ID   R1A_BCHK4               Reviewed;        4434 AA.
AC   P0C6T4; A3EX93;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Replicase polyprotein 1a;
DE            Short=pp1a;
DE   AltName: Full=ORF1a polyprotein;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=nsp1;
DE     AltName: Full=Leader protein;
DE   Contains:
DE     RecName: Full=Non-structural protein 2;
DE              Short=nsp2;
DE     AltName: Full=p65 homolog;
DE   Contains:
DE     RecName: Full=Non-structural protein 3;
DE              Short=nsp3;
DE              EC=3.4.19.12;
DE              EC=3.4.22.-;
DE     AltName: Full=PL2-PRO;
DE     AltName: Full=Papain-like proteinase;
DE              Short=PL-PRO;
DE   Contains:
DE     RecName: Full=Non-structural protein 4;
DE              Short=nsp4;
DE   Contains:
DE     RecName: Full=3C-like proteinase nsp5;
DE              Short=3CL-PRO;
DE              Short=3CLp;
DE              EC=3.4.22.69;
DE     AltName: Full=nsp5;
DE   Contains:
DE     RecName: Full=Non-structural protein 6;
DE              Short=nsp6;
DE   Contains:
DE     RecName: Full=Non-structural protein 7;
DE              Short=nsp7;
DE   Contains:
DE     RecName: Full=Non-structural protein 8;
DE              Short=nsp8;
DE   Contains:
DE     RecName: Full=RNA-capping enzyme subunit nsp9;
DE     AltName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE              EC=2.7.7.50;
DE   Contains:
DE     RecName: Full=Non-structural protein 10;
DE              Short=nsp10;
DE     AltName: Full=Growth factor-like peptide;
DE              Short=GFL;
DE   Contains:
DE     RecName: Full=Non-structural protein 11;
DE              Short=nsp11;
GN   ORFNames=1a;
OS   Bat coronavirus HKU4 (BtCoV) (BtCoV/HKU4/2004).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Merbecovirus.
OX   NCBI_TaxID=694007;
OH   NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat) (Vespertilio pachypus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate HKU4-1;
RX   PubMed=17121802; DOI=10.1128/jvi.02182-06;
RA   Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA   Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA   Zheng B.-J., Yuen K.-Y.;
RT   "Comparative analysis of twelve genomes of three novel group 2c and group
RT   2d coronaviruses reveals unique group and subgroup features.";
RL   J. Virol. 81:1574-1585(2007).
CC   -!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for the
CC       cleavages located at the N-terminus of replicase polyprotein. In
CC       addition, PL-PRO possesses a deubiquitinating/deISGylating activity and
CC       processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
CC       cellular substrates. Antagonizes innate immune induction of type I
CC       interferon by blocking the phosphorylation, dimerization and subsequent
CC       nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [3C-like proteinase nsp5]: Responsible for the majority of
CC       cleavages as it cleaves the C-terminus of replicase polyprotein at 11
CC       sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-
CC       [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC       CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function
CC       (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}.
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:0000250}.
CC   -!- FUNCTION: [RNA-capping enzyme subunit nsp9]: Catalytic subunit of viral
CC       RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction
CC       for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12
CC       transfers RNA to the amino terminus of NSP9, forming a covalent RNA-
CC       protein intermediate. Subsequently, the NiRAN domain transfers RNA to
CC       GDP, forming the core cap structure GpppA-RNA. The NSP14 and NSP16
CC       methyltransferases then add methyl groups to form functional cap
CC       structures. {ECO:0000250|UniProtKB:P0DTC1}.
CC   -!- FUNCTION: [Non-structural protein 1]: Binds to the 40S ribosomal
CC       subunit and inhibits host translation. The nsp1-40S ribosome complex
CC       further induces an endonucleolytic cleavage near the 5'UTR of host
CC       mRNAs, targeting them for degradation. By suppressing host gene
CC       expression, nsp1 facilitates efficient viral gene expression in
CC       infected cells and evasion from host immune response (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: [Non-structural protein 3]:
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:0000250|UniProtKB:P0DTC1};
CC   -!- CATALYTIC ACTIVITY: [3C-like proteinase nsp5]:
CC       Reaction=TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides
CC         corresponding to the two self-cleavage sites of the SARS 3C-like
CC         proteinase are the two most reactive peptide substrates. The enzyme
CC         exhibits a strong preference for substrates containing Gln at P1
CC         position and Leu at P2 position.; EC=3.4.22.69;
CC         Evidence={ECO:0000250|UniProtKB:P0DTC1};
CC   -!- CATALYTIC ACTIVITY: [RNA-capping enzyme subunit nsp9]:
CC       Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC         end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC         Evidence={ECO:0000250|UniProtKB:P0DTC1};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67014;
CC         Evidence={ECO:0000250|UniProtKB:P0DTC1};
CC   -!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of nsp7
CC       and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is
CC       a dimer. Nsp10 forms a dodecamer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [RNA-capping enzyme subunit nsp9]: Host
CC       cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9
CC       and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
CC       in infection, they merge into confluent complexes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6T4-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6W3-1; Sequence=External;
CC   -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC       association of the replication complex and thereby alter the
CC       architecture of the host cell membrane. {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC       mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC       processed (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
CC       conventional translation.
CC   -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC       {ECO:0000305}.
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DR   EMBL; EF065505; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   PDB; 2YNA; X-ray; 1.50 A; A/B=3292-3597.
DR   PDB; 2YNB; X-ray; 1.96 A; A/B=3292-3597.
DR   PDBsum; 2YNA; -.
DR   PDBsum; 2YNB; -.
DR   SMR; P0C6T4; -.
DR   SABIO-RK; P0C6T4; -.
DR   Proteomes; UP000006574; Genome.
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-KW.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; 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:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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; cd21560; betaCoV-Nsp6; 1.
DR   CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR   CDD; cd21827; betaCoV_Nsp7; 1.
DR   CDD; cd21831; betaCoV_Nsp8; 1.
DR   CDD; cd21898; betaCoV_Nsp9; 1.
DR   CDD; cd21732; betaCoV_PLPro; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21878; MERS-CoV-like_Nsp1; 1.
DR   CDD; cd21815; MERS-CoV-like_Nsp3_betaSM; 1.
DR   CDD; cd21823; MERS-CoV-like_Nsp3_NAB; 1.
DR   CDD; cd21523; SUD_C_MERS-CoV_Nsp3; 1.
DR   CDD; cd21716; TM_Y_MERS-CoV-like_Nsp3_C; 1.
DR   CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR   Gene3D; 1.10.8.1190; -; 1.
DR   Gene3D; 2.60.120.1680; -; 1.
DR   Gene3D; 3.10.20.350; -; 1.
DR   Gene3D; 3.10.20.540; -; 1.
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; 3.40.220.20; Nsp3, SUD-M subdomain; 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; 3.40.50.11020; Replicase polyprotein, nucleic acid-binding domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR046443; a/bCoV_NSP1_glob.
DR   InterPro; IPR046442; bCoV_NSP1_C.
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; IPR022733; DPUP_SUD_C_bCoV.
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; IPR021590; NSP1_glob_bCoV.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR024375; NSP3_bCoV.
DR   InterPro; IPR047567; NSP3_G2M_bCoV.
DR   InterPro; IPR032592; NSP3_NAB_bCoV.
DR   InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR   InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR   InterPro; IPR044382; NSP3_SUD_C_MERS-CoV.
DR   InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR   InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR   InterPro; IPR038083; NSP3A-like.
DR   InterPro; IPR038123; NSP4_C_sf_CoV.
DR   InterPro; IPR044367; NSP6_betaCoV.
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; 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; IPR043177; PLpro_N_sf_CoV.
DR   InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR   InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   PANTHER; PTHR11106; GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR11106:SF111; MACRO DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF16251; bCoV_NAB; 1.
DR   Pfam; PF11501; bCoV_NSP1; 1.
DR   Pfam; PF11633; bCoV_SUD_M; 1.
DR   Pfam; PF09401; CoV_NSP10; 1.
DR   Pfam; PF19212; CoV_NSP2_C; 1.
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; SSF159936; NSP3A-like; 1.
DR   SUPFAM; SSF101816; Replicase NSP9; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51963; BCOV_NSP1_C; 1.
DR   PROSITE; PS51942; BCOV_NSP3C_C; 1.
DR   PROSITE; PS51941; BCOV_NSP3C_M; 1.
DR   PROSITE; PS51994; BCOV_NSP3E_G2M; 1.
DR   PROSITE; PS51945; BCOV_NSP3E_NAB; 1.
DR   PROSITE; PS51993; COV_3ECTO; 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_Y; 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; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus;
KW   Decay of host mRNAs by virus; Disulfide bond; Endonuclease;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW   Host gene expression shutoff by virus; Host membrane;
KW   Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host ISG15 by virus;
KW   Inhibition of host RLR pathway by virus;
KW   Interferon antiviral system evasion; Membrane; Metal-binding;
KW   Methyltransferase;
KW   Modulation of host ubiquitin pathway by viral deubiquitinase;
KW   Modulation of host ubiquitin pathway by virus; Nuclease; Protease;
KW   Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
KW   Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..4434
FT                   /note="Replicase polyprotein 1a"
FT                   /id="PRO_0000338086"
FT   CHAIN           1..195
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338087"
FT   CHAIN           196..847
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338088"
FT   CHAIN           848..2784
FT                   /note="Non-structural protein 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338089"
FT   CHAIN           2785..3291
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338090"
FT   CHAIN           3292..3597
FT                   /note="3C-like proteinase nsp5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338091"
FT   CHAIN           3598..3889
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338092"
FT   CHAIN           3890..3972
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338093"
FT   CHAIN           3973..4171
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338094"
FT   CHAIN           4172..4281
FT                   /note="RNA-capping enzyme subunit nsp9"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338095"
FT   CHAIN           4281..4434
FT                   /note="Non-structural protein 11"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338097"
FT   CHAIN           4282..4420
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338096"
FT   TRANSMEM        2145..2165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2222..2242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2326..2346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2350..2370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2375..2395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2800..2820
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3072..3092
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3105..3125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3149..3169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3603..3623
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3637..3657
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3662..3682
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3707..3727
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3735..3755
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3784..3804
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3808..3828
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..151
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          167..195
FT                   /note="BetaCoV Nsp1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT   DOMAIN          197..472
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          478..712
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          714..847
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          851..960
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1152..1321
FT                   /note="Macro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1322..1446
FT                   /note="Macro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1446..1519
FT                   /note="DPUP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT   DOMAIN          1524..1579
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1593..1864
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1878..1995
FT                   /note="Nucleic acid-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT   DOMAIN          2012..2133
FT                   /note="G2M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT   DOMAIN          2259..2325
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2409..2782
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          3195..3291
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          3292..3597
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3890..3972
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3973..4171
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          4172..4281
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          4282..4420
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   ZN_FING         1714..1751
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4355..4371
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4397..4410
FT                   /evidence="ECO:0000250"
FT   REGION          339..360
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          2112..2395
FT                   /note="HD1"
FT                   /evidence="ECO:0000250"
FT   REGION          2409..2499
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2413..2426
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2459..2469
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2500..2782
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2500..2598
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2599..2681
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2682..2782
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2800..3169
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3603..3828
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1634
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1800
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1815
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3332
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3439
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1714
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1717
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1749
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1751
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2418
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2423
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2426
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2462
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2469
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4400
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   SITE            195..196
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            847..848
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            2784..2785
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3291..3292
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3597..3598
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3889..3890
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3972..3973
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4171..4172
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4281..4282
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4420..4421
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   DISULFID        2275..2303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2293..2300
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   HELIX           3302..3305
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3308..3313
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3316..3323
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3326..3330
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3331..3334
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3337..3339
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3345..3350
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3354..3356
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3358..3360
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3363..3365
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3367..3369
FT                   /evidence="ECO:0007829|PDB:2YNB"
FT   STRAND          3371..3377
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3380..3387
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3394..3397
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3405..3412
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3415..3423
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3442..3447
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3450..3462
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3465..3469
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3476..3478
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3481..3484
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3495..3507
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3521..3530
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3540..3549
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3553..3565
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   STRAND          3575..3577
FT                   /evidence="ECO:0007829|PDB:2YNA"
FT   HELIX           3584..3591
FT                   /evidence="ECO:0007829|PDB:2YNA"
SQ   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
//