ID   R1A_BC133               Reviewed;        4441 AA.
AC   P0C6F7; Q0Q4F3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 105.
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 133/2005 (BtCoV) (BtCoV/133/2005).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Merbecovirus; Bat coronavirus HKU4.
OX   NCBI_TaxID=389230;
OH   NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat) (Vespertilio pachypus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16840328; DOI=10.1128/jvi.00697-06;
RA   Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
RA   Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
RA   Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
RT   "Prevalence and genetic diversity of coronaviruses in bats from China.";
RL   J. Virol. 80:7481-7490(2006).
RN   [2]
RP   FUNCTION OF NSP1.
RX   PubMed=19264783; DOI=10.1128/jvi.02485-08;
RA   Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K., Makino S.;
RT   "Suppression of host gene expression by nsp1 proteins of group 2 bat
RT   coronaviruses.";
RL   J. Virol. 83:5282-5288(2009).
CC   -!- FUNCTION: [Papain-like protease nsp3]: Responsible for the cleavages
CC       located at the N-terminus of replicase polyprotein. In addition, PL-PRO
CC       possesses a deubiquitinating/deISGylating activity and processes both
CC       'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular
CC       substrates. Antagonizes innate immune induction of type I interferon by
CC       blocking the phosphorylation, dimerization and subsequent nuclear
CC       translocation of host IRF-3. {ECO:0000269|PubMed:19264783}.
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: [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.
CC       {ECO:0000269|PubMed:19264783}.
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   -!- 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=P0C6F7-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6W1-1; 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; DQ648794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0C6F7; -.
DR   Proteomes; UP000007449; 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   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..4441
FT                   /note="Replicase polyprotein 1a"
FT                   /id="PRO_0000338062"
FT   CHAIN           1..195
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338063"
FT   CHAIN           196..847
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338064"
FT   CHAIN           848..2791
FT                   /note="Papain-like protease nsp3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338065"
FT   CHAIN           2792..3298
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338066"
FT   CHAIN           3299..3604
FT                   /note="3C-like proteinase nsp5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338067"
FT   CHAIN           3605..3896
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338068"
FT   CHAIN           3897..3979
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338069"
FT   CHAIN           3980..4178
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338070"
FT   CHAIN           4179..4288
FT                   /note="RNA-capping enzyme subunit nsp9"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338071"
FT   CHAIN           4288..4441
FT                   /note="Non-structural protein 11"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338073"
FT   CHAIN           4289..4427
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338072"
FT   TRANSMEM        2152..2172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2229..2249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2333..2353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2357..2377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2382..2402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2807..2827
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3079..3099
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3112..3132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3156..3176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3610..3630
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3644..3664
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3669..3689
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3714..3734
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3742..3762
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3791..3811
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3815..3835
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          1159..1328
FT                   /note="Macro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1329..1453
FT                   /note="Macro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1453..1526
FT                   /note="DPUP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT   DOMAIN          1531..1586
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1600..1871
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1885..2002
FT                   /note="Nucleic acid-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT   DOMAIN          2019..2140
FT                   /note="G2M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT   DOMAIN          2266..2332
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2416..2789
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          3202..3298
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          3299..3604
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3897..3979
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3980..4178
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          4179..4288
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          4289..4427
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   ZN_FING         1721..1758
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4362..4378
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4404..4417
FT                   /evidence="ECO:0000250"
FT   REGION          339..360
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          1039..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2119..2402
FT                   /note="HD1"
FT                   /evidence="ECO:0000250"
FT   REGION          2416..2506
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2420..2433
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2466..2476
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2507..2789
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2507..2605
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2606..2688
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2689..2789
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2807..3176
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3610..3835
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1040..1061
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1641
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1807
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1822
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3339
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3446
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         1721
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1724
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1756
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1758
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
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         2473
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4365
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         4378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4415
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4417
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            2791..2792
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3298..3299
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3604..3605
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3896..3897
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3979..3980
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4178..4179
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4288..4289
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4427..4428
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   DISULFID        2282..2310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2300..2307
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
SQ   SEQUENCE   4441 AA;  492464 MW;  A6E0DB4CDDA40AC7 CRC64;
     MLSKAGVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTED MASKLTPWFE DGETAFNQVS
     SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS KHFLVNQLAY KDHVGAAMMR
     TTLNVKPLGM FFPYDSSLET GEHTFLLRKN GLGGQLFRER PWDRKETPYV EILDDLEADP
     TGKYSQNLLK KLIGGDCIPV DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS
     DRFIVLNKKL YRVVWNVTRR NVPYSKQTAF TVVSVIQCDD KESVPEHTFT IGSQILMVSP
     LKATNNKNFN LKQRLLHTFY GKEAVQQPGY IYHSAYVDCN ACGRGTWCTG NAIQGFACDC
     GANYSANDVD LQSSGLVPKN ALFLANCPCA NNGACSHNAA QVYSILDGKA CVEVGGKSFT
     LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR IGDAIFTGCT GTWDKVVETA NLFLEKAQHS
     LNFCQQFALT EVVLAILSGT TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI
     NIGANGVCNA TINAPFIAFT GLGESFKKVA AIPWKICSNL KSALDYYCSN IMFRVFPYDI
     PCDVNDFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SNACQTALSS FLNACVAASR
     ATAGFISDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ QVLDIMSKAM KLLHTNVSWA
     GTKLSAIIYE GREALLFNSG TYFCLSTKAK TLQDQMNLVL PGDYNKKTLG ILDPVPNADT
     IDVTANSTVV DVVHGQLEPT NEHGPSMIVG NYVLVSDKLF VRTDDEEFYP LCINGKVVST
     LFRLKGGMPS KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
     DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN MTFSINPVED
     VEEVEEFIED DYLSDELPIA DDEEAWTRAV EEVMPLDDIL VAEIELEEDL PLETALESVE
     AEVGESISDE LCVVETAKAQ EPSVESTDST PSTSTVVSEN DLSVKPMSRV AETGDVLEVE
     TAVVGGPVSD VTASVVTNDI VSVEQAQQCG VSSLPIQDEA SENQVHQVPD LQCTSETKVE
     IVQPRQDLRP RRLRKSKVDL SKYKHTVINN SVTLVLGDAI QIASLLPKCV LVNAANRHLK
     HGGGIAGAIN KASGGDVQEE SDEYISNSGP LHVGDSVLLK GYGLADAILR VVGPDARNNE
     DAALLKRCYK TFNKHTIVVT PLISSGIFSV DPKVSFEYLL ANVTTTTYVV VNNEDIYNTL
     ATPSKPDGLV YSFEGWRGTV RTAKNYGFTC FICTEYSANV KFLRTKGVDT TKKIQTVDGV
     SYYLYSARDA LTDVIAAANG CPGICAMPFG YVTHGLDLAQ SGNYVRQVKV PYVCLLASKE
     QIPIMNSDVA IQTPETAFIN NVTSNGGYHS WHLVSGDLIV KDVCYKKLLH WSGQTICYAD
     NKFYVVKNDV ALPFSDLEAC RAYLTSRAAQ QVNIEVLVTI DGVNFRTVIL NDATTFRKQL
     GATFYKGVDI SDALPTVKMG GESLFVADNL SESEEVVLKE YYGTSDVTFL QRYYSLQPLV
     QQWKFVVHDG VKSLKLSNYN CYINATIMMI DMLHDIKFVV PALQNAYLRY KGGDPYDFLA
     LIMAYGDCTF DNPDDEAKLL HTLLAKAELT VSAKMVWREW CTVCGIRDIE YTGMRACVYA
     GVNSMEELQS VFNETCVCGS VKHRQLVEHS TPWLLVSGLN EVKVSTSTDP VYRAFNVFQG
     VETSVGHYVH VRVKDGLFYK YDSGSLTKTS DMKCKMTSVW YPKVRYTADC NVVVYDLDGV
     TKVEVNPDLS NYYMKDGKYY TSKPTIKYSP ATILPGSVYS NSCLVGVDGT PGSDTISKFF
     NDLLGFDETK PISKKLTYSL LPNEDGDVLL SEFNNYNPVY KKGVMLKGKP ILWVNNGVCD
     SALNKPNRAS LRQLYDVAPI VLDNKYTVLQ DNTSQLIEPN VPVVEDVSIT TRKLIEVKCK
     GLNKPFVKGN FSFVNDPNGV TVVDTLGLTE LRALYVDINT RYIVLRDNNW SSLFKLHTVE
     SGDLQIVANG GSVTRRARVL LGASSLFASF AKITVTATTA ACKTAGRSFC KFVVNYGVLQ
     NMFLFLKMLF FLPFNYLWPK KQPTVDVGVS GLRTAGVVTT NIVKQCGTAA YYMLLGKFKR
     VDWKATLRLF LLLCTTILLL SSIYHLVIFN QVLSSDVMLE DATGILAMYK EVRSYLGIRT
     LCDGLAVEYR NTSFDVVDFC SNRSVLCQWC LIGQDSLTRY SALQMLQTHI TSYVLNIDWI
     WFALEFFLAY VLYTSSFNVL LLVVTAQYFF AYTSAFVNWR AYNYIVSGLF FLVTHIPLHG
     LVRVYNFLAC LWFLRKFYSH VINGCKDTAC LLCYKRNRLT RVEASTIVCG TKRTFYIAAN
     GGTSYCCKHN WNCVECDTAG VGNTFICTEV ANDLTTTLRR LIKPTDQSHY YVDSVVVKDA
     VVELHYNRDG SSCYERYPLC YFTNLEKLKF KEVCKTPTGI PEHNFLIYDT NDRGQENLAR
     SACVYYSQVL CKPMLLVDVN LVTTVGDSRE IAIKMLDSFI NSFISLFSVS RDKLEKLINT
     ARDCVRRGDD FQTVLKTFTD AARGHAGVES DVETTMVVDA LQYAHKNDIQ LTTECYNNYV
     PGYIKPDSIN TLDLGCLIDL KAASVNQTSM RNANGACVWN SGDYMKLSDS FKRQIRIACR
     KCNIPFRLTT SKLRAADNIL SVKFSATKIV GGAPSWLLRV RDLTVKGYCI LTLFVFTVAV
     LSWFCLPSYS IATVNFNDDR ILTYKVIENG IVRDIAPNDA CFANKYGHFS KWFNENHGGV
     YRNSVDCPIT IAVIAGVAGA RVANVPATLA WVGRQIVLFV SRVFANTNVC FTPTNEIPYD
     TFSDSGCVLS SECTLFRDAE GNLNPFCYDP TVLPGASSYA DMKPHVRYDM YDSDMYIKFP
     EVIFESTLRI TKTLATQYCR FGSCEESAAG VCISTNGSWA LYNQNYSTRP GIYCGDDYFD
     IVRRLAVSLF QPVTYFQLST SLAMGLVLCV FLTAAFYYIN KVKRALADYT QCAVVAVVAA
     LLNSLCLCFI VANPLLVAPY TAMYYYATFY LTGEPAFIMH ISWYVMFGTV VPIWMLASYT
     VGVMLRHLFW VLAYFSKKHV DVFTDGKLNC SFQDAASNIF VIGKDTYVAL RNAITQDSFV
     RYLSLFNKYK YYSGAMDTAS YREACAAHLC KALQTYSETG SDILYQPPNC SVTSSVLQSG
     LVKMSAPSGA VENCIVQVTC GSMTLNGLWL DNTVWCPRHI MCPADQLTDP NYDALLISKT
     NHSFIVQKHI GAQANLRVVA HSMVGVLLKL TVDVANPSTP AYTFSTVKPG ASFSVLACYN
     GKPTGVFTVN LRHNSTIKGS FLCGSCGSVG YTENGGVLNF VYMHQMELSN GTHTGSSFDG
     VMYGAFEDKQ THQLQLTDKY CTINVVAWLY AAVLNGCKWF VKPTRVGIVT YNEWALSNQF
     TEFVGTQSID MLAHRTGVSV EQMLAAIQSL HAGFQGKTIL GQSTLEDEFT PDDVNMQVMG
     VVMQSGVKRI SYGFMHWLMS TLVLAYVSVM QLTKFTMWTY LFETIPTQMT PLLFGFMACV
     MFTVKHKHTF LSLFLLPVAL CLTYANIVYE PQTLVSSTLI AVANWLTPTS VYMRTTHLDF
     GLYISLSFVL AIIVRRLYRP SMSNLALALC SGVMWFYTYV IGDHSSPITY LMFITTLTSD
     YTITVFATVN LAKFISGLVF LYAPHLGFIL PEVKLVLLIY LCLGYMCTMY FGVFSLLNLK
     LRVPLGVYDY SVSTQEFRFL TGNGLHAPRN SWEALILNFK LLGIGGTPCI KVATVQSKLT
     DLKCTSVVLL TVLQQLHLES NSKAWSYCVK LHNEILAAVD PTEAFERFVC LFATLMSFSA
     NVDLDALAND LFENSSVLQA TLTEFSHLAT YAELETAQSS YQKALNSGDA SPQVLKALQK
     AVNVAKNAYE KDKAVARKLE RMAEQAMTSM YKQARAEDKK AKIVSAMQTM LFGMIKKLDN
     DVLNGVIANA RNGCVPLSIV PLCASNKLRV VIPDISVWNK VVNWPSVSYA GSLWDVTVIN
     NVDNEVVKPT DVVETNESLT WPLVIECSRA SSSAVKLQNN EIHPKGLKTM VVTAGIDQVN
     CSSSAVAYYE PVQGHRMVMG LLSENAHLKW AKVEGKDGFI NIELQPPCKF LIAGPKGPEI
     RYLYFVKNLN NLHRGQLLGH IAATVRLQAG ANTEFASNST VLTLVAFAVD PAKAYLDYVG
     SGGTPLSNYV KMLAPKTGTG VAISVKPEAT ADQETYGGAS VCLYCRAHIE HPDVSGVCKY
     KTRFVQIPAH VRDPVGFLLK NVPCNVCQYW VGYGCNCDAL RNNTVPQSKD TNFLNESGVL
     V
//