ID A0A7D4WTF8_9ALPC Unreviewed; 4117 AA. AC A0A7D4WTF8; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 28-JUN-2023, entry version 12. DE SubName: Full=Polyprotein 1a {ECO:0000313|EMBL:QKV43822.1}; GN Name=ORF1a {ECO:0000313|EMBL:QKV43822.1}; OS Porcine epidemic diarrhea virus. OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; OC Alphacoronavirus; Pedacovirus. OX NCBI_TaxID=28295 {ECO:0000313|EMBL:QKV43822.1}; RN [1] {ECO:0000313|EMBL:QKV43822.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEDV-2118-1-Orense-Covelas {ECO:0000313|EMBL:QKV43822.1}; RA de Nova P.J., Cortey M., Diaz I., Rubio P., Martin M., Carvajal A.; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QKV43822.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEDV-2118-1-Orense-Covelas {ECO:0000313|EMBL:QKV43822.1}; RX PubMed=32511876; RA de Nova P.J.G., Cortey M., Diaz I., Puente H., Rubio P., Martin M., RA Carvajal A.; RT "A retrospective study of porcine epidemic diarrhoea virus (PEDV) reveals RT the presence of swine enteric coronavirus (SeCoV) since 1993 and the recent RT introduction of a recombinant PEDV-SeCoV in Spain."; RL Transbound. Emerg. Dis. 0:0-0(2020). CC -!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity to the CC polymerase, maybe by binding to dsRNA or by producing primers utilized CC by the latter. {ECO:0000256|ARBA:ARBA00002928}. CC -!- FUNCTION: Nsp9 is a ssRNA-binding protein. CC {ECO:0000256|ARBA:ARBA00003140}. CC -!- FUNCTION: The papain-like proteinase 1 (PLP1) and papain-like CC proteinase 2 (PLP2) are responsible for the cleavages located at the N- CC terminus of the replicase polyprotein. In addition, PLP2 possesses a CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and CC 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 CC also antagonizes innate immune induction of type I interferon by CC blocking the nuclear translocation of host IRF-3. CC {ECO:0000256|ARBA:ARBA00025562}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707}; CC -!- SUBCELLULAR LOCATION: Host cytoplasm, host perinuclear region CC {ECO:0000256|ARBA:ARBA00004407}. Host membrane CC {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004301}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. CC {ECO:0000256|ARBA:ARBA00008087, ECO:0000256|PROSITE-ProRule:PRU01294}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN692788; QKV43822.1; -; Genomic_RNA. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. DR GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR GO; GO:0019082; P:viral protein processing; IEA:InterPro. DR CDD; cd21901; alpha_betaCoV_Nsp10; 1. DR CDD; cd21558; alphaCoV-Nsp6; 1. DR CDD; cd21514; alphaCoV_Nsp2_HCoV-229E-like; 1. DR CDD; cd21665; alphaCoV_Nsp5_Mpro; 1. DR CDD; cd21826; alphaCoV_Nsp7; 1. DR CDD; cd21830; alphaCoV_Nsp8; 1. DR CDD; cd21897; alphaCoV_Nsp9; 1. DR CDD; cd21731; alphaCoV_PLPro; 1. DR CDD; cd21473; cv_Nsp4_TM; 1. DR CDD; cd21557; Macro_X_Nsp3-like; 1. DR CDD; cd21875; PEDV-like_alphaCoV_Nsp1; 1. DR CDD; cd21712; TM_Y_alphaCoV_Nsp3_C; 1. DR Gene3D; 1.10.8.1190; -; 2. DR Gene3D; 6.10.140.2090; -; 1. DR Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1. DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1. DR Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1. DR Gene3D; 1.10.8.370; nsp7 replicase; 1. DR Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1. DR Gene3D; 2.40.10.250; Replicase NSP9; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR046443; a/bCoV_NSP1_glob. DR InterPro; IPR043613; CoV_NSP2_C. DR InterPro; IPR047573; CoV_NSP2_M. DR InterPro; IPR043611; CoV_NSP3_C. DR InterPro; IPR047566; CoV_NSP3_Y3. DR InterPro; IPR032505; CoV_NSP4_C. DR InterPro; IPR043612; CoV_NSP4_N. DR InterPro; IPR002589; Macro_dom. DR InterPro; IPR043472; Macro_dom-like. DR InterPro; IPR044371; Macro_X_NSP3-like. DR InterPro; IPR036333; NSP10_sf_CoV. DR InterPro; IPR044385; NSP2_HCoV-229E-like. DR InterPro; IPR043615; NSP2_N_CoV. DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV. DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV. DR InterPro; IPR038123; NSP4_C_sf_CoV. DR InterPro; IPR044309; NSP5_Mpro_alphaCoV. DR InterPro; IPR044369; NSP6_alphaCoV. DR InterPro; IPR043610; NSP6_CoV. DR InterPro; IPR014828; NSP7_CoV. DR InterPro; IPR037204; NSP7_sf_CoV. DR InterPro; IPR014829; NSP8_CoV. DR InterPro; IPR037230; NSP8_sf_CoV. DR InterPro; IPR014822; NSP9_CoV. DR InterPro; IPR036499; NSP9_sf_CoV. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR013016; Peptidase_C16_CoV. DR InterPro; IPR008740; Peptidase_C30_CoV. DR InterPro; IPR043477; Peptidase_C30_dom3_CoV. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR043178; PLpro_thumb_sf_CoV. DR InterPro; IPR018995; RNA_synth_NSP10_CoV. DR Pfam; PF09401; CoV_NSP10; 1. DR Pfam; PF19212; CoV_NSP2_C; 2. DR Pfam; PF19211; CoV_NSP2_N; 1. DR Pfam; PF19218; CoV_NSP3_C; 1. DR Pfam; PF16348; CoV_NSP4_C; 1. DR Pfam; PF19217; CoV_NSP4_N; 1. DR Pfam; PF19213; CoV_NSP6; 1. DR Pfam; PF08716; CoV_NSP7; 1. DR Pfam; PF08717; CoV_NSP8; 1. DR Pfam; PF08710; CoV_NSP9; 1. DR Pfam; PF08715; CoV_peptidase; 1. DR Pfam; PF01661; Macro; 1. DR Pfam; PF05409; Peptidase_C30; 1. DR SMART; SM00506; A1pp; 1. DR SUPFAM; SSF144246; Coronavirus NSP10-like; 1. DR SUPFAM; SSF140367; Coronavirus NSP7-like; 1. DR SUPFAM; SSF143076; Coronavirus NSP8-like; 1. DR SUPFAM; SSF52949; Macro domain-like; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. DR SUPFAM; SSF101816; Replicase NSP9; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1. DR PROSITE; PS51962; COV_NSP1; 1. DR PROSITE; PS51991; COV_NSP2_C; 1. DR PROSITE; PS51990; COV_NSP2_M; 1. DR PROSITE; PS51989; COV_NSP2_N; 1. DR PROSITE; PS51992; COV_NSP3_Y3; 1. DR PROSITE; PS51943; COV_NSP3A_UBL; 1. DR PROSITE; PS51944; COV_NSP3D_UBL; 1. DR PROSITE; PS51946; COV_NSP4C; 1. DR PROSITE; PS51949; COV_NSP7; 1. DR PROSITE; PS51950; COV_NSP8; 1. DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1. DR PROSITE; PS51442; M_PRO; 1. DR PROSITE; PS51154; MACRO; 1. DR PROSITE; PS51124; PEPTIDASE_C16; 2. PE 3: Inferred from homology; KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632}; KW Inhibition of host IRF3 by virus {ECO:0000256|ARBA:ARBA00022931}; KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Modulation of host ubiquitin pathway by viral deubiquitinase KW {ECO:0000256|ARBA:ARBA00022876}; KW Modulation of host ubiquitin pathway by virus KW {ECO:0000256|ARBA:ARBA00022662}; Protease {ECO:0000256|ARBA:ARBA00022670}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE- KW ProRule:PRU01296}; Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00444}. FT TRANSMEM 1964..1982 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2025..2044 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2104..2125 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2132..2153 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2165..2185 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2528..2546 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2787..2804 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2859..2887 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3337..3354 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3361..3381 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3401..3419 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3431..3449 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3469..3493 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3500..3520 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 2..109 FT /note="CoV Nsp1 globular" FT /evidence="ECO:0000259|PROSITE:PS51962" FT DOMAIN 112..364 FT /note="CoV Nsp2 N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51989" FT DOMAIN 383..776 FT /note="CoV Nsp2 middle" FT /evidence="ECO:0000259|PROSITE:PS51990" FT DOMAIN 778..895 FT /note="CoV Nsp2 C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51991" FT DOMAIN 896..991 FT /note="Ubiquitin-like" FT /evidence="ECO:0000259|PROSITE:PS51943" FT DOMAIN 1057..1296 FT /note="Peptidase C16" FT /evidence="ECO:0000259|PROSITE:PS51124" FT DOMAIN 1286..1465 FT /note="Macro" FT /evidence="ECO:0000259|PROSITE:PS51154" FT DOMAIN 1630..1685 FT /note="Ubiquitin-like" FT /evidence="ECO:0000259|PROSITE:PS51944" FT DOMAIN 1691..1951 FT /note="Peptidase C16" FT /evidence="ECO:0000259|PROSITE:PS51124" FT DOMAIN 2412..2516 FT /note="CoV Nsp3 Y3" FT /evidence="ECO:0000259|PROSITE:PS51992" FT DOMAIN 2902..2997 FT /note="Nsp4C" FT /evidence="ECO:0000259|PROSITE:PS51946" FT DOMAIN 2998..3299 FT /note="Peptidase C30" FT /evidence="ECO:0000259|PROSITE:PS51442" FT DOMAIN 3580..3662 FT /note="RdRp Nsp7 cofactor" FT /evidence="ECO:0000259|PROSITE:PS51949" FT DOMAIN 3663..3857 FT /note="RdRp Nsp8 cofactor" FT /evidence="ECO:0000259|PROSITE:PS51950" FT DOMAIN 3858..3965 FT /note="Nsp9 ssRNA-binding" FT /evidence="ECO:0000259|PROSITE:PS51951" FT DOMAIN 3966..4103 FT /note="ExoN/MTase coactivator" FT /evidence="ECO:0000259|PROSITE:PS51952" FT REGION 1012..1039 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 4117 AA; 453053 MW; 12D3BC4AE1DFDE21 CRC64; MASNHVTLAF ANDAEISAFG FCTASEAVSY YSEAAASGFM LCRFVSFDLA DTVEGLLPED YVMVVVGTTK LSAYVDTFGS RPKNICGWLL FSNCNYFLEE LELTFGRRGG NIVPVDQYMC GADGKPVLQE SEWEYTDFFA DSEDGQLNIA GITYVKAWIV ERSDVSYASQ NLTSIKSITY CSTYEHTFPD GTAMKVARTP KIKKTVVLSE PLATIYREIG SPFVDNGSDA RSIIKRPVFL HAFVKCKCGS CHWTVGDWTS YVSTCCGFKC KPVLVASCSA TPGSVVVTRA GAGTGVKYYN NMFLRHVADI DGLAFWRILK VQSKDDLACS GKFLEHHEEG FTDPCYFLND SSIATKLKFD ILSGKFSDEV KQAIFAGHVV VGSALVDIVD DALGQPWFIR KLGDLASAAW EQLKAVVRGL NLLSDEVVLF GKRLSCATLS IVNGVFEFLA EVPEKLAAAV TVFVNFLNEF FESACDCLKV GGKTFNKVGS YVLFDNALVK LVKAKVRGPR QAGVCEVRYT SLVIGSTSKV VSKRVENANV NLVVVDEDVT LNTTGRTVVV DGLAFFESDG FYRHLADADV VIEHPVYKSA CELKPVFECD PIPDFPMPVA ASVAELCVQT DLLLKNYNTP YKTYSCVVRG DKCCITCTLH FTAPSYMEAA ANFVDLCTKN IGTAGFHEFY ITAHEQQDLQ GFVTTCCTMS GFECFMPIIP QCPAVLEEID GGSIWRSFIT GLNTMWDFCK HLKVSFGLDG IVVTVARKFK RLGALLAEMY NTYLSTVVEN LVLAGVSFKY YATSVPKIVL GCCFHSVKSV LASAFQIPVQ AGVEKFKVFL NCVHPVVPRV IETSFVELEE TTFKPPALNG SIAIVDGFAF YYDGTLYYPT DGNSVVPICF KKKGGGDVKF SDEVSVKTID PVYKVSLEFE FESETIMAVL NKAVGNCIKV TGGWDDVVEY INVAIEVLKD HIDVPKYYIY DEEGGTDPNL PVMVSQWPLN DDTISQDLLD VEVITDAPVD FEGDEVDSSE PDKLADVANS EPEDDGLNVA PETNVESGVE EVAATWPFIK VTPSTVTKDP FAFDFASYGG LKVLRQSHNN CWVTSTLVQL QLLGIVDDPA MELFSAGRVG PMVRKCYESQ KAILGSLGDV SACLESLTKD LHTLKITCSV VCGCGTGERI YEGCAFRMTP TLEPFPYGAC AQCAQVLMHT FKSIVGTGIF CRDTTALSLD SLVVKPFCAA AFIGKDSGHY VTNFYDAAMA IDGYGRHQIK YDTLNTICVK DVNWTAPFVP DFEPVLEPVV KPFYSYKNVD FYQGDFSDLV KLPCDFVVNA ANESLSHGGG IAKAIDVYTK GMWQKCLNDY IPGHGPIKVG RGVMLEALGL KVFNVVGPRK GKHAPELLVK AYKSVFANSG VALTPFISVG IFSVPLEESL SAFLACVGDR HCKCFCYSDK EREAIINYMD GLVDAIFKDA LVDTTPVQED VQQVSQKPVL PNFEPFRIEG AHAFYECNPE GLMSLGADKL VLFTNSNLDF CSVGKCLNNV TGGALLEAIN VFKKSNKTVP AGNCVTFECA DMISITMVVL PSDGDANYDK NYARAVVKVS KLKGKLLLAV GDATLYSKLS HLSVVGFVST PDDVERFYAN KSVVIKVTED TRSVKAVKVE STVTYGQQIG PCLVNDTVVT DNKPVVADVV AKVVPSANWD SHYGFDKAGE FHMLDHTGFA FPSEVVNGRR VLKTTDNNCW VNVTCLQLQF ARFRFKSAGL QAMCESYCTG DVAMFVHWLY WLTGVDKGQP SDSENALNML SKYIVSAGSV TIERVTHDGC CCSKRVVTAP VVNASVLKLG VEDGLCPHGL NYIDKVVVVK GTTIVVNVGK PVVAPSHLFL KGVSYTTFLD NGNCVVGHYT VFDHDTGMVH DGDAFVPGDL NVSPVTNVVI SEQTAVVIKD PVKKVELDAT KLLDTMNYAS ERFFSFGDFM SRNLITVFLY ILSILGLCFR AFRKRDVKVL AGVPQRTGII LRKSVRYNAK ALGVFFKLKL YWFKVLGKFS LGIYALYALL FMTIRFTPIG GPVCDDVVAG YANSSFDKDE YCNSVICKVC LYGYQELSDF SHTQVVWQHL RDPLIGNVIP FFYLAFLAIF GGVYVKAITL YFICQYLNIL GVFLGLQQSI WFLQLVPFDV FGDEIVVFFI VTRVLMFLKH VFLGCDKASC VACSRSARLK RVPVQTIFQG TSKSFYVHAN GGSKFCKKHN FFCLNCDSYG PGCTFINDVI ATEVGNVVKL NVQPTGPATI LIDKVEFSNG FYYLYSGDTF WKYNFDITDS KYTCKESLKN CSIITDFIVF NNNGSNVNQV KNACVYFSQM LCKPVKLVDS ALLASLSVDF GASLHSAFVS VLSNSFGKDL SSCNDMQDCK STLGFDDVPL DTFNAAVAEA HRYDVLLTDM SFNNFTTSYA KPEEKLPVHD IATCMRVGAQ IVINNVFVKD SIPVVWLVRD FIALSEETRK YIIRTTKVKG ITFMLTFNDC RMHTTIPTVC IANKKGAGLP SFSKVKKFFW SLCLFIVAVF FALSFLDFST QVSIDSDYDF KYIESGQLKT FDNPLSCVHN VFSNFDQWHD AKFGFTPVNN PSCPIVVGVS DEARTVPGIP AGVYLAGKTL VFAINTIFGT SGLCFDASGV ADKGACIFNS ACTTLSGLGG TAVYCYKNGL VEGAKLYSEL APHSYYKMVD GNAVSLPEII SRGFGIRTIR TKAMTYCRVG QCVQSAEGVC FGADRFFVYN AESGSDFVCG TGLFTLLMNV ISVFSKTVPV TVLSGQILFN CIIAFAAVAV CFLFTKFKRM FGDMSVGVFT VGACTLLNNV SYIVTQNTLG MLGYATLYFL CTKGVRYMWI WHLGFLISYI LIAPWWVLMV YAFSAIFEFM PNLFKLKVST QLFEGDKFVG SFENAAAGTF VLDMHAYERL ANSISTEKLR QYASTYNKYK YYSGSASEAD YRLACFAHLA KAMMDYASNH NDTLYTPPTV SYNSTLQAGL RKMAQPSGVV EKCIVRVCYG NMALNGLWLG DTVMCPRHVI ASSTTSTIDY DYALSVLRLH NFSISSGNVF LGVVGVTMRG ALLQIKVNQN NVHTPKYTYR TVRPGESFNI LACYDGAAAG VYGVNMRSNY TIRGSFINGA CGSPGYNINN GTVEFCYLHQ LELGSGCHVG SDLDGVMYGG YEDQPTLQVE GASSLFTENV LAFLYAALIN GSTWWLSSSR IAVDRFNEWA VHNGMTTVGN TDCFSILAAK TGVDVQRLLA SIQSLHKNFG GKQILGYTSL TDEFTTGEVI RQMYGVNLQS GYVSRACRNV LLVGSFLTFF WSELVSYTKF FWVNPGYVTP MFACLSLLSS LLMFTLKHKT FFFQVFLIPA LIVTSCINLA FDVEVYNYLA EHFDYHVSLM GFNAQGLVNI FVCFVVTILH GTYTWRFFNT PVSSVTYVVA LLTAAYNYFY ASDILSCAMT LFASVTGNWF VGAVCYKAAV YMALRFPTFV AIFGDIKSVM FCYLVLGYFT CCFYGILYWF NRFFKVSVGV YDYTVSAAEF KYMVANGLRA PTGTLDSLLL SAKLIVIGGE RNIKLSSVQS KLTDIKCSNV VLLGCLSSMN VSANSTEWAY CVDLHNKINL CNDPEKAQEM LLALLAFFLS KNSAFGLDDL LESYFNDNSM LQSVASTYVG LPSYVIYENA RQQYEDAVNN GSPPQLVKQL RHAMNVAKSE FDREASTQRK LDRMAEQAAA QMYKEARAVN RKSKVVSAMH SLLFGMLRRL DMSSVDTILN LAKDGVVPLS VIPAVSATKL NIVTSDIDSY NRIQREGCVH YAGTIWNIID IKDNDGKVVH VKEVTAQNAE SLSWPLVLGC ERIVKLQNNE IIPGKLKQRS IKAEGDGIVG EGKALYNNEG GRTFMYAFIS DKPDLRVVKW EFDGGCNTIE LEPPRKFLVD SPNGAQIKYL YFVRNLNTLR RGAVLGYIGA TVRLQAGKQT EQAINSSLLT LCAFAVDPAK TYIDAVKSGH KPVGNCVKML ANGSGNGQAV TNGVEASTNQ DSYGGASVCL YCRAHVEHPS MDGFCRLKGK YVQVPLGTVD PIRFVLENDV CKVCGCWLAN GCTCDRSIMQ STDMAYLNEY GALVQLD //