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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_BCRP3               Reviewed;        4380 AA.
P0C6T7; Q3I5J6;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
22-APR-2020, entry version 73.
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 Rp3/2004 (BtCoV/Rp3/2004) (SARS-like coronavirus Rp3).
Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae;
Orthocoronavirinae; Betacoronavirus; Sarbecovirus.
NCBI_TaxID=349344;
NCBI_TaxID=59479; Rhinolophus ferrumequinum (Greater horseshoe bat).
NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
NCBI_TaxID=188571; Rhinolophus pearsonii.
NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16195424; DOI=10.1126/science.1118391;
Li W., Shi Z., Yu M., Ren W., Smith C., Epstein J.H., Wang H., Crameri G.,
Hu Z., Zhang H., Zhang J., McEachern J., Field H., Daszak P., Eaton B.T.,
Zhang S., Wang L.F.;
"Bats are natural reservoirs of SARS-like coronaviruses.";
Science 310:676-679(2005).
-!- 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 (By similarity). {ECO:0000250}.
-!- FUNCTION: [3C-like proteinase]: 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:
Reaction=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.; EC=3.4.22.69;
-!- CATALYTIC ACTIVITY:
Reaction=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).; EC=3.4.19.12;
-!- 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=P0C6T7-1; Sequence=Displayed;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W6-1; Sequence=External;
-!- 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}.
-!- MISCELLANEOUS: Bat coronavirus rp3 is highly similar to SARS-CoV (SARS-
like).
-!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
conventional translation.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; DQ071615; AAZ67050.1; -; Genomic_RNA.
SMR; P0C6T7; -.
MEROPS; C16.009; -.
PRIDE; P0C6T7; -.
Proteomes; UP000006570; 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; 2.30.30.590; -; 1.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 2.40.10.290; -; 1.
Gene3D; 3.10.20.350; -; 1.
Gene3D; 3.40.220.20; -; 1.
Gene3D; 3.40.50.11020; -; 1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR042570; NAR_sf.
InterPro; IPR021590; NSP1.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR038030; NSP1_sf.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR038400; Nsp3_coronavir_sf.
InterPro; IPR022733; Nsp3_PL2pro.
InterPro; IPR038166; Nsp3_PL2pro_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; R1a/1ab.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR024358; SARS-CoV_Nsp3_N.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF12379; DUF3655; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF11501; Nsp1; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF12124; Nsp3_PL2pro; 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; SSF160099; SSF160099; 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; 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..4380
/note="Replicase polyprotein 1a"
/id="PRO_0000338122"
CHAIN 1..179
/note="Non-structural protein 1"
/evidence="ECO:0000250"
/id="PRO_0000338123"
CHAIN 180..818
/note="Non-structural protein 2"
/evidence="ECO:0000250"
/id="PRO_0000338124"
CHAIN 819..2738
/note="Non-structural protein 3"
/evidence="ECO:0000250"
/id="PRO_0000338125"
CHAIN 2739..3238
/note="Non-structural protein 4"
/evidence="ECO:0000250"
/id="PRO_0000338126"
CHAIN 3239..3544
/note="3C-like proteinase"
/evidence="ECO:0000250"
/id="PRO_0000338127"
CHAIN 3545..3834
/note="Non-structural protein 6"
/evidence="ECO:0000250"
/id="PRO_0000338128"
CHAIN 3835..3917
/note="Non-structural protein 7"
/evidence="ECO:0000250"
/id="PRO_0000338129"
CHAIN 3918..4115
/note="Non-structural protein 8"
/evidence="ECO:0000250"
/id="PRO_0000338130"
CHAIN 4116..4228
/note="Non-structural protein 9"
/evidence="ECO:0000250"
/id="PRO_0000338131"
CHAIN 4229..4367
/note="Non-structural protein 10"
/evidence="ECO:0000250"
/id="PRO_0000338132"
CHAIN 4368..4380
/note="Non-structural protein 11"
/evidence="ECO:0000255"
/id="PRO_0000338133"
TRANSMEM 2201..2221
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2312..2334
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2349..2369
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2753..2773
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3020..3040
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3059..3079
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3081..3101
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3103..3123
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3140..3160
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3562..3582
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3584..3604
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3610..3630
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3657..3676
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3683..3702
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3726..3746
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3754..3774
/note="Helical"
/evidence="ECO:0000255"
DOMAIN 1001..1167
/note="Macro"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
DOMAIN 1609..1873
/note="Peptidase C16"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
DOMAIN 3239..3544
/note="Peptidase C30"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
ZN_FING 1727..1764
/note="C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ZN_FING 4302..4318
/evidence="ECO:0000250"
ZN_FING 4345..4358
/evidence="ECO:0000250"
REGION 2201..2369
/note="HD1"
/evidence="ECO:0000250"
REGION 2753..3160
/note="HD2"
/evidence="ECO:0000250"
REGION 3562..3774
/note="HD3"
/evidence="ECO:0000250"
COMPBIAS 930..999
/note="Glu-rich"
COMPBIAS 2208..2211
/note="Poly-Leu"
COMPBIAS 3764..3767
/note="Poly-Cys"
ACT_SITE 1649
/note="For PL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ACT_SITE 1810
/note="For PL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ACT_SITE 3279
/note="For 3CL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
ACT_SITE 3383
/note="For 3CL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
SITE 179..180
/note="Cleavage"
/evidence="ECO:0000250"
SITE 818..819
/note="Cleavage; by PL-PRO"
/evidence="ECO:0000250"
SITE 3238..3239
/note="Cleavage; by PL-PRO"
/evidence="ECO:0000250"
SITE 3544..3545
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3834..3835
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3917..3918
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4115..4116
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4228..4229
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4367..4368
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SEQUENCE 4380 AA; 486337 MW; 0DDA57CD3DF1535B CRC64;
MESLVLGINE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKSGT CGIVELEKGV
LPQPEQPYVF IKRSDAQGTD HGHRVRELVA ELDGVQYGRS GITLGVLVPH VGETPIAYRN
VLLRKNGNKG AGGHSFGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGVL RELTRELNGG
ALTRYVDNNF CGPDGYPLEC IKDLLARAGK SMCTLSEQLD YIESKRGVYC CRDHGHEIAW
FTERSDKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV SEGPNTCGYL
PTNAVVKMPC PACQDPEIGP EHSAADYHNH SNIETRLRKG GRTRCFGGCV FAYVGCYNKR
AYWVPRASAD IGSGHTGITG DNVETLNEDL LEILSRERVN INIVGDFQLN EEVAIILASF
SASTSAFIDT IKSLDYKSFK TIVESCGNYK VTKGKPIKGA WNIGQHRSVL TPLCGFPSQA
AGVIRSIFSR TLDAANHSIP DLQRAAVTIL DSISEQSLRL VDAMVYTSNL LTNSVIIMAY
VTGGLVQQTS QWLSNLLDTT VEKLRPIFAW IEAKLSAGVE FLKDAWEILK FLITGVFDIV
KGQIQVASDN IKDCVKCFVD VVNKALEMCI DQVTIAGAKL RSLNLGEVFI AQSKGLYRQC
IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV LTSEEVVLKN GELEALETPV DSFTNGAVVG
TPVCINGLML LEIKANEQYC ALSPGLLATN NVFRLKGGAP TKGVTFGEDT VVEVQGYKNV
RITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
WSVATFYLFD DSGEEKLSSR MYCSFYPPDE EEDCEEYEEE EEVSERTCEH EYGTEEDYKG
LPLEFGASTD IIQVEEQEEE DWLDDAVEAE PEPEPLHEEP VNQLTGYLKL TDNVAIKCVD
IVEEAQNANP MVIVNAANIH LKHGGGVAGA LNKATNGAMQ KESDHYIKLN GPLTVGGSCL
LSGHNLAKKC LHVVGPNLNA GEDIQLLKAA YENFNSQDIL LAPLLSAGIF GAKPLQSLQM
CVQTVRTQVY IVVNDKVLYE QVVMDYLDSL KPKVEAPKQE VLPKAEYPKV DEKSVVQKTI
DVKPKIKACI DEVTTTLEET KFLTNKLLLF TDINGKLYQD SKNMLRGEDM SFLEKDAPYM
VGDVITSGDI TCVVIPSKKA GGTTEMLSRA LKKVPINEYI TTYPGQGCAG YTLEEAKTAL
KKCKSAFYVL PSETPNAKEE ILGTVSWNLR EMLAHAEETR KLMPVCMDVR AIMATIQRKY
KGIKIQEGIV DYGVRFFFYT SKEPVASIIT KLNSLNEPLV TMPIGYVTHG FNLEEAARCM
RSLKAPAIVS VSSPDAVTTY NGYLTSSSKT SEDHFVETVS LAGSYRDWSY SGQRTELGVE
FLKRGEKIVY HTLESPVKFH LDGEVLPLDK LKSLLSLREV KTIKVFTTVD NTNLHTQLVD
MSMTYGQQLG PTYLEGADVT KIKPHVNHEG KTFFVLPSDD TLRSEAFEYY HTLDESFLGR
YMSALNHTKK WKFPQVGGLT SIKWADNNCY LSSVLLALQQ IEVKFNAPAL QEAYYRARAG
DAANFCALIL AYSNKTVGEL GDVRETMTHL LQHANLESAK RVLNVVCKHC GQKTTTLTGV
EAVMYMGTLS YDNLKMGVSI PCVCGRDATQ YLVQQESSFV MMSAPPAEYK LQQGTFLCAN
EYTGNYQCGH YTHITAKETL YRIDGAHLTK MSEYKGPVTD VFYKETSYTT TIKPVSYKLD
GVTYTEIEPK LDGYYKKDNA YYTEQPIDLI PTQPLPNASF DNFKLTCSNT KFADDLNQMT
GFTKPASREL SVTFFPDLNG DVVAIDYRHY SASFKKGAKL LHKPIVWHIN QATTKTTFKP
NTWCLRCLWS TKPVDTSNSF EVLAVEDTQG MDNLACESQQ PTPEEVVENP TIQKEVIECD
VKTTEVVGNV ILKPSDEGVK VTQELDHEDL MAAYVENTSI TIKKPNELSL ALGLKTIATH
GIAAINSVPW GKILAYVKPF LGQAAVTTSN CAKRLVQRMF NNYMPYVLTL LFQLCTFTKS
TNSRIRASLP TTIAKNSVRG IVRLCLDAGI NYVKSPKFSK LFTIAMWLLL LSICLGSLIY
VTAALGVLLS NFGAPSYCSG VRESYLNSSN VTTMDFCEGS FPCSVCLSGL DSLDSYPALE
TIQVTISSYK LDLTILGLAA EWFFAYMLFT KFFYLLGLSA IMQVFFGYFA SHFISNSWLM
WFIISIVQMA PVSAMVRMYI FFASFYYIWK SYVHIMDGCT SSTCMMCYKR NRATRVECTT
IVNGMKRSFY VYANGGRGFC KTHNWNCLNC DTFCAGSTFI SDEVARDLSL QFKRPINPTD
QSSYVVDSVA VKNGALHLYF DKAGQKTYER HPLSHFVNLD NLRANNTKGS LPINVIVFDG
KSKCDESAAK SASVYYSQLM CQPILLLDQA LVSDVGDSTE VSVKMFDAYV DTFSATFSVP
MEKLKALVAT AHSELAKGVA LDGVLSTFVS ASRQGVVDTD VDTKDVIECL KLSHHSDLEV
TGDSCNNFML TYNKVENMTP RDLGACIDCN ARHINAQVAR SHNVSLIWNV KDYMSLSEQL
RKQIRSAAKK NNIPFRLTCA TTRQVVNVIT TKISLKGGKI VSTWFKIMLK ATLLCVLAAL
VCYIVMPVHI LSVHGGYTNE IIGYKAIQDG VTRDIVSTDD CFANKHAGFD SWFSQRGGSY
KNDKSCPVVA AIITREIGFI VPGLPGTVLR AINGDFLHFL PRVFSAVGNI CYTPSKLIEY
SDFSTSACVL AAECTIFKDA MGKPVPYCYD TNLLEGSISY SELRPDTRYV LMDGSIIQFP
NAYLEGSVRV VTTFDAEYCR HGTCERSEAG ICLSTSGRWV LNNEHYRALP GVFCGVDAMN
LIANIFTPLV QPVGALDVSA SVVAGGIIAI LVTCAAYYFM KFRRAFGEYN HVVAANAPLF
LMSFTILCLA PAYSFLPGVY SVFYLYLTFY FTNDVSFLAH LQWFAMFSPI VPFWITAIYV
FCISLKHFHW FFNNYLRKRV VFNGVTFSTF EEAALCTFLL NKEMYLKLRS ETLLPLTQYN
RYLALYNKYK YFSGALDTTS YREAACCHLA KALNDFSNSG ADVLYQPPQT SITSAVLQSG
FRKMAFPSGK VEGCMVQVTC GTTTLNGLWL DDTVYCPRHV ICTAEDMLNP NYEDLLIRKS
NHSFLVQAGN VQLRVIGHSM QNCLLRLKVD TSNPKTPKYK FVRIQPGQTF SVLACYNGSP
SGVYQCAMRP NHTIKGSFLN GSCGSVGFNI DYDCVSFCYM HHMELPTEVH AGTDLEGKFY
GPFVDRQTAQ AAGTDTTITL NVLAWLYAAV INGDRWFLNR FTTTLNDFNL VAMKYNYEPL
TQDHVDILGP LSAQTGIAVL DMCAALKELL QNGMNGRTIL GSTILEDEFT PFDVVRQCSG
VTFQGKFKRI VKGTHHWMLL TFLTSLLILV QSTQWSLFFF VYENAFLPFT LGIMAVAACA
MLLVKHKHAF LCLFLLPSLA TVAYFNMVYM PASWVMRIMT WLELADTSLS GYRLKDCVMY
ASALVLLVLM TARTVYDDAA RRVWTLMNVI TLVYKVYYGN ALDQAISMWA LVISVTSNYS
GVVTTIMFLA RAIVFVCVEY YPLLFITGNT LQCIMLVYCF LGYCCCCYFG LFCLLNRYFR
LTLGVYDYLV STQEFRYMNS QGLLPPKSSI DAFKLNIKLL GIGGKPCIKV ATVQSKMSDV
KCTSVVLLSV LQQLRVESSS KLWAQCVQLH NDILLAKDTT EAFEKMVSLL SVLLSMQGAV
DINKLCEEML DNRATLQAIA SEFSSLPSYA AYATAQEAYE QAVANGDSEV VLKKLKKSLN
VAKSEFDRNA AMQRKLEKMA DQAMTQMYKQ ARSEDKRAKV TSAMQTMLFT MLRKLDNDAL
NNIINNARDG CVPLNIIPLT TAAKLMVVVP DYGTYKNTCD GNTFTYASAL WEIQQVVDAD
SKIVQLSEIN MENSSNLAWP LIVTALRANS AVKLQNNELS PVALRQMSCA AGTTQTACTD
DNALAYYNNS KGGRFVLALL SDHQDLKWAR FPKSDGTGTI YTELEPPCRF VTDTPKGPKV
KYLHFIKGLN NLNRGMVLGS LAATVRLQAG NATEVPANST VLSFCAFAVD PAKAYKDYLA
SGGQPITNCV KMLCTHTGTG QAITVTPEAN MDQESFGGAS CCLYCRCHID HPNPKGFCDL
KGKYVQIPTT CANDPVGFTL RNTVCTVCGM WKGYGCSCDQ LREPMMQSAD ASTFLNGFAV


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