVVGGPVSD VTASVVTNDI VSVEQAQQCG VSSLPIQDEA SENQVHQVPD LQCTSETKVE
IVQPRQDLRP RRLRKSKVDL SKYKHTVINN SVTLVLGDAI QIASLLPKCV LVNAANRHLK
HGGGIAGAIN KASGGDVQEE SDEYISNSGP LHVGDSVLLK GYGLADAILR VVGPDARNNE
DAALLKRCYK TFNKHTIVVT PLISSGIFSV DPKVSFEYLL ANVTTTTYVV VNNEDIYNTL
ATPSKPDGLV YSFEGWRGTV RTAKNYGFTC FICTEYSANV KFLRTKGVDT TKKIQTVDGV
SYYLYSARDA LTDVIAAANG CPGICAMPFG YVTHGLDLAQ SGNYVRQVKV PYVCLLASKE
QIPIMNSDVA IQTPETAFIN NVTSNGGYHS WHLVSGDLIV KDVCYKKLLH WSGQTICYAD
NKFYVVKNDV ALPFSDLEAC RAYLTSRAAQ QVNIEVLVTI DGVNFRTVIL NDATTFRKQL
GATFYKGVDI SDALPTVKMG GESLFVADNL SESEEVVLKE YYGTSDVTFL QRYYSLQPLV
QQWKFVVHDG VKSLKLSNYN CYINATIMMI DMLHDIKFVV PALQNAYLRY KGGDPYDFLA
LIMAYGDCTF DNPDDEAKLL HTLLAKAELT VSAKMVWREW CTVCGIRDIE YTGMRACVYA
GVNSMEELQS VFNETCVCGS VKHRQLVEHS TPWLLVSGLN EVKVSTSTDP VYRAFNVFQG
VETSVGHYVH VRVKDGLFYK YDSGSLTKTS DMKCKMTSVW YPKVRYTADC NVVVYDLDGV
TKVEVNPDLS NYYMKDGKYY TSKPTIKYSP ATILPGSVYS NSCLVGVDGT PGSDTISKFF
NDLLGFDETK PISKKLTYSL LPNEDGDVLL SEFNNYNPVY KKGVMLKGKP ILWVNNGVCD
SALNKPNRAS LRQLYDVAPI VLDNKYTVLQ DNTSQLIEPN VPVVEDVSIT TRKLIEVKCK
GLNKPFVKGN FSFVNDPNGV TVVDTLGLTE LRALYVDINT RYIVLRDNNW SSLFKLHTVE
SGDLQIVANG GSVTRRARVL LGASSLFASF AKITVTATTA ACKTAGRSFC KFVVNYGVLQ
NMFLFLKMLF FLPFNYLWPK KQPTVDVGVS GLRTAGVVTT NIVKQCGTAA YYMLLGKFKR
VDWKATLRLF LLLCTTILLL SSIYHLVIFN QVLSSDVMLE DATGILAMYK EVRSYLGIRT
LCDGLAVEYR NTSFDVVDFC SNRSVLCQWC LIGQDSLTRY SALQMLQTHI TSYVLNIDWI
WFALEFFLAY VLYTSSFNVL LLVVTAQYFF AYTSAFVNWR AYNYIVSGLF FLVTHIPLHG
LVRVYNFLAC LWFLRKFYSH VINGCKDTAC LLCYKRNRLT RVEASTIVCG TKRTFYIAAN
GGTSYCCKHN WNCVECDTAG VGNTFICTEV ANDLTTTLRR LIKPTDQSHY YVDSVVVKDA
VVELHYNRDG SSCYERYPLC YFTNLEKLKF KEVCKTPTGI PEHNFLIYDT NDRGQENLAR
SACVYYSQVL CKPMLLVDVN LVTTVGDSRE IAIKMLDSFI NSFISLFSVS RDKLEKLINT
ARDCVRRGDD FQTVLKTFTD AARGHAGVES DVETTMVVDA LQYAHKNDIQ LTTECYNNYV
PGYIKPDSIN TLDLGCLIDL KAASVNQTSM RNANGACVWN SGDYMKLSDS FKRQIRIACR
KCNIPFRLTT SKLRAADNIL SVKFSATKIV GGAPSWLLRV RDLTVKGYCI LTLFVFTVAV
LSWFCLPSYS IATVNFNDDR ILTYKVIENG IVRDIAPNDA CFANKYGHFS KWFNENHGGV
YRNSVDCPIT IAVIAGVAGA RVANVPATLA WVGRQIVLFV SRVFANTNVC FTPTNEIPYD
TFSDSGCVLS SECTLFRDAE GNLNPFCYDP TVLPGASSYA DMKPHVRYDM YDSDMYIKFP
EVIFESTLRI TKTLATQYCR FGSCEESAAG VCISTNGSWA LYNQNYSTRP GIYCGDDYFD
IVRRLAVSLF QPVTYFQLST SLAMGLVLCV FLTAAFYYIN KVKRALADYT QCAVVAVVAA
LLNSLCLCFI VANPLLVAPY TAMYYYATFY LTGEPAFIMH ISWYVMFGTV VPIWMLASYT
VGVMLRHLFW VLAYFSKKHV DVFTDGKLNC SFQDAASNIF VIGKDTYVAL RNAITQDSFV
RYLSLFNKYK YYSGAMDTAS YREACAAHLC KALQTYSETG SDILYQPPNC SVTSSVLQSG
LVKMSAPSGA VENCIVQVTC GSMTLNGLWL DNTVWCPRHI MCPADQLTDP NYDALLISKT
NHSFIVQKHI GAQANLRVVA HSMVGVLLKL TVDVANPSTP AYTFSTVKPG ASFSVLACYN
GKPTGVFTVN LRHNSTIKGS FLCGSCGSVG YTENGGVLNF VYMHQMELSN GTHTGSSFDG
VMYGAFEDKQ THQLQLTDKY CTINVVAWLY AAVLNGCKWF VKPTRVGIVT YNEWALSNQF
TEFVGTQSID MLAHRTGVSV EQMLAAIQSL HAGFQGKTIL GQSTLEDEFT PDDVNMQVMG
VVMQSGVKRI SYGFMHWLMS TLVLAYVSVM QLTKFTMWTY LFETIPTQMT PLLFGFMACV
MFTVKHKHTF LSLFLLPVAL CLTYANIVYE PQTLVSSTLI AVANWLTPTS VYMRTTHLDF
GLYISLSFVL AIIVRRLYRP SMSNLALALC SGVMWFYTYV IGDHSSPITY LMFITTLTSD
YTITVFATVN LAKFISGLVF LYAPHLGFIL PEVKLVLLIY LCLGYMCTMY FGVFSLLNLK
LRVPLGVYDY SVSTQEFRFL TGNGLHAPRN SWEALILNFK LLGIGGTPCI KVATVQSKLT
DLKCTSVVLL TVLQQLHLES NSKAWSYCVK LHNEILAAVD PTEAFERFVC LFATLMSFSA
NVDLDALAND LFENSSVLQA TLTEFSHLAT YAELETAQSS YQKALNSGDA SPQVLKALQK
AVNVAKNAYE KDKAVARKLE RMAEQAMTSM YKQARAEDKK AKIVSAMQTM LFGMIKKLDN
DVLNGVIANA RNGCVPLSIV PLCASNKLRV VIPDISVWNK VVNWPSVSYA GSLWDVTVIN
NVDNEVVKPT DVVETNESLT WPLVIECSRA SSSAVKLQNN EIHPKGLKTM VVTAGIDQVN
CSSSAVAYYE PVQGHRMVMG LLSENAHLKW AKVEGKDGFI NIELQPPCKF LIAGPKGPEI
RYLYFVKNLN NLHRGQLLGH IAATVRLQAG ANTEFASNST VLTLVAFAVD PAKAYLDYVG
SGGTPLSNYV KMLAPKTGTG VAISVKPEAT ADQETYGGAS VCLYCRAHIE HPDVSGVCKY
KTRFVQIPAH VRDPVGFLLK NVPCNVCQYW VGYGCNCDAL RNNTVPQSKD TNFLNESGVL
V


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