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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_BCHK4               Reviewed;        4434 AA.
P0C6T4; A3EX93;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
05-DEC-2018, entry version 74.
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 HKU4 (BtCoV) (BtCoV/HKU4/2004).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=694007;
NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU4-1;
PubMed=17121802; DOI=10.1128/JVI.02182-06;
Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R.,
Wong B.H.L., Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F.,
Chan K.-H., Zheng B.-J., Yuen K.-Y.;
"Comparative analysis of twelve genomes of three novel group 2c and
group 2d coronaviruses reveals unique group and subgroup features.";
J. Virol. 81:1574-1585(2007).
-!- 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:
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=P0C6T4-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W3-1; 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; EF065505; -; NOT_ANNOTATED_CDS; Genomic_RNA.
PDB; 2YNA; X-ray; 1.50 A; A/B=3292-3597.
PDB; 2YNB; X-ray; 1.96 A; A/B=3292-3597.
PDBsum; 2YNA; -.
PDBsum; 2YNB; -.
ProteinModelPortal; P0C6T4; -.
SMR; P0C6T4; -.
PRIDE; P0C6T4; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006574; 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; IPR039658; Macro_domain_protein.
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.
PANTHER; PTHR11106; PTHR11106; 1.
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.
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 4434 Replicase polyprotein 1a.
/FTId=PRO_0000338086.
CHAIN 1 195 Non-structural protein 1. {ECO:0000255}.
/FTId=PRO_0000338087.
CHAIN 196 847 Non-structural protein 2. {ECO:0000255}.
/FTId=PRO_0000338088.
CHAIN 848 2784 Non-structural protein 3. {ECO:0000255}.
/FTId=PRO_0000338089.
CHAIN 2785 3291 Non-structural protein 4. {ECO:0000255}.
/FTId=PRO_0000338090.
CHAIN 3292 3597 3C-like proteinase. {ECO:0000255}.
/FTId=PRO_0000338091.
CHAIN 3598 3889 Non-structural protein 6. {ECO:0000255}.
/FTId=PRO_0000338092.
CHAIN 3890 3972 Non-structural protein 7. {ECO:0000255}.
/FTId=PRO_0000338093.
CHAIN 3973 4171 Non-structural protein 8. {ECO:0000255}.
/FTId=PRO_0000338094.
CHAIN 4172 4281 Non-structural protein 9. {ECO:0000255}.
/FTId=PRO_0000338095.
CHAIN 4281 4434 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338097.
CHAIN 4282 4420 Non-structural protein 10. {ECO:0000255}.
/FTId=PRO_0000338096.
TRANSMEM 2145 2165 Helical. {ECO:0000255}.
TRANSMEM 2222 2242 Helical. {ECO:0000255}.
TRANSMEM 2326 2346 Helical. {ECO:0000255}.
TRANSMEM 2350 2370 Helical. {ECO:0000255}.
TRANSMEM 2375 2395 Helical. {ECO:0000255}.
TRANSMEM 2800 2820 Helical. {ECO:0000255}.
TRANSMEM 3072 3092 Helical. {ECO:0000255}.
TRANSMEM 3105 3125 Helical. {ECO:0000255}.
TRANSMEM 3149 3169 Helical. {ECO:0000255}.
TRANSMEM 3603 3623 Helical. {ECO:0000255}.
TRANSMEM 3637 3657 Helical. {ECO:0000255}.
TRANSMEM 3662 3682 Helical. {ECO:0000255}.
TRANSMEM 3707 3727 Helical. {ECO:0000255}.
TRANSMEM 3735 3755 Helical. {ECO:0000255}.
TRANSMEM 3784 3804 Helical. {ECO:0000255}.
TRANSMEM 3808 3828 Helical. {ECO:0000255}.
DOMAIN 1152 1321 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1593 1864 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3292 3597 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1714 1751 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4355 4371 {ECO:0000250}.
ZN_FING 4397 4410 {ECO:0000250}.
REGION 2112 2395 HD1. {ECO:0000250}.
REGION 2800 3169 HD2. {ECO:0000250}.
REGION 3603 3828 HD3. {ECO:0000250}.
COMPBIAS 960 1049 Glu-rich.
COMPBIAS 4161 4166 Poly-Ser.
ACT_SITE 1634 1634 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1800 1800 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3332 3332 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3439 3439 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 2784 2785 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 3291 3292 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3597 3598 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3889 3890 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3972 3973 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4171 4172 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4281 4282 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4420 4421 Cleavage; by 3CL-PRO. {ECO:0000255}.
HELIX 3302 3305 {ECO:0000244|PDB:2YNA}.
STRAND 3308 3313 {ECO:0000244|PDB:2YNA}.
STRAND 3316 3323 {ECO:0000244|PDB:2YNA}.
STRAND 3326 3330 {ECO:0000244|PDB:2YNA}.
HELIX 3331 3334 {ECO:0000244|PDB:2YNA}.
HELIX 3337 3339 {ECO:0000244|PDB:2YNA}.
HELIX 3345 3350 {ECO:0000244|PDB:2YNA}.
HELIX 3354 3356 {ECO:0000244|PDB:2YNA}.
STRAND 3358 3360 {ECO:0000244|PDB:2YNA}.
STRAND 3363 3365 {ECO:0000244|PDB:2YNA}.
STRAND 3367 3369 {ECO:0000244|PDB:2YNB}.
STRAND 3371 3377 {ECO:0000244|PDB:2YNA}.
STRAND 3380 3387 {ECO:0000244|PDB:2YNA}.
STRAND 3394 3397 {ECO:0000244|PDB:2YNA}.
STRAND 3405 3412 {ECO:0000244|PDB:2YNA}.
STRAND 3415 3423 {ECO:0000244|PDB:2YNA}.
STRAND 3442 3447 {ECO:0000244|PDB:2YNA}.
STRAND 3450 3462 {ECO:0000244|PDB:2YNA}.
STRAND 3465 3469 {ECO:0000244|PDB:2YNA}.
HELIX 3476 3478 {ECO:0000244|PDB:2YNA}.
STRAND 3481 3484 {ECO:0000244|PDB:2YNA}.
HELIX 3495 3507 {ECO:0000244|PDB:2YNA}.
HELIX 3521 3530 {ECO:0000244|PDB:2YNA}.
HELIX 3540 3549 {ECO:0000244|PDB:2YNA}.
HELIX 3553 3565 {ECO:0000244|PDB:2YNA}.
STRAND 3575 3577 {ECO:0000244|PDB:2YNA}.
HELIX 3584 3591 {ECO:0000244|PDB:2YNA}.
SEQUENCE 4434 AA; 491823 MW; 942E92FE623EFBCD CRC64;
MLSKASVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTDD MACKLTPWFE DGETAFNQVS
SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS KHFLVNQLAY KDQVGAAMMR
TTLNAKPLGM FFPYDSSLET GEYTFLLRKN GLGGQLFRER PWDRKETPYV EILDDLEADP
TGKYSQNLLK KLIGGDCIPI DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS
DRFIVLNKKL YRVVWNVTRR NVPYPKQTAF TIVSVVQCDD KDSVPEHTFT IGSQILMVSP
LKATNNKNFN LKQRLLYTFY GKDAVQQPGY IYHSAYVDCN ACGRGTWCTG NAIQGFACDC
GANYSANDVD LQSSGLVPRN ALFLANCPCA NNGACSHSAA QVYNILDGKA CVEVGGKSFT
LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR IGDAIFTGCT GTWDKVVETA NLFLEKAQRS
LNFCQQFALT EVVLAILSGT TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI
NIGANGVCNA TINAPFIAFT GLGESFKKVS AIPWKICSNL KSALDYYSSN IMFRVFPYDI
PCDVSNFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SSACQTALSS FLNACVAASR
ATAGFINDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ QVLDIMSKAM KLLHTNVSWA
GTKLSAIIYE GREALLFNSG TYFCLSTKAK TLQGQMNLVL PGDYNKKTLG ILDPVPNADT
IDVNANSTVV DVVHGQLEPT NEHGPSMIVG NYVLVSDKLF VRTEDEEFYP LCTNGKVVST
LFRLKGGMPS KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN MTFSINPVED
VEEVEEFIED DYLSDELPIA DDEEAWARAV EEVMPLDDIL VAEIELEEDP PLETALESVE
AEVVETAEAQ EPSVESIDST PSTSTVVGEN DLSVKPMSRV AETDDVLELE TAVVGGPVSD
VTAIVTNDIV SVEQAQQCGV SSLPIQDEAS ENQVHQVSDL QGNELLCSET KVEIVQPRQD
LKPRRSRKSK VDLSKYKHTV INNSVTLVLG DAIQIASLLP KCILVNAANR HLKHGGGIAG
VINKASGGDV QEESDEYISN NGPLHVGDSV LLKGHGLADA ILHVVGPDAR NNEDAALLKR
CYKAFNKHTI VVTPLISAGI FSVDPKVSFE YLLANVTTTT YVVVNNEDIY NTLATPSKPD
GLVYSFEGWR GTVRTAKNYG FTCFICTEYS ANVKFLRTKG VDTTKKIQTV DGVSYYLYSA
RDALTDVIAA ANGCSGICAM PFGYVTHGLD LAQSGNYVRQ VKVPYVCLLA SKEQIPIMNS
DVAIQTPETA FINNVTSNGG YHSWHLVSGD LIVKDVCYKK LLHWSGQTIC YADNKFYVVK
NDVALPFSDL EACRAYLTSR AAQQVNIEVL VTIDGVNFRT VILNDTTTFR KQLGATFYKG
VDISDAFPTV KMGGESLFVA DNLSESEKVV LKEYYGTSDV TFLQRYYSLQ PLVQQWKFVV
HDGVKSLKLS NYNCYINATI MMIDMLHDIK FVVPALQNAY LRYKGGDPYD FLALIMAYGD
CTFDNPDDEA KLLHTLLAKA ELTVSAKMVW REWCTVCGIR DIEYTGMRAC VYAGVNSMEE
LQSVFNETCV CGSVKHRQLV EHSAPWLLVS GLNEVKVSTS TDPIYRAFNV FQGVETSVGH
YVHIRVKDGL FYKYDSGSLT KTSDMKCKMT SVWYPTVRYT ADCNVVVYDL DGVTKVEVNP
DLSNYYMKDG KYYTSKPTIK YSPATILPGS VYSNSCLVGV DGTPGSDTIS KFFNDLLGFD
ETKPISKKLT YSLLPNEDGD VLLSEFSNYN PVYKKGVMLK GKPILWVNNG VCDSALNKPN
RASLRQLYDV APIVLDNKYT VLQDNTSQLV EHNVPVVDDV PITTRKLIEV KCKGLNKPFV
KGNFSFVNDP NGVTVVDTLG LTELRALYVD INTRYIVLRD NNWSSLFKLH TVESGDLQIV
AAGGSVTRRA RVLLGASSLF ASFAKITVTA TTAACKTAGR GFCKFVVNYG VLQNMFVFLK
MLFFLPFNYL WPKKQPTVDI GVSGLRTAGI VTTNIVKQCG TAAYYMLLGK FKRVDWKATL
RLFLLLCTTI LLLSSIYHLV LFNQVLSSDV MLEDATGILA IYKEVRSYLG IRTLCDGLVV
EYRNTSFDVM EFCSNRSVLC QWCLIGQDSL TRYSALQMLQ THITSYVLNI DWIWFALEFF
LAYVLYTSSF NVLLLVVTAQ YFFAYTSAFV NWRAYNYIVS GLFFLVTHIP LHGLVRVYNF
LACLWFLRKF YSHVINGCKD TACLLCYKRN RLTRVEASTI VCGTKRTFYI AANGGTSYCC
KHNWNCVECD TAGVGNTFIC TEVANDLTTT LRRLIKPTDQ SHYYVDSVVV KDAVVELHYN
RDGSSCYERY PLCYFTNLEK LKFKEVCKTP TGIPEHNFLI YDTNDRGQEN LARSACVYYS
QVLCKPMLLV DVNLVTTVGD SREIAIKMLD SFINSFISLF SVSRDKLEKL INTARDCVRR
GDDFQNVLKT FTDAARGHAG VESDVETTMV VDALQYAHKN DIQLTTECYN NYVPGYIKPD
SINTLDLGCL IDLKAASVNQ TSMRNANGAC VWNSGDYMKL SDSFKRQIRI ACRKCNIPFR
LTTSKLRAAD NILSVKFSAT KIVGGAPSWL LRVRDLTVKG YCILTLFVFT VAVLSWFCLP
SYSIATVNFN DDRILTYKVI ENGIVRDIAP NDVCFANKYG HFSKWFNENH GGVYRNSMDC
PITIAVIAGV AGARVANVPA NLAWVGKQIV LFVSRVFANT NVCFTPINEI PYDTFSDSGC
VLSSECTLFR DAEGNLNPFC YDPTVLPGAS SYADMKPHVR YDMYDSDMYI KFPEVIVEST
LRITKTLATQ YCRFGSCEES AAGVCISTNG SWALYNQNYS TRPGIYCGDD YFDIVRRLAI
SLFQPVTYFQ LSTSLAMGLV LCVFLTAAFY YINKVKRALA DYTQCAVVAV VAALLNSLCL
CFIVANPLLV APYTAMYYYA TFYLTGEPAF IMHISWYVMF GAVVPIWMLA SYTVGVMLRH
LFWVLAYFSK KHVDVFTDGK LNCSFQDAAS NIFVIGKDTY VALRNAITQD SFVRYLSLFN
KYKYYSGAMD TASYREACAA HLCKALQTYS ETGSDILYQP PNCSVTSSVL QSGLVKMSAP
SGAVENCIVQ VTCGSMTLNG LWLDNTVWCP RHIMCPADQL TDPNYDALLI SKTNHSFIVQ
KHIGAQANLR VVAHSMVGVL LKLTVDVANP STPAYTFSTV KPGASFSVLA CYNGKPTGVF
TVNLRHNSTI KGSFLCGSCG SVGYTENGGV INFVYMHQME LSNGTHTGSS FDGVMYGAFE
DKQTHQLQLT DKYCTINVVA WLYAAVLNGC KWFVKPTRVG IVTYNEWALS NQFTEFVGTQ
SIDMLAHRTG VSVEQMLAAI QSLHAGFQGK TILGQSTLED EFTPDDVNMQ VMGVVMQSGV
KRISYGFIHW LISTFVLAYV SVMQLTKFTM WTYLFETIPT QMTPLLLGFM ACVMFTVKHK
HTFMSLFLLP VALCLTYANI VYEPQTLISS TLIAVANWLT PTSVYMRTTH FDFGLYISLS
FVLAIIVRRL YRPSMSNLAL ALCSGVMWFY TYVIGDHSSP ITYLMFITTL TSDYTITVFA
TVNLAKFISG LVFFYAPHLG FILPEVKLVL LIYLGLGYMC TMYFGVFSLL NLKLRVPLGV
YDYSVSTQEF RFLTGNGLHA PRNSWEALIL NFKLLGIGGT PCIKVATVQS KLTDLKCTSV
VLLTVLQQLH LESNSKAWSY CVKLHNEILA AVDPTEAFER FVCLFATLMS FSANVDLDAL
ANDLFENSSV LQATLTEFSH LATYAELETA QSSYQKALNS GDASPQVLKA LQKAVNVAKN
AYEKDKAVAR KLERMAEQAM TSMYKQARAE DKKAKIVSAM QTMLFGMIKK LDNDVLNGVI
ANARNGCVPL SIVPLCASNK LRVVIPDISV WNKVVNWPSV SYAGSLWDIT VINNVDNEVV
KPTDVVETNE SLTWPLVIEC SRSSSSAVKL QNNEIHPKGL KTMVITAGVD QVNCNSSAVA
YYEPVQGHRM VMGLLSENAH LKWAKVEGKD GFINIELQPP CKFLIAGPKG PEIRYLYFVK
NLNNLHRGQL LGHIAATVRL QAGANTEFAS NSTVLTLVAF AVDPAKAYLD YVGSGGTPLS
NYVKMLAPKT GTGVAISVKP EATADQETYG GASVCLYCRA HIEHPDVSGV CKYKTRFVQI
PAHVRDPVGF LLKNVPCNVC QYWVGYGCNC DALRNNTVPQ SKDTNFLNES GVLV


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