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 R1A_BCHK3               Reviewed;        4376 AA.
P0C6F8; Q3LZX2;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
28-MAR-2018, entry version 60.
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 HKU3 (BtCoV) (SARS-like coronavirus HKU3).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=442736;
NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU3-1;
PubMed=16169905; DOI=10.1073/pnas.0506735102;
Lau S.K.P., Woo P.C.Y., Li K.S.M., Huang Y., Tsoi H.-W., Wong B.H.L.,
Wong S.S.Y., Leung S.-Y., Chan K.-H., Yuen K.-Y.;
"Severe acute respiratory syndrome coronavirus-like virus in Chinese
horseshoe bats.";
Proc. Natl. Acad. Sci. U.S.A. 102:14040-14045(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: 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 (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=P0C6F8-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W2-1; 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}.
-!- MISCELLANEOUS: Bat coronavirus HKU3 is highly similar to SARS-CoV
(SARS-like).
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; DQ022305; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; P0C6F8; -.
SMR; P0C6F8; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000007450; 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:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
GO; GO:0016788; F:hydrolase activity, acting on ester bonds; 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; 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; 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; pp1a/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; 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 4376 Replicase polyprotein 1a.
/FTId=PRO_0000338074.
CHAIN 1 179 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338075.
CHAIN 180 818 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338076.
CHAIN 819 2734 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338077.
CHAIN 2735 3234 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338078.
CHAIN 3235 3540 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338079.
CHAIN 3541 3830 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338080.
CHAIN 3831 3913 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338081.
CHAIN 3914 4111 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338082.
CHAIN 4112 4224 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338083.
CHAIN 4225 4363 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338084.
CHAIN 4364 4376 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338085.
TRANSMEM 2197 2217 Helical. {ECO:0000255}.
TRANSMEM 2298 2318 Helical. {ECO:0000255}.
TRANSMEM 2345 2365 Helical. {ECO:0000255}.
TRANSMEM 2744 2764 Helical. {ECO:0000255}.
TRANSMEM 2986 3006 Helical. {ECO:0000255}.
TRANSMEM 3016 3036 Helical. {ECO:0000255}.
TRANSMEM 3048 3068 Helical. {ECO:0000255}.
TRANSMEM 3071 3091 Helical. {ECO:0000255}.
TRANSMEM 3099 3119 Helical. {ECO:0000255}.
TRANSMEM 3136 3156 Helical. {ECO:0000255}.
TRANSMEM 3558 3578 Helical. {ECO:0000255}.
TRANSMEM 3580 3600 Helical. {ECO:0000255}.
TRANSMEM 3606 3626 Helical. {ECO:0000255}.
TRANSMEM 3652 3672 Helical. {ECO:0000255}.
TRANSMEM 3679 3698 Helical. {ECO:0000255}.
TRANSMEM 3722 3742 Helical. {ECO:0000255}.
TRANSMEM 3750 3770 Helical. {ECO:0000255}.
DOMAIN 998 1164 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1605 1869 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3235 3540 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1723 1760 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4298 4314 {ECO:0000250}.
ZN_FING 4341 4354 {ECO:0000250}.
REGION 2086 2365 HD1. {ECO:0000250}.
REGION 2749 3156 HD2. {ECO:0000250}.
REGION 3558 3770 HD3. {ECO:0000250}.
COMPBIAS 930 996 Glu-rich.
COMPBIAS 2204 2207 Poly-Leu.
COMPBIAS 3760 3763 Poly-Cys.
ACT_SITE 1645 1645 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1806 1806 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3275 3275 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3379 3379 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 179 180 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 818 819 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3234 3235 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3540 3541 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3830 3831 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3913 3914 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4111 4112 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4224 4225 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4363 4364 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 4376 AA; 485585 MW; 338874921B682E15 CRC64;
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT CGLVELEKGV
LPQLEQPYVF IKRSDALSTN HGHKVVELVA ELDGIQFGRS GITLGVLVPH VGETPIAYRN
VLLRKNGNKG AGGHSFGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGAL RELTRELNGG
VVTRYVDNNF CGPDGYPLEC IKDFLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW
FTERSEKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV CEGPTTCGYL
PTNAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG GRTKCFGGCV FSYVGCYNKR
AYWVPRASAN IGANHTGITG ENVETLNEDL LEILNRERVN INIVGDFRFN EEVAIILASF
SASPSAFIET VKGLDYKSFK VIVESCGNYK VTNGKPVTGA WNIGQQRSIL TPLCGFPSQA
AGVIRSIFSR TLDAANHSIL DLQRAAVTTL DGISEQSLRL VDAMVYTSDL LTNSVVVMAY
VTGGLVQQTM QWLSNMLGTA VDKLKPVFTW VEAKLSAGVE FLRDAWEILK FLITGVFDVI
KGQIQVATDN IKECVKIFLG VVNKALEMCL DQVTIAGTKL RALNLGEVFI AQSRGLYRQC
IRGKEQLQLL MPLKAPKEVT FLEGDAHDTV LTSEEVVLKS GELEALETPI DSFTSGAVVG
TPVCINGLML LELENKEQYC ALSPGLLATN NVFRLKGGAP VKGVTFGEDT VLEVQGYKNV
KITFELDVRV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTPMGIDLDE
WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEECEDE EETCEHEYGT EDDYKGLPLE
FGASTETPHV EEEEEEEDWL DDAIEAEPEP EPLPEEPVNQ FVGYLKLTDN VAIKCIDIVK
EAQSAKPTVI VNAANTHLKH GGGVAGALNK ATNGAMQNES DEYIRQNGPL TVGGSCLLSG
HNLAEKCLHV VGPNLNAGED VQLLKRAYEN FNSQDVLLAP LLSAGIFGAK PLQSLKMCVE
IVRTQVYLAV NDKSLYDQIV LDYLDSLKPK VESPNKEEEP KLEEPKAVQP VAEKPVDVKP
KIKACIDEVT TTLEETKFLT NKLLLFADIN GKLYQDSQNM LRGEDMSFLE KDAPYIVGDV
ITSGDITCVI IPAKKSGGTT EMLARALKEV PVAEYITTYP GQGCAGYTLE EAKTALKKCK
SAFYVLPSET PNEKEEVLGT VSWNLREMLA HAEETRKLMP ICLDVRAIMA TIQRKYKGIK
VQEGIVDYGV RFFFYTSKEP VASIITKLNS LNEPLVTMPI GYVTHGLNLE EAARCMRSLK
APAVVSVSSP DAVTAYNGYL TSSSKTPEEY FVETTSLAGS YRDWSYSGQR TELGVEFLKR
GDKIVYHTTG SPIEFHLDGE VLPLDKLKSL LSLREVKTIK VFTTVDNTNL HTHIVDMSMT
YGQQFGPTYL DGADVTKIKP HVNHEGKTFF VLPSDDTLRS EAFEYYHTID ESFLGRYMSA
LNHTKKWKFP QVGGLTSIKW ADNNCYLSSV LLALQQVEVK FNAPALQEAY YRARAGDAAN
FCALILAYSN KTVGELGDVR ETMTHLLQHA NLESAKRVLN VVCKHCGQKT TTLKGVEAVM
YMGTLSYDEL KTGVSIPCVC GRNATQYLVQ QESSFVMMSA PPAEYKLQQG AFLCANEYTG
NYQCGHYTHI TAKETLYRVD GAHLTKMSEY KGPVTDVFYK ETSYTTAIKP VSYKLDGVTY
TEIEPKLDGY YKKGNAYYTE QPIDLVPTQP MPNASFDNFK LTCSNTKFAD DLNQMTGFKK
PASRELTVTF FPDLNGDVVA IDYRHYSTSF KKGAKLVHKP ILWHINQTTN KTTYKPNIWC
LRCLWSTKPV DTSNSFEVLV VEDTQGMDNL ACESQTTTSE EVVENPTVQK EIIECDVKTT
EVVGNVILKP SEEGVKVTQE LGHEDLMAAY VEETSITIKK PNELSLALGL KTLATHGAAA
INSVPWSKIL AYVKPFLGQT AVITSNCIKK CVQRVFSNYM PYVITLLFQL CTFTKSTNSR
IKASLPTTIA KNSVKSVAKL CLDVCINYVK SPKFSKLFTI VMWLLLLSIC LGSLTYVTAV
LGVCLSSLGV PSYCDGVREL YINSSNVTTM DFCQGYFPCS VCLSGLDSLD SYPALETIQV
TISSYKLDLT FLGLAAEWLL AYMLFTKFFY LLGLSAIMQA FFGYFASHFI SNSWLMWFII
SIVQMAPVSA MVRMYIFFAS FYYVWKSYVH IMDGCTSSTC MMCYKRNRAT RVECTTIVNG
VKRSFYVYAN GGRGFCKAHN WNCLNCDTFC AGSTFISDEV ARDLSLQFKR PINPTDQSAY
VVDSVTVKNG ALHLYFDKAG QKTYERHPLS HFVNLDNLRA NNTKGSLPIN VIVFDGKSKC
EESAAKSASV YYSQLMCQPI LLLDQALVSD VGDSTEVSVK MFDAYVDTFS ATFSVPMEKL
KALVATAHSE LAKGVALDGV LSTFVSAARQ GVVDTDVDTK DVIECLKLSH HSDIEVTGDS
CNNFMLTYNK VENMTPRDLG ACIDCNARHI NAQVAKSHNV SLVWNVKDYM SLSEQLRKQI
RSAAKKNNIP FRLTCATTRQ VVNVITTKIS LKGGKVVSTW FKLLLKVTLL CVLAALFCYV
IMPVHSLSVH DGYTNEIIGY KAIQDGVTRD IVSTDDCFAN KHAGFDSWFS QRGGSYRNDK
NCPVVAAIIT REIGFIVPGL PGTVLRALNG DFLHFLPRVF SAVGNICYTP SKLIEYSDFA
TSACVLAAEC TIFKDAMGKP VPYCYDTNLL EGSISYSELR PDTRYVLMDG SIIQFPNTYL
EGSVRVVTTF DAEYCRHGTC ERSEVGVCLS TSGRWVLNNE HYRALPGVFC GVDAMNLIAN
IFTPLVQPVG ALDVSASVVA GGIIAILVTC AAYYFMKFRR AFGEYNHVVA ANALLFLMSF
TILCLAPAYS FLPGVYSIFY LYLTFYFTND VSFLAHLQWF AMFSPIVPFW ITAIYVFCIS
LKHFHWFFSN YLKKRVMFNG VTFSTFEEAA LCTFLLNKEM YLRLRSETLL PLTQYNRYLA
LYNKYKYFSG ALDTTSYREA ACCHLAKALN DFSNSGADVL YQPPQTSITS AVLQSGFRKM
AFPSGKVEGC MVQVTCGTTT LNGLWLDDTV YCPRHVVCTA EDMLNPNYDD LLIRKSNHSF
LVQAGNVQLR VIGHSMQNCL LRLKVDTSNP KTPKYKFVRI QPGQTFSVLA CYNGSPSGVY
QCAMRPNHTI KGSFLNGSCG SVGFNIDYDC VSFCYMHHME LPTGVHAGTD LEGKFYGPFV
DRQTAQAAGT DTTITLNVLA WLYAAVINGD RWFLNRFTTT LNDFNLVAMK YNYEPLTQDH
VDILGPLSAQ TGIAVLDMCA ALKELLQNGM NGRTILGSTI LEDEFTPFDV VRQCSGVTFQ
GKFKKIVKGT HHWMLLTFLT SLLILVQSTQ WSLFFFVYEN AFLPFALGIM AVAACAMLLV
KHKHAFLCLF LLPSLATVAY FNMVYMPASW VMRIMTWLEL ADTSLSGYRL KDCVMYASAL
VLLILMTART VYDDAARRVW TLMNVITLVY KVYYGNSLDQ AISMWALVIS VTSNYSGVVT
TIMFLARAIV FVCVEYYPLL FITGNTLQCI MLVYCFLGYC CCCYFGLFCL LNRYFRLTLG
VYDYLVSTQE FRYMNSQGLL PPKSSIDAFK LNIKLLGIGG KPCIKVATVQ SKMSDVKCTS
VVLLSVLQQL RVESSSKLWA QCVQLHNDIL LAKDTTEAFE KMVSLLSVLL SMQGAVDINK
LCEEMLDNRA TLQAIASEFS SLPSYAAYAT AQEAYEQAVS NGDSEVVLKK LKKSLNVAKS
EFDHDAAMQR KLEKMADQAM TQMYKQARSE DKRAKVTSAM QTMLFTMLRK LDNDALNNII
NNARDGCVPL NIIPLTTAAK LMVVVPDYGT YKNTCDGNTF TYASALWEIQ QVVDADSKIV
QLSEINMDNS PNLAWPLIVT ALRANSAVKL QNNELSPVAL RQMSCAAGTT QTACTDDNAL
AYYNNAKGGR FVLALLSDHQ DLKWARFPKS DGTGTIYTEL EPPCRFVTDT PKGPKVKYLY
FIKGLNNLNR GMVLGSLAAT VRLQAGNATE VPANSTVLSF CAFAVDPAKA YKDYLASGGQ
PITNCVKMLC THTGTGQAIT VTPEANMDQE SFGGASCCLY CRCHIDHPNP KGFCDLKGKY
VQIPTTCAND PVGFTLRNTV CTVCGMWKGY GCSCDQLREP MMQSADASTF LNGFAV


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