ID   R1A_BCRP3               Reviewed;        4380 AA.
AC   P0C6T7; Q3I5J6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=Papain-like protease nsp3;
DE              Short=PL-PRO;
DE              EC=3.4.19.12;
DE              EC=3.4.22.-;
DE     AltName: Full=Non-structural protein 3;
DE              Short=nsp3;
DE     AltName: Full=PL2-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 Rp3/2004 (BtCoV/Rp3/2004) (SARS-like coronavirus Rp3).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Sarbecovirus;
OC   Severe acute respiratory syndrome coronavirus.
OX   NCBI_TaxID=349344;
OH   NCBI_TaxID=59479; Rhinolophus ferrumequinum (Greater horseshoe bat).
OH   NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
OH   NCBI_TaxID=188571; Rhinolophus pearsonii.
OH   NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16195424; DOI=10.1126/science.1118391;
RA   Li W., Shi Z., Yu M., Ren W., Smith C., Epstein J.H., Wang H., Crameri G.,
RA   Hu Z., Zhang H., Zhang J., McEachern J., Field H., Daszak P., Eaton B.T.,
RA   Zhang S., Wang L.F.;
RT   "Bats are natural reservoirs of SARS-like coronaviruses.";
RL   Science 310:676-679(2005).
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: [Papain-like protease nsp3]:
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: [Papain-like protease nsp3]: 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=P0C6T7-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6W6-1; 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: Bat coronavirus rp3 is highly similar to SARS-CoV (SARS-
CC       like).
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; DQ071615; AAZ67050.1; -; Genomic_RNA.
DR   BMRB; P0C6T7; -.
DR   SMR; P0C6T7; -.
DR   Proteomes; UP000006570; 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; cd21560; betaCoV-Nsp6; 1.
DR   CDD; cd21516; betaCoV_Nsp2_SARS-like; 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; cd21872; CoV_Nsp10; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR   CDD; cd21562; Macro_cv_SUD-N_Nsp3-like; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd22662; SARS-CoV-like_Nsp1_C; 1.
DR   CDD; cd21796; SARS-CoV-like_Nsp1_N; 1.
DR   CDD; cd21814; SARS-CoV-like_Nsp3_betaSM; 1.
DR   CDD; cd21822; SARS-CoV-like_Nsp3_NAB; 1.
DR   CDD; cd21525; SUD_C_SARS-CoV_Nsp3; 1.
DR   CDD; cd21717; TM_Y_SARS-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; 3.40.30.150; Coronavirus polyprotein cleavage domain; 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; 3.40.220.30; Nsp3, SUD-N 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; IPR038030; NSP1_glob_sf_bCoV.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR044389; NSP2_SARS-CoV-like.
DR   InterPro; IPR024375; NSP3_bCoV.
DR   InterPro; IPR047567; NSP3_G2M_bCoV.
DR   InterPro; IPR024358; NSP3_N_bCoV.
DR   InterPro; IPR032592; NSP3_NAB_bCoV.
DR   InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR   InterPro; IPR038166; NSP3_PL2pro_sf_bCoV.
DR   InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR   InterPro; IPR044864; NSP3_SUD-N_bCoV.
DR   InterPro; IPR044374; NSP3_SUD-N_SARS-CoV.
DR   InterPro; IPR043478; NSP3_SUD-N_sf_bCoV.
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   Pfam; PF16251; bCoV_NAB; 1.
DR   Pfam; PF11501; bCoV_NSP1; 1.
DR   Pfam; PF12379; bCoV_NSP3_N; 1.
DR   Pfam; PF12124; bCoV_SUD_C; 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; SSF160099; SARS Nsp1-like; 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.
DR   PROSITE; PS51940; SARS_NSP3C_N; 1.
PE   3: Inferred from homology;
KW   Activation of host autophagy by virus; Decay of host mRNAs by virus;
KW   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; Repeat;
KW   Ribosomal frameshifting; RNA-binding; Thiol protease; Transferase;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..4380
FT                   /note="Replicase polyprotein 1a"
FT                   /id="PRO_0000338122"
FT   CHAIN           1..179
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338123"
FT   CHAIN           180..818
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338124"
FT   CHAIN           819..2738
FT                   /note="Papain-like protease nsp3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338125"
FT   CHAIN           2739..3238
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338126"
FT   CHAIN           3239..3544
FT                   /note="3C-like proteinase nsp5"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338127"
FT   CHAIN           3545..3834
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338128"
FT   CHAIN           3835..3917
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338129"
FT   CHAIN           3918..4115
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338130"
FT   CHAIN           4116..4228
FT                   /note="RNA-capping enzyme subunit nsp9"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338131"
FT   CHAIN           4229..4367
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338132"
FT   CHAIN           4368..4380
FT                   /note="Non-structural protein 11"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338133"
FT   TRANSMEM        2201..2221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2312..2334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2349..2369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2753..2773
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3020..3040
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3059..3079
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3081..3101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3103..3123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3140..3160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3562..3582
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3584..3604
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3610..3630
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3657..3676
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3683..3702
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3726..3746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3754..3774
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          12..127
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          148..179
FT                   /note="BetaCoV Nsp1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT   DOMAIN          183..456
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          458..688
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          690..818
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          822..930
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1001..1167
FT                   /note="Macro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1205..1333
FT                   /note="Macro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1341..1468
FT                   /note="Macro 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1470..1536
FT                   /note="DPUP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT   DOMAIN          1540..1595
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1609..1873
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1886..1996
FT                   /note="Nucleic acid-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT   DOMAIN          2021..2130
FT                   /note="G2M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT   DOMAIN          2222..2292
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2370..2738
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          3140..3238
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          3239..3544
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3835..3917
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3918..4115
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          4116..4228
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          4229..4367
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   ZN_FING         1727..1764
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4302..4318
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4345..4358
FT                   /evidence="ECO:0000250"
FT   REGION          200..236
FT                   /note="C2H2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          323..344
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          370..416
FT                   /note="C2HC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          2201..2369
FT                   /note="HD1"
FT                   /evidence="ECO:0000250"
FT   REGION          2370..2460
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2374..2387
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2420..2430
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2461..2738
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2461..2555
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2556..2637
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2638..2738
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2753..3160
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3562..3774
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1649
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1810
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1824
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3279
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3383
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         370
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1727
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1730
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1762
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1764
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2374
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2379
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2387
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2423
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4345
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   SITE            179..180
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   SITE            818..819
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3238..3239
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3544..3545
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3834..3835
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3917..3918
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4115..4116
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4228..4229
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4367..4368
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   DISULFID        2238..2266
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2257..2263
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
SQ   SEQUENCE   4380 AA;  486337 MW;  0DDA57CD3DF1535B CRC64;
     MESLVLGINE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKSGT CGIVELEKGV
     LPQPEQPYVF IKRSDAQGTD HGHRVRELVA ELDGVQYGRS GITLGVLVPH VGETPIAYRN
     VLLRKNGNKG AGGHSFGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGVL RELTRELNGG
     ALTRYVDNNF CGPDGYPLEC IKDLLARAGK SMCTLSEQLD YIESKRGVYC CRDHGHEIAW
     FTERSDKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
     RSVYPVATPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV SEGPNTCGYL
     PTNAVVKMPC PACQDPEIGP EHSAADYHNH SNIETRLRKG GRTRCFGGCV FAYVGCYNKR
     AYWVPRASAD IGSGHTGITG DNVETLNEDL LEILSRERVN INIVGDFQLN EEVAIILASF
     SASTSAFIDT IKSLDYKSFK TIVESCGNYK VTKGKPIKGA WNIGQHRSVL TPLCGFPSQA
     AGVIRSIFSR TLDAANHSIP DLQRAAVTIL DSISEQSLRL VDAMVYTSNL LTNSVIIMAY
     VTGGLVQQTS QWLSNLLDTT VEKLRPIFAW IEAKLSAGVE FLKDAWEILK FLITGVFDIV
     KGQIQVASDN IKDCVKCFVD VVNKALEMCI DQVTIAGAKL RSLNLGEVFI AQSKGLYRQC
     IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV LTSEEVVLKN GELEALETPV DSFTNGAVVG
     TPVCINGLML LEIKANEQYC ALSPGLLATN NVFRLKGGAP TKGVTFGEDT VVEVQGYKNV
     RITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
     WSVATFYLFD DSGEEKLSSR MYCSFYPPDE EEDCEEYEEE EEVSERTCEH EYGTEEDYKG
     LPLEFGASTD IIQVEEQEEE DWLDDAVEAE PEPEPLHEEP VNQLTGYLKL TDNVAIKCVD
     IVEEAQNANP MVIVNAANIH LKHGGGVAGA LNKATNGAMQ KESDHYIKLN GPLTVGGSCL
     LSGHNLAKKC LHVVGPNLNA GEDIQLLKAA YENFNSQDIL LAPLLSAGIF GAKPLQSLQM
     CVQTVRTQVY IVVNDKVLYE QVVMDYLDSL KPKVEAPKQE VLPKAEYPKV DEKSVVQKTI
     DVKPKIKACI DEVTTTLEET KFLTNKLLLF TDINGKLYQD SKNMLRGEDM SFLEKDAPYM
     VGDVITSGDI TCVVIPSKKA GGTTEMLSRA LKKVPINEYI TTYPGQGCAG YTLEEAKTAL
     KKCKSAFYVL PSETPNAKEE ILGTVSWNLR EMLAHAEETR KLMPVCMDVR AIMATIQRKY
     KGIKIQEGIV DYGVRFFFYT SKEPVASIIT KLNSLNEPLV TMPIGYVTHG FNLEEAARCM
     RSLKAPAIVS VSSPDAVTTY NGYLTSSSKT SEDHFVETVS LAGSYRDWSY SGQRTELGVE
     FLKRGEKIVY HTLESPVKFH LDGEVLPLDK LKSLLSLREV KTIKVFTTVD NTNLHTQLVD
     MSMTYGQQLG PTYLEGADVT KIKPHVNHEG KTFFVLPSDD TLRSEAFEYY HTLDESFLGR
     YMSALNHTKK WKFPQVGGLT SIKWADNNCY LSSVLLALQQ IEVKFNAPAL QEAYYRARAG
     DAANFCALIL AYSNKTVGEL GDVRETMTHL LQHANLESAK RVLNVVCKHC GQKTTTLTGV
     EAVMYMGTLS YDNLKMGVSI PCVCGRDATQ YLVQQESSFV MMSAPPAEYK LQQGTFLCAN
     EYTGNYQCGH YTHITAKETL YRIDGAHLTK MSEYKGPVTD VFYKETSYTT TIKPVSYKLD
     GVTYTEIEPK LDGYYKKDNA YYTEQPIDLI PTQPLPNASF DNFKLTCSNT KFADDLNQMT
     GFTKPASREL SVTFFPDLNG DVVAIDYRHY SASFKKGAKL LHKPIVWHIN QATTKTTFKP
     NTWCLRCLWS TKPVDTSNSF EVLAVEDTQG MDNLACESQQ PTPEEVVENP TIQKEVIECD
     VKTTEVVGNV ILKPSDEGVK VTQELDHEDL MAAYVENTSI TIKKPNELSL ALGLKTIATH
     GIAAINSVPW GKILAYVKPF LGQAAVTTSN CAKRLVQRMF NNYMPYVLTL LFQLCTFTKS
     TNSRIRASLP TTIAKNSVRG IVRLCLDAGI NYVKSPKFSK LFTIAMWLLL LSICLGSLIY
     VTAALGVLLS NFGAPSYCSG VRESYLNSSN VTTMDFCEGS FPCSVCLSGL DSLDSYPALE
     TIQVTISSYK LDLTILGLAA EWFFAYMLFT KFFYLLGLSA IMQVFFGYFA SHFISNSWLM
     WFIISIVQMA PVSAMVRMYI FFASFYYIWK SYVHIMDGCT SSTCMMCYKR NRATRVECTT
     IVNGMKRSFY VYANGGRGFC KTHNWNCLNC DTFCAGSTFI SDEVARDLSL QFKRPINPTD
     QSSYVVDSVA VKNGALHLYF DKAGQKTYER HPLSHFVNLD NLRANNTKGS LPINVIVFDG
     KSKCDESAAK SASVYYSQLM CQPILLLDQA LVSDVGDSTE VSVKMFDAYV DTFSATFSVP
     MEKLKALVAT AHSELAKGVA LDGVLSTFVS ASRQGVVDTD VDTKDVIECL KLSHHSDLEV
     TGDSCNNFML TYNKVENMTP RDLGACIDCN ARHINAQVAR SHNVSLIWNV KDYMSLSEQL
     RKQIRSAAKK NNIPFRLTCA TTRQVVNVIT TKISLKGGKI VSTWFKIMLK ATLLCVLAAL
     VCYIVMPVHI LSVHGGYTNE IIGYKAIQDG VTRDIVSTDD CFANKHAGFD SWFSQRGGSY
     KNDKSCPVVA AIITREIGFI VPGLPGTVLR AINGDFLHFL PRVFSAVGNI CYTPSKLIEY
     SDFSTSACVL AAECTIFKDA MGKPVPYCYD TNLLEGSISY SELRPDTRYV LMDGSIIQFP
     NAYLEGSVRV VTTFDAEYCR HGTCERSEAG ICLSTSGRWV LNNEHYRALP GVFCGVDAMN
     LIANIFTPLV QPVGALDVSA SVVAGGIIAI LVTCAAYYFM KFRRAFGEYN HVVAANAPLF
     LMSFTILCLA PAYSFLPGVY SVFYLYLTFY FTNDVSFLAH LQWFAMFSPI VPFWITAIYV
     FCISLKHFHW FFNNYLRKRV VFNGVTFSTF EEAALCTFLL NKEMYLKLRS ETLLPLTQYN
     RYLALYNKYK YFSGALDTTS YREAACCHLA KALNDFSNSG ADVLYQPPQT SITSAVLQSG
     FRKMAFPSGK VEGCMVQVTC GTTTLNGLWL DDTVYCPRHV ICTAEDMLNP NYEDLLIRKS
     NHSFLVQAGN VQLRVIGHSM QNCLLRLKVD TSNPKTPKYK FVRIQPGQTF SVLACYNGSP
     SGVYQCAMRP NHTIKGSFLN GSCGSVGFNI DYDCVSFCYM HHMELPTEVH AGTDLEGKFY
     GPFVDRQTAQ AAGTDTTITL NVLAWLYAAV INGDRWFLNR FTTTLNDFNL VAMKYNYEPL
     TQDHVDILGP LSAQTGIAVL DMCAALKELL QNGMNGRTIL GSTILEDEFT PFDVVRQCSG
     VTFQGKFKRI VKGTHHWMLL TFLTSLLILV QSTQWSLFFF VYENAFLPFT LGIMAVAACA
     MLLVKHKHAF LCLFLLPSLA TVAYFNMVYM PASWVMRIMT WLELADTSLS GYRLKDCVMY
     ASALVLLVLM TARTVYDDAA RRVWTLMNVI TLVYKVYYGN ALDQAISMWA LVISVTSNYS
     GVVTTIMFLA RAIVFVCVEY YPLLFITGNT LQCIMLVYCF LGYCCCCYFG LFCLLNRYFR
     LTLGVYDYLV STQEFRYMNS QGLLPPKSSI DAFKLNIKLL GIGGKPCIKV ATVQSKMSDV
     KCTSVVLLSV LQQLRVESSS KLWAQCVQLH NDILLAKDTT EAFEKMVSLL SVLLSMQGAV
     DINKLCEEML DNRATLQAIA SEFSSLPSYA AYATAQEAYE QAVANGDSEV VLKKLKKSLN
     VAKSEFDRNA AMQRKLEKMA DQAMTQMYKQ ARSEDKRAKV TSAMQTMLFT MLRKLDNDAL
     NNIINNARDG CVPLNIIPLT TAAKLMVVVP DYGTYKNTCD GNTFTYASAL WEIQQVVDAD
     SKIVQLSEIN MENSSNLAWP LIVTALRANS AVKLQNNELS PVALRQMSCA AGTTQTACTD
     DNALAYYNNS KGGRFVLALL SDHQDLKWAR FPKSDGTGTI YTELEPPCRF VTDTPKGPKV
     KYLHFIKGLN NLNRGMVLGS LAATVRLQAG NATEVPANST VLSFCAFAVD PAKAYKDYLA
     SGGQPITNCV KMLCTHTGTG QAITVTPEAN MDQESFGGAS CCLYCRCHID HPNPKGFCDL
     KGKYVQIPTT CANDPVGFTL RNTVCTVCGM WKGYGCSCDQ LREPMMQSAD ASTFLNGFAV
//