ID   R1A_BCHK9               Reviewed;        4248 AA.
AC   P0C6T6; A3EXG5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
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 HKU9 (BtCoV) (BtCoV/HKU9).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Nobecovirus.
OX   NCBI_TaxID=694006;
OH   NCBI_TaxID=9408; Rousettus leschenaultii (Leschenault's rousette).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate HKU9-1;
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).
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: 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.
CC       {ECO:0000269|PubMed:19264783}.
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=P0C6T6-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6W5-1; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF065513; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0C6T6; -.
DR   Proteomes; UP000006576; 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: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; cd21518; betaCoV_Nsp2_HKU9-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; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21877; HKU9-like_Nsp1; 1.
DR   CDD; cd21813; HKU9-like_Nsp3_betaSM; 1.
DR   CDD; cd21825; HKU9-like_Nsp3_NAB; 1.
DR   CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21537; SUD_C_HKU9_CoV_Nsp3; 1.
DR   CDD; cd21715; TM_Y_HKU9-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; IPR044386; NSP2_HKU9-like.
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; IPR044352; Nsp3_SUD_C_HKU9_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   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; 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; 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..4248
FT                   /note="Replicase polyprotein 1a"
FT                   /id="PRO_0000338110"
FT   CHAIN           1..175
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338111"
FT   CHAIN           176..772
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338112"
FT   CHAIN           773..2609
FT                   /note="Papain-like protease nsp3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338113"
FT   CHAIN           2610..3103
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338114"
FT   CHAIN           3104..3409
FT                   /note="3C-like proteinase nsp5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338115"
FT   CHAIN           3410..3699
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338116"
FT   CHAIN           3700..3782
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338117"
FT   CHAIN           3783..3982
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338118"
FT   CHAIN           3983..4094
FT                   /note="RNA-capping enzyme subunit nsp9"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338119"
FT   CHAIN           4094..4248
FT                   /note="Non-structural protein 11"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338121"
FT   CHAIN           4095..4233
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338120"
FT   TRANSMEM        2040..2060
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2081..2101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2162..2182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2183..2203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2218..2238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2621..2641
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2719..2739
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2865..2885
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2887..2907
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2916..2936
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2946..2966
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2970..2990
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3423..3443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3449..3469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3474..3494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3517..3537
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3569..3589
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3592..3612
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3620..3640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          10..131
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          149..175
FT                   /note="BetaCoV Nsp1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT   DOMAIN          177..431
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          432..644
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          646..772
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          775..885
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          930..1097
FT                   /note="Macro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1216..1340
FT                   /note="Macro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1345..1417
FT                   /note="DPUP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT   DOMAIN          1423..1478
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1492..1757
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1770..1870
FT                   /note="Nucleic acid-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT   DOMAIN          1883..2012
FT                   /note="G2M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT   DOMAIN          2105..2162
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2239..2610
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          3007..3103
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          3104..3409
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3700..3782
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3783..3982
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          3983..4094
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          4095..4233
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   ZN_FING         1610..1647
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4168..4184
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4211..4224
FT                   /evidence="ECO:0000250"
FT   REGION          312..333
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          1188..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2015..2238
FT                   /note="HD1"
FT                   /evidence="ECO:0000250"
FT   REGION          2239..2329
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2243..2256
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2289..2299
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2330..2610
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2330..2425
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2426..2509
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2510..2610
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2621..2990
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3423..3640
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1533
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1694
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1708
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3144
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3248
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1610
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1613
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1645
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1647
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   SITE            175..176
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            772..773
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            2609..2610
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3103..3104
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3409..3410
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3699..3700
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3782..3783
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3982..3983
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4094..4095
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4233..4234
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   DISULFID        2121..2138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
SQ   SEQUENCE   4248 AA;  468590 MW;  C0D0584A862070A7 CRC64;
     MEGVPDPPKL KSMVVTTLKW CDPFANPNVT GWDIPIEEAL EYAKQQLRTP EPQLVFVPYY
     LSHAPGISGD RVVITDSIWY ATNFGWQPIR ELAMDKDGVR YGRGGTHGVL LPMQDPSFIM
     GDIDIQIRKY GIGANSPPDV LPLWDGFSDP GPDVGPYLDF PDNCCPTKPK AKRGGDVYLS
     DQYGFDNNGI LVEPVMKLLG VIKSDFTLEQ LLAALGKYRT EDGYDLPDGY VKVAIKVGRK
     AVPVLKQSIF TVVGVTEQLV PGYYYPFSTS SVVEHTKPTR GGPVGKTVEA VMLSLYGTNN
     YNPATPVARL KCSYCDYYGW TPLKDIGTVN CLCGAEFQLT SSCVDAESAG VIKPGCVMLL
     DKSPGMRLIP GNRTYVSFGG AIWSPIGKVN GVTVWVPRAY SIVAGEHSGA VGSGDTVAIN
     KELVEYLIEG IRVDADTLDN PTCATFIANL DCDTKAPVVH TVESLQGLCL ANKIMLGDKP
     LPTDEFHPFI VGLAYHVQRA CWYGALASRT FEAFRDFVRT EEERFAQFFG KVCAPINGCV
     YLAYTTGRVT LFSAYQVLNT AIAKSKDAFG GVAAIVVDML KPILEWVLKK MSIAKGAWLP
     YAEGLLALFK AQFTVVKGKF QFLRASLNSK CHSLCDLLTT IMSKLLTSVK WAGCKVDALY
     TGTYYYFSRK GVLTEVQLCA KRLGLLLTPK QQKMEVEVLD GDFDAPVTLT DLELEECTGV
     LEEVFGASDV KLVKGTLVSL ASKLFVRTED GFLYRYVKSG GVLGKAFRLR GGGVSKVTFG
     DEEVHTIPNT VTVNFSYDVC EGLDAILDKV MAPFQVEEGT KLEDLACVVQ KAVYERLSDL
     FSDCPAELRP INLEDFLTSE CFVYSKDYEK ILMPEMYFSL EDAVPVDDEM VDDIEDTVEQ
     ASDSDDQWLG DEGAEDCDNT IQDVDVATSM TTPCGYTKIA EHVYIKCADI VQEARNYSYA
     VLVNAANVNL HHGGGVAGAL NRATNNAMQK ESSEYIKANG SLQPGGHVLL SSHGLASHGI
     LHVVGPDKRL GQDLALLDAV YAAYTGFDSV LTPLVSAGIF GFTVEESLCS LVKNVACTTY
     VVVYDRQLYE RALATSFDVP GPQSSVQHVP AIDWAEAVEV QESIVDQVET PSLGAVDTVD
     SNADSGLNET ARSPENVVGS VPDDVVADVE SCVRDLVRQV VKKVKRDKRP PPIVPQQTVE
     QQPQEISSPG DCNTVLVDVV SMSFSAMVNF GKEKGLLIPV VIDYPAFLKV LKRFSPKEGL
     FSSNGYEFYG YSRDKPLHEV SKDLNSLGRP LIMIPFGFIV NGQTLAVSAV SMRGLTVPHT
     VVVPSESSVP LYRAYFNGVF SGDTTAVQDF VVDILLNGAR DWDVLQTTCT VDRKVYKTIC
     KRGNTYLCFD DTNLYAITGD VVLKFATVSK ARAYLETKLC APEPLIKVLT TVDGINYSTV
     LVSTAQSYRA QIGTVFCDGH DWSNKNPMPT DEGTHLYKQD NFSSAEVTAI REYYGVDDSN
     IIARAMSIRK TVQTWPYTVV DGRVLLAQRD SNCYLNVAIS LLQDIDVSFS TPWVCRAYDA
     LKGGNPLPMA EVLIALGKAT PGVSDDAHMV LSAVLNHGTV TARRVMQTVC EHCGVSQMVF
     TGTDACTFYG SVVLDDLYAP VSVVCQCGRP AIRYVSEQKS PWLLMSCTPT QVPLDTSGIW
     KTAIVFRGPV TAGHYMYAVN GTLISVYDAN TRRRTSDLKL PATDILYGPT SFTSDSKVET
     YYLDGVKRTT IDPDFSKYVK RGDYYFTTAP IEVVAAPKLV TSYDGFYLSS CQNPQLAESF
     NKAINATKTG PMKLLTMYPN VAGDVVAISD DNVVAHPYGS LHMGKPVLFV TRPNTWKKLV
     PLLSTVVVNT PNTYDVLAVD PLPVNNETSE EPISVKAPIP LYGLKATMVL NGTTYVPGNK
     GHLLCLKEFT LTDLQTFYVE GVQPFVLLKA SHLSKVLGLR VSDSSLHVNH LSKGVVYAYA
     ATRLTTRVTT SLLGGLVTRS VRKTADFVRS TNPGSKCVGL LCLFYQLFMR FWLLVKKPPI
     VKVSGIIAYN TGCGVTTCVL NYLRSRCGNI SWSRLLKLLR YMLYIWFVWT CLTICGVWLS
     EPYAPSLVTR FKYFLGIVMP CDYVLVNETG TGWLHHLCMA GMDSLDYPAL RMQQHRYGSP
     YNYTYILMLL EAFFAYLLYT PALPIVGILA VLHLIVLYLP IPLGNSWLVV FLYYIIRLVP
     FTSMLRMYIV IAFLWLCYKG FLHVRYGCNN VACLMCYKKN VAKRIECSTV VNGVKRMFYV
     NANGGTHFCT KHNWNCVSCD TYTVDSTFIC RQVALDLSAQ FKRPIIHTDE AYYEVTSVEV
     RNGYVYCYFE SDGQRSYERF PMDAFTNVSK LHYSELKGAA PAFNVLVFDA TNRIEENAVK
     TAAIYYAQLA CKPILLVDKR MVGVVGDDAT IARAMFEAYA QNYLLKYSIA MDKVKHLYST
     ALQQISSGMT VESVLKVFVG STRAEAKDLE SDVDTNDLVS CIRLCHQEGW EWTTDSWNNL
     VPTYIKQDTL STLEVGQFMT ANAKYVNANI AKGAAVNLIW RYADFIKLSE SMRRQLKVAA
     RKTGLNLLVT TSSLKADVPC MVTPFKIIGG HRRIVSWRRV LIHVFMLLVV LNPQWFTPWY
     IMRPIEYNVV DFKVIDNAVI RDITSADQCF ANKFSAFENW YSNRYGSYVN SRGCPMVVGV
     VSDIVGSLVP GLPARFLRVG TTLLPLVNYG LGAVGSVCYT PHYAINYDVF DTSACVLAAT
     CTLFSSASGE RMPYCADAAL IQNASRYDML KPHVMYPFYE HSGYIRFPEV ISAGVHIVRT
     MAMEYCKVGR CDVSEAGLCM SLQPRWVVNN AYFRQQSGVY CGTSAFDLFM NMLLPIFTPV
     GAVDITTSIL MGALLAVVVS MSLYYLLRFR RAFGDYSGVI FTNILAFVLN VIVLCLEGPY
     PMLPSIYAMV FLYATCYFGS DIACMMHVSF LIMFAGVVPL WVTVLYIVVV LSRHILWFAS
     LCTKRTVQVG DLAFHSFQDA ALQTFMLDKE VFLRLKREIS SDAYFKYLAM YNKYKYYSGP
     MDTAAYREAA CSHLVMALEK YSNGGGDTIY QPPRCSVASA ALQAGLTRMA HPSGLVEPCL
     VKVNYGSMTL NGIWLDNFVI CPRHVMCSRD ELANPDYPRL SMRAANYDFH VSQNGHNIRV
     IGHTMEGSLL KLTVDVNNPK TPAYSFIRVS TGQAMSLLAC YDGLPTGVYT CTLRSNGTMR
     ASFLCGSCGS PGFVMNGKEV QFCYLHQLEL PNGTHTGTDF SGVFYGPFED KQVPQLAAPD
     CTITVNVLAW LYAAVLSGEN WFLTKSSISP AEFNNCAVKY MCQSVTSESL QVLQPLAAKT
     GISVERMLSA LKVLLSAGFC GRTIMGSCSL EDEHTPYDIG RQMLGVKLQG KFQSMFRWTL
     QWFAIIFVLT ILILLQLAQW TFVGALPFTL LLPLIGFVAV CVGFVSLLIK HKHTYLTVYL
     LPVAMVTAYY NFQYTPEGVQ GYLLSLYNYV NPGRIDVIGT DLLTMLIISV ACTLLSVRMV
     RTDAYSRIWY VCTAVGWLYN CWTGSADTVA ISYLTFMVSV FTNYTGVACA SLYAAQFMVW
     VLKFLDPTIL LLYGRFRCVL VCYLLVGYLC TCYFGVFNLI NRLFRCTLGN YEYVVSSQEL
     RYMNSHGLLP PTNSWQALML NIKLAGIGGI PIYRVSTIQS NMTDLKCTSV VLLSVLQQLR
     VESSSKLWAL CVKLHNEILA SNSPTEAFEA FVSLLSVLLS LPGAINLDEL CSSILENNSV
     LQAVASEFSN LSSYVDYENA QKAYDTAVAT GAPASTVNAL KKAMNVAKSV LDKDVATTRK
     LERMSELAMT AMYKQARAED RRSKVTAAMQ TMLFNMIRRL DSDALSNILN NARNGVVPLG
     VIPRTAANKL LLVVPDFSVY TATITMPTLT YAGSAWDVMQ VADADGKTVN ATDITRENSV
     NLAWPLVVTA QRQQATSPVK LQNNELMPQT VKRMNVVAGV SQTACVTDAV AYYNATKEGR
     HVMAILADTD GLAFAKVEKS TGDGFVILEL EPPCKFMVDT PKGPALKYLY FTKGLKNLCR
     GTVLGTLACT VRLHAGSATE VASNSSILSL CSFSVDPEAT YKDYLDNGGS PIGNCVKMLT
     PHTGTGLAIT AKPDANIDQE SFGGASCCLY CRCHIEHPGA SGVCKYKGKF VQIPLVGVND
     PIGFCIRNVV CAVCNMWQGY GCPCSSLREI NLQARDECFL NESGVLVE
//