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 R1A_CVBM                Reviewed;        4383 AA.
P0C6U0; Q66198;
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=p28;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=PL1-PRO/PL2-PRO;
AltName: Full=PL1/PL2;
AltName: Full=Papain-like proteinases 1/2;
AltName: Full=p210;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
AltName: Full=p44;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p27;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p10;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p22;
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=p15;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Bovine coronavirus (strain Mebus) (BCoV) (BCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=11132;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Brian D.A.;
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
[2]
SEQUENCE REVISION.
Brian D.A.;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: The papain-like proteinase 1 (PL1-PRO) and papain-like
proteinase 2 (PL2-PRO) 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. 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=P0C6U0-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W9-1; 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 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; U00735; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; P0C6U0; -.
SMR; P0C6U0; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000007554; 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.
InterPro; IPR022570; B-CoV_NSP1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR036333; NSP10_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; IPR002705; Pept_C30/C16_B_coronavir.
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; PF11963; DUF3477; 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; PF01831; Peptidase_C16; 1.
Pfam; PF05409; Peptidase_C30; 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; 2.
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 4383 Replicase polyprotein 1a.
/FTId=PRO_0000338158.
CHAIN 1 246 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338159.
CHAIN 247 851 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338160.
CHAIN 852 2750 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338161.
CHAIN 2751 3246 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338162.
CHAIN 3247 3549 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338163.
CHAIN 3550 3836 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338164.
CHAIN 3837 3925 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338165.
CHAIN 3926 4122 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338166.
CHAIN 4123 4232 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338167.
CHAIN 4233 4369 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338168.
CHAIN 4370 4383 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338169.
TRANSMEM 2138 2158 Helical. {ECO:0000255}.
TRANSMEM 2199 2219 Helical. {ECO:0000255}.
TRANSMEM 2221 2241 Helical. {ECO:0000255}.
TRANSMEM 2313 2333 Helical. {ECO:0000255}.
TRANSMEM 2343 2363 Helical. {ECO:0000255}.
TRANSMEM 2365 2385 Helical. {ECO:0000255}.
TRANSMEM 2752 2772 Helical. {ECO:0000255}.
TRANSMEM 3031 3051 Helical. {ECO:0000255}.
TRANSMEM 3063 3083 Helical. {ECO:0000255}.
TRANSMEM 3090 3110 Helical. {ECO:0000255}.
TRANSMEM 3115 3135 Helical. {ECO:0000255}.
TRANSMEM 3558 3578 Helical. {ECO:0000255}.
TRANSMEM 3588 3608 Helical. {ECO:0000255}.
TRANSMEM 3615 3635 Helical. {ECO:0000255}.
TRANSMEM 3657 3677 Helical. {ECO:0000255}.
TRANSMEM 3684 3704 Helical. {ECO:0000255}.
TRANSMEM 3711 3731 Helical. {ECO:0000255}.
TRANSMEM 3755 3775 Helical. {ECO:0000255}.
DOMAIN 1036 1274 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1275 1435 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1631 1892 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3247 3549 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1151 1179 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1749 1785 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4306 4322 {ECO:0000250}.
ZN_FING 4348 4361 {ECO:0000250}.
REGION 2138 2385 HD1.
REGION 2752 3135 HD2.
REGION 3558 3775 HD3.
ACT_SITE 1074 1074 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1225 1225 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1671 1671 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1828 1828 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3287 3287 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3391 3391 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 246 247 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 851 852 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2750 2751 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3246 3247 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3549 3550 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3836 3837 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3925 3926 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4122 4123 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4232 4233 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4369 4370 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 4383 AA; 490562 MW; 3B4FBFA0C0C7EE34 CRC64;
MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDIVC STTAQKLETG GICPENHVMV
DCRRLLKQEC CVQSSLIREI VMNTRPYDLE VLLQDALQSR EAVLVTPPLG MSLEACYVRG
CNPNGWTMGL FRRRSVCNTG RCAVNKHVAY QLYMIDPAGV CFGAGQFVGW VIPLAFMPVQ
SRKFIVPWVM YLRKCGEKGA YNKDHKRGGF EHVYNFKVED AYDLVHDEPK GKFSKKAYAL
IRGYRGVKPL LYVDQYGCDY TGGLADGLEA YADKTLQEMK ALFPIWSQEL PFDVTVAWHV
VRDPRYVMRL QSASTIRSVA YVANPTEDLC DGSVVIKEPV HVYADDSIIL RQHNLVDIMS
CFYMEADAVV NAFYGVDLKD CGFVMQFGYI DCEQDLCDFK GWVPGNMIDG FACTTCGHVY
ETGDLLAQSS GVLPVNPVLH TKSAAGYGGF GCKDSFTLYG QTVVYFGGCV YWSPARNIWI
PILKSSVKSY DGLVYTGVVG CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH
KQLLLNRGVY KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA
FCDYAGKICH AVVSKSKELL DVSLDSLGAA IHYLNSKIVD LAQHFSDFGT SFVSKIVHFF
KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA SAVAQAFRSV AKVVLDSLRV
TFIDGLSCFK IGRRRICLSG SKIYEVERGL LHSSQLPLDV YDLTMPSQVQ KTKQKPIYLK
GSGSDFSLAD SVVEVVTTSL TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDGHVG
LLDQAWRVPC AGRCVTFKEQ PTVNEIASTP KTIKVFYELD KDFNTILNTA CGVFEVDDTV
DMEEFYAVVI DAIEEKLSPC KELEGVGAKV SAFLQKLEDN SLFLFDEAGE EVLAPKLYCA
FTAPEDDDFL EESGVEEDDV EGEETDLTVT SAGEPCVASE QEESSEILED TLDDGPCVET
SDSQVEEDVQ MSDFVDLESV IQDYENVCFE FYTTEPEFVK VLDLYVPKAT RNNCWLRSVL
AVMQKLPCQF KDKNLQDLWV LYKQQYSQLF VDTLVNKIPA NIVVPQGGYV ADFAYWFLTL
CDWQCVAYWK CIKCDLALKL KGLDAMFFYG DVVSHVCKCG ESMVLIDVDV PFTAHFALKD
KLFCAFITKR SVYKAACVVD VNDSHSMAVV DGKQIDDHRI TSITSDKFDF IIGHGMSFSM
TTFEIAQLYG SCITPNVCFV KGDIIKVSKR VKAEVVVNPA NGHMAHGGGV AKAIAVAAGQ
QFVKETTDMV KSKGVCATGD CYVSTGGKLC KTVLNVVGPD ARTQGKQSYA LLERVYKHLN
KYDCVVTTLI SAGIFSVPSD VSLTYLLGTA KKQVVLVSNN QEDFDLISKC QITAVEGTKK
LAERLSFNVG RSIVYETDAN KLILSNDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN
VDVVPEGWRV VNKFYQINGV RTVKYFECPG GIDICSQDKV FGYVQQGSFN KATVAQIKAL
FLDKVDILLT VDGVNFTNRF VPVGESFGKS LGNVFCDGVN VTKHKCDINY KGKVFFQFDN
LSSEDLKAVR SSFNFDQKEL LAYYNMLVNC SKWQVVFNGK YFTFKQANNN CFVNVSCLML
QSLNLKFKIV QWQEAWLEFR SGRPARFVSL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG
AICDFEIACK CGVKQEQRTG VDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL
ICSNTPASVK LPKGVGSANI FKGDKVGHYV HVKCEQSYQL YDASNVKKVT DVTGNLSDCL
YLKNLKQTFK SVLTTYYLDD VKKIEYKPDL SQYYCDGGKY YTQRIIKAQF KTFEKVDGVY
TNFKLIGHTV CDILNAKLGF DSSKEFVEYK VTEWPTATGD VVLATDDLYV KRYERGCITF
GKPVIWLSHE QASLNSLTYF NRPLLVDENK FDVLKVDDVD DGGDISESDA KEPKEINIIK
LSGVKKPFKV EDSVIVNDDT SEIKYVKSLS IVDVYDMWLT GCRCVVRTAN ALSRAVNVPT
IRKFIKFGMT LVSIPIDLLN LREIKPVFNV VKAVRNKISA CFNFIKWLFV LLFGWIKISA
DNKVIYTTEV ASKLTCKLVA LAFKNAFLTF KWSVVARGAC IIATIFLLWF NFIYANVIFS
DFYLPKIGFL PTFVGKIAQW IKNTFSLVTI CDLYSIQDVG FKNQYCNGSI ACQFCLAGFD
MLDNYKAIDV VQYEADRRAF VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL
PELFMLSTLH WSVRLLVSLA NMLPAHVFMR FYIIIASFIK LFSLFRHVAY GCSKSGCLFC
YKRNRSLRVK CSTIVGGMIR YYDAMANGGT GFCSKHQWNC IDCDSYKPGN TFITVEAALD
LSKELKRPIQ PTDVAYHTVT DVKQVGCYMR LFYDRDGQRT YDDVNASLFV DYSNLLHSKV
KSVPNMHVVV VENDADKANF LNAAVFYAQS LFRPILMVDK NLITTANTGT SVTETMFDVY
VDTFLSMFDV DKKSLNALIA TAHSSIKQGT QICKVLDTFL SCARKSCSID SDVDTKCLAD
SVMSAVSAGL ELTDESCNNL VPTYLKGDNI VAADLGVLIQ NSAKHVQGNV AKIAGVSCIW
SVDAFNQLSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG AVFSYFVYVC
FVLSLVCFIG LWCLMPTYTV HKSDFQLPVY ASYKVLDNGV IRDVSVEDVC FANKFEQFDQ
WYESTFGLSY YSNSMACPIV VAVVDQDFGS TVFNVPTKVL RYGYHVLHFI THALSADGVQ
CYTPHSQISY SNFYASGCVL SSACTMFAMA DGSPQPYCYT DGLMQNASLY SSLVPHVRYN
LANAKGFIRF PEVLREGLVR IVRTRSMPYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL
PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL IKLKRAFGDY
TSIVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYATL YFPSEISVIM HLQWLVMYGT
IMPLWFCLLY ISVVVSNHAF WVFSYCRQLG TSVRSDGTFE EMALTTFMIT KDSYCKLKNS
LSDVAFNRYL SLYNKYRYYS GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV
STSFLQSGIV KMVNPTSKVE PCIVSVTYGN MTLNGLWLGD KVYCPRHVIC SASDMTNPDY
TNLLCRVTSS DFTVLFDRLS LTVMSYQMQG CMLVLTVTLQ NSRTPKYTFG VVKPGETFTV
LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVVYVIMG DCVKFVYMHQ LELSTGCHTG
TDFNGDFYGP YKDAQVVQLP VQDYIQSVNF VAWLYAAILN NCNWFVQSDK CSVEDFNVWA
LSNGFSQVKS DLVIDALASM TGVSLETLLA AIKHLKNGFQ GRQIMGSCSF EDELTPSDVY
QQLAGIKLQS KRTRLVKGIV CWIMASTFLF SCIITAFVKW TMFMYVTTNM LSITFCALCV
ISLTMLLVKH KHLYLTMYII PVLFTLLYNN YLVVYKQTFR GYVYAWLSYY VPSVEYTYTD
EVIYGMLLLI GMVFVTLRSI NQYLFSFIMF VGRVISVVSL WYMGSNLEEE ILLMLASLFG
TYTWTTALSM AAAKVIAKWV AVNVLYFTDI PQIKIVLVCY LFIGYIISCY WGLFSLMNSL
FRMPLGVYNY KISVQELRYM NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT
DVKCANVVLL NCLQHLHVAS NSKLWQYCST LHNEILATSD LGVAFEKLAQ LLIVLFANPA
AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA CSSGSANQQQ
LKQLEKACNI AKSAYERDRA VARKLERMAD LALTNMYKEA RINDKKSKVV SALQTMLFSM
VRKLDNQALN SILDNAVKGC VPLNAIPSLA ANTLTIIVPD KSVYDQVVDN VYVTYAGNVW
QIQTIQDSDG TNKQLHEISD DCNWPLVIIA NRHNEVSATA LQNNELMPAK LKTQVVNSGP
DQTCNTPTQC YYNNSYNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDVK
GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA FSVDPKKTYL
DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTSQDSY GGASVCIYCR ARVEHPDVDG
LCKLRGKFVQ VPVGIKDPVS YVLTHDVCQV CGFWRDGSCS CVSTDTTVQS KDTNFLNGFG
VRV


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