ID   R1A_CVPPU               Reviewed;        4017 AA.
AC   P0C6V2; Q9IW06;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   08-NOV-2023, entry version 95.
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=p9;
DE   Contains:
DE     RecName: Full=Non-structural protein 2;
DE              Short=nsp2;
DE     AltName: Full=p87;
DE   Contains:
DE     RecName: Full=Non-structural protein 3;
DE              Short=nsp3;
DE              EC=3.4.19.12;
DE              EC=3.4.22.-;
DE     AltName: Full=PL1-PRO/PL2-PRO;
DE     AltName: Full=PLP1/PLP2;
DE     AltName: Full=Papain-like proteinases 1/2;
DE     AltName: Full=p195;
DE   Contains:
DE     RecName: Full=Non-structural protein 4;
DE              Short=nsp4;
DE     AltName: Full=Peptide HD2;
DE   Contains:
DE     RecName: Full=3C-like proteinase;
DE              Short=3CL-PRO;
DE              Short=3CLp;
DE              EC=3.4.22.-;
DE     AltName: Full=M-PRO;
DE     AltName: Full=nsp5;
DE     AltName: Full=p34;
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     AltName: Full=p5;
DE   Contains:
DE     RecName: Full=Non-structural protein 8;
DE              Short=nsp8;
DE     AltName: Full=p23;
DE   Contains:
DE     RecName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE     AltName: Full=p12;
DE   Contains:
DE     RecName: Full=Non-structural protein 10;
DE              Short=nsp10;
DE     AltName: Full=Growth factor-like peptide;
DE              Short=GFL;
DE     AltName: Full=p14;
DE   Contains:
DE     RecName: Full=Non-structural protein 11;
DE              Short=nsp11;
GN   ORFNames=1a;
OS   Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Tegacovirus; Alphacoronavirus 1.
OX   NCBI_TaxID=11151;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate Purdue-115;
RX   PubMed=7856095; DOI=10.1006/viro.1995.1004;
RA   Eleouet J., Rasschaert D., Lambert P., Levy L., Vende P., Laude H.;
RT   "Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of
RT   transmissible gastroenteritis virus.";
RL   Virology 206:817-822(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate PUR46-MAD;
RX   PubMed=10805807; DOI=10.1073/pnas.97.10.5516;
RA   Almazan F., Gonzalez J.M., Penzes Z., Izeta A., Calvo E., Plana-Duran J.,
RA   Enjuanes L.;
RT   "Engineering the largest RNA virus genome as an infectious bacterial
RT   artificial chromosome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:5516-5521(2000).
RN   [3]
RP   PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC   STRAIN=Isolate Purdue-115;
RX   PubMed=11842254; DOI=10.1099/0022-1317-83-3-595;
RA   Hegyi A., Ziebuhr J.;
RT   "Conservation of substrate specificities among coronavirus main
RT   proteases.";
RL   J. Gen. Virol. 83:595-599(2002).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 2879-3180.
RX   PubMed=12093723; DOI=10.1093/emboj/cdf327;
RA   Anand K., Palm G.J., Mesters J.R., Siddell S.G., Ziebuhr J., Hilgenfeld R.;
RT   "Structure of coronavirus main proteinase reveals combination of a
RT   chymotrypsin fold with an extra alpha-helical domain.";
RL   EMBO J. 21:3213-3224(2002).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 2879-3180 COMPLEXED WITH THE
RP   SUBSTRATE-ANALOG HEXAPEPTIDYL CMK.
RX   PubMed=12746549; DOI=10.1126/science.1085658;
RA   Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.;
RT   "Coronavirus main proteinase (3CLpro) structure: basis for design of anti-
RT   SARS drugs.";
RL   Science 300:1763-1767(2003).
CC   -!- FUNCTION: The papain-like proteinase 1 (PLP1) and papain-like
CC       proteinase 2 (PLP2) are responsible for the cleavages located at the N-
CC       terminus of the replicase polyprotein. In addition, PLP2 possesses a
CC       deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC       'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2
CC       also antagonizes innate immune induction of type I interferon by
CC       blocking the nuclear translocation of host IRF-3 (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: [3C-like proteinase]: 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       [SAGC]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC       CMK.
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: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
CC   -!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of nsp7
CC       and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is
CC       a dimer. Nsp10 forms a dodecamer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: 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 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=P0C6V2-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6Y5-1; 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.
CC   -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC       mature proteins. 3CL-PRO is autocatalytically processed.
CC       {ECO:0000269|PubMed:11842254}.
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; Z34093; CAA83979.1; -; mRNA.
DR   EMBL; AJ271965; CAB91144.1; -; Genomic_RNA.
DR   PDB; 1LVO; X-ray; 1.96 A; A/B/C/D/E/F=2879-3180.
DR   PDB; 1P9U; X-ray; 2.37 A; A/B/C/D/E/F=2879-3180.
DR   PDB; 2AMP; X-ray; 2.70 A; A/B=2879-3180.
DR   PDB; 3MP2; X-ray; 2.50 A; A=1071-1281.
DR   PDB; 3ZBD; X-ray; 1.49 A; A/B=1-105.
DR   PDB; 4F49; X-ray; 2.25 A; A/B/C/D=2879-3181.
DR   PDB; 6IVD; X-ray; 1.98 A; A/B=1-105.
DR   PDBsum; 1LVO; -.
DR   PDBsum; 1P9U; -.
DR   PDBsum; 2AMP; -.
DR   PDBsum; 3MP2; -.
DR   PDBsum; 3ZBD; -.
DR   PDBsum; 4F49; -.
DR   PDBsum; 6IVD; -.
DR   SMR; P0C6V2; -.
DR   MEROPS; C30.004; -.
DR   BRENDA; 3.4.22.66; 4985.
DR   BRENDA; 3.4.22.B14; 4985.
DR   EvolutionaryTrace; P0C6V2; -.
DR   Proteomes; UP000001440; Segment.
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:0008242; F:omega peptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   CDD; cd21901; alpha_betaCoV_Nsp10; 1.
DR   CDD; cd21558; alphaCoV-Nsp6; 1.
DR   CDD; cd21514; alphaCoV_Nsp2_HCoV-229E-like; 1.
DR   CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR   CDD; cd21826; alphaCoV_Nsp7; 1.
DR   CDD; cd21830; alphaCoV_Nsp8; 1.
DR   CDD; cd21897; alphaCoV_Nsp9; 1.
DR   CDD; cd21731; alphaCoV_PLPro; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21687; TGEV-like_alphaCoV_Nsp1; 1.
DR   CDD; cd21712; TM_Y_alphaCoV_Nsp3_C; 1.
DR   Gene3D; 1.10.8.1190; -; 2.
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; 1.10.8.370; nsp7 replicase; 1.
DR   Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR   Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR   Gene3D; 2.30.30.1000; Replicase polyprotein 1a; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR032039; A-CoV_nsp1.
DR   InterPro; IPR038634; A-CoV_nsp1_sf.
DR   InterPro; IPR046443; a/bCoV_NSP1_glob.
DR   InterPro; IPR043613; CoV_NSP2_C.
DR   InterPro; IPR047573; CoV_NSP2_M.
DR   InterPro; IPR043611; CoV_NSP3_C.
DR   InterPro; IPR047566; CoV_NSP3_Y3.
DR   InterPro; IPR032505; CoV_NSP4_C.
DR   InterPro; IPR043612; CoV_NSP4_N.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR044371; Macro_X_NSP3-like.
DR   InterPro; IPR036333; NSP10_sf_CoV.
DR   InterPro; IPR044385; NSP2_HCoV-229E-like.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR   InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR   InterPro; IPR038123; NSP4_C_sf_CoV.
DR   InterPro; IPR044309; NSP5_Mpro_alphaCoV.
DR   InterPro; IPR044369; NSP6_alphaCoV.
DR   InterPro; IPR043610; NSP6_CoV.
DR   InterPro; IPR014828; NSP7_CoV.
DR   InterPro; IPR037204; NSP7_sf_CoV.
DR   InterPro; IPR014829; NSP8_CoV.
DR   InterPro; IPR037230; NSP8_sf_CoV.
DR   InterPro; IPR014822; NSP9_CoV.
DR   InterPro; IPR036499; NSP9_sf_CoV.
DR   InterPro; 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; IPR043178; PLpro_thumb_sf_CoV.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   Pfam; PF16688; CNV-Replicase_N; 1.
DR   Pfam; PF09401; CoV_NSP10; 1.
DR   Pfam; PF19212; CoV_NSP2_C; 2.
DR   Pfam; PF19211; CoV_NSP2_N; 1.
DR   Pfam; PF19218; CoV_NSP3_C; 1.
DR   Pfam; PF16348; CoV_NSP4_C; 1.
DR   Pfam; PF19217; CoV_NSP4_N; 1.
DR   Pfam; PF19213; CoV_NSP6; 1.
DR   Pfam; PF08716; CoV_NSP7; 1.
DR   Pfam; PF08717; CoV_NSP8; 1.
DR   Pfam; PF08710; CoV_NSP9; 1.
DR   Pfam; PF08715; CoV_peptidase; 2.
DR   Pfam; PF01661; Macro; 1.
DR   Pfam; PF05409; Peptidase_C30; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF144246; Coronavirus NSP10-like; 2.
DR   SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR   SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF101816; Replicase NSP9; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; Disulfide bond;
KW   Host cytoplasm; Host membrane; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW   Membrane; Metal-binding;
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; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..4017
FT                   /note="Replicase polyprotein 1a"
FT                   /id="PRO_0000338302"
FT   CHAIN           1..110
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338303"
FT   CHAIN           111..879
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338304"
FT   CHAIN           880..2388
FT                   /note="Non-structural protein 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338305"
FT   CHAIN           2389..2878
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338306"
FT   CHAIN           2879..3180
FT                   /note="3C-like proteinase"
FT                   /id="PRO_0000338307"
FT   CHAIN           3181..3474
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338308"
FT   CHAIN           3475..3557
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338309"
FT   CHAIN           3558..3752
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338310"
FT   CHAIN           3753..3863
FT                   /note="Non-structural protein 9"
FT                   /id="PRO_0000338311"
FT   CHAIN           3864..3998
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338312"
FT   CHAIN           3999..4017
FT                   /note="Non-structural protein 11"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338313"
FT   TRANSMEM        1896..1916
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1995..2015
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2033..2053
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2401..2421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2467..2487
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2497..2517
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2538..2558
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2666..2686
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2695..2715
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2721..2741
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2746..2766
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3187..3207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3217..3237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3242..3262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3280..3300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3313..3333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3347..3367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3371..3391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3394..3414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2..108
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          111..349
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          378..773
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          768..879
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          882..983
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1055..1299
FT                   /note="Peptidase C16 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1318..1489
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1486..1542
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1550..1803
FT                   /note="Peptidase C16 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1905..1970
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2044..2384
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          2783..2878
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          2879..3180
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3475..3557
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3558..3752
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          3753..3863
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          3864..4004
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   ZN_FING         1164..1195
FT                   /note="C4-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         1667..1696
FT                   /note="C4-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         3937..3953
FT                   /evidence="ECO:0000250"
FT   ZN_FING         3979..3992
FT                   /evidence="ECO:0000250"
FT   REGION          240..260
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          989..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1896..2053
FT                   /note="HD1"
FT   REGION          2044..2134
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2048..2061
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2094..2104
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2135..2384
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2135..2224
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2225..2281
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2282..2384
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2401..2766
FT                   /note="HD2"
FT   REGION          3187..3414
FT                   /note="HD3"
FT   COMPBIAS        994..1015
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1032
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1093
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1244
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1257
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1588
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1741
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1754
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        2919
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3022
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1667
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1670
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1694
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1696
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2048
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2053
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2058
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2061
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2094
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2097
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         3937
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3940
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3946
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3953
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3979
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3982
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3990
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3992
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   SITE            110..111
FT                   /note="Cleavage; by PL1-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            879..880
FT                   /note="Cleavage; by PL1-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            2388..2389
FT                   /note="Cleavage; by PL2-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            2878..2879
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3180..3181
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3474..3475
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3557..3558
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3752..3753
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3863..3864
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3998..3999
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   DISULFID        1921..1948
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        1939..1945
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   VARIANT         572
FT                   /note="F -> S (in strain: Isolate Purdue-115)"
FT   VARIANT         1041
FT                   /note="E -> D (in strain: Isolate Purdue-115)"
FT   VARIANT         2375
FT                   /note="P -> T (in strain: Isolate Purdue-115)"
FT   VARIANT         2381
FT                   /note="E -> Q (in strain: Isolate Purdue-115)"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:3ZBD"
FT   HELIX           23..36
FT                   /evidence="ECO:0007829|PDB:3ZBD"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:3ZBD"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:3ZBD"
FT   STRAND          59..75
FT                   /evidence="ECO:0007829|PDB:3ZBD"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:3ZBD"
FT   STRAND          96..104
FT                   /evidence="ECO:0007829|PDB:3ZBD"
FT   STRAND          1077..1080
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1083..1086
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   HELIX           1093..1102
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   HELIX           1111..1116
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   TURN            1117..1119
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   HELIX           1122..1132
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   HELIX           1142..1150
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1156..1164
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1167..1180
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1183..1185
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1187..1191
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   TURN            1193..1195
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1198..1217
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   HELIX           1223..1225
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1226..1228
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1231..1238
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   TURN            1240..1242
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1244..1249
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   TURN            1250..1253
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1254..1257
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1260..1262
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   STRAND          1269..1280
FT                   /evidence="ECO:0007829|PDB:3MP2"
FT   TURN            2889..2891
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           2892..2894
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2895..2900
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2903..2910
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2913..2917
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           2918..2921
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           2931..2936
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           2940..2942
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2943..2948
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2950..2952
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2954..2960
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2963..2970
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2988..2995
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          2998..3006
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          3025..3030
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          3033..3043
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          3049..3052
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           3059..3061
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           3078..3090
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           3104..3111
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   TURN            3112..3115
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           3123..3125
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           3126..3132
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           3136..3146
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   STRAND          3158..3160
FT                   /evidence="ECO:0007829|PDB:4F49"
FT   HELIX           3167..3175
FT                   /evidence="ECO:0007829|PDB:4F49"
SQ   SEQUENCE   4017 AA;  447352 MW;  97ED2B170C4FD248 CRC64;
     MSSKQFKILV NEDYQVNVPS LPIRDVLQEI KYCYRNGFEG YVFVPEYCRD LVDCDRKDHY
     VIGVLGNGVS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF DLKIARTGRG AIYVDQYMCG
     ADGKPVIEGD FKDYFGDEDI IEFEGEEYHC AWTTVRDEKP LNQQTLFTIQ EIQYNLDIPH
     KLPNCATRHV APPVKKNSKI VLSEDYKKLY DIFGSPFMGN GDCLSKCFDT LHFIAATLRC
     PCGSESSGVG DWTGFKTACC GLSGKVKGVT LGDIKPGDAV VTSMSAGKGV KFFANCVLQY
     AGDVEGVSIW KVIKTFTVDE TVCTPGFEGE LNDFIKPESK SLVACSVKRA FITGDIDDAV
     HDCIITGKLD LSTNLFGNVG LLFKKTPWFV QKCGALFVDA WKVVEELCGS LTLTYKQIYE
     VVASLCTSAF TIVNYKPTFV VPDNRVKDLV DKCVKVLVKA FDVFTQIITI AGIEAKCFVL
     GAKYLLFNNA LVKLVSVKIL GKKQKGLECA FFATSLVGAT VNVTPKRTET ATISLNKVDD
     VVAPGEGYIV IVGDMAFYKS GEYYFMMSSP NFVLTNNVFK AVKVPSYDIV YDVDNDTKSK
     MIAKLGSSFE YDGDIDAAIV KVNELLIEFR QQSLCFRAFK DDKSIFVEAY FKKYKMPACL
     AKHIGLWNII KKDSCKRGFL NLFNHLNELE DIKETNIQAI KNILCPDPLL DLDYGAIWYN
     CMPGCSDPSV LGSVQLLIGN GVKVVCDGCK GFANQLSKGY NKLCNAARND IEIGGIPFST
     FKTPTNTFIE MTDAIYSVIE QGKALSFRDA DVPVVDNGTI STADWSEPIL LEPAEYVKPK
     NNGNVIVIAG YTFYKDEDEH FYPYGFGKIV QRMYNKMGGG DKTVSFSEEV DVQEIAPVTR
     VKLEFEFDNE IVTGVLERAI GTRYKFTGTT WEEFEESISE ELDAIFDTLA NQGVELEGYF
     IYDTCGGFDI KNPDGIMISQ YDINITADEK SEVSASSEEE EVESVEEDPE NEIVEASEGA
     EGTSSQEEVE TVEVADITST EEDVDIVEVS AKDDPWAAAV DVQEAEQFNP SLPPFKTTNL
     NGKIILKQGD NNCWINACCY QLQAFDFFNN EAWEKFKKGD VMDFVNLCYA ATTLARGHSG
     DAEYLLELML NDYSTAKIVL AAKCGCGEKE IVLERAVFKL TPLKESFNYG VCGDCMQVNT
     CRFLSVEGSG VFVHDILSKQ TPEAMFVVKP VMHAVYTGTT QNGHYMVDDI EHGYCVDGMG
     IKPLKKRCYT STLFINANVM TRAEKPKQEF KVEKVEQQPI VEENKSSIEK EEIQSPKNDD
     LILPFYKAGK LSFYQGALDV LINFLEPDVI VNAANGDLKH MGGVARAIDV FTGGKLTERS
     KDYLKKNKSI APGNAVFFEN VIEHLSVLNA VGPRNGDSRV EAKLCNVYKA IAKCEGKILT
     PLISVGIFNV RLETSLQCLL KTVNDRGLNV FVYTDQERQT IENFFSCSIP VNVTEDNVNH
     ERVSVSFDKT YGEQLKGTVV IKDKDVTNQL PSAFDVGQKV IKAIDIDWQA HYGFRDAAAF
     SASSHDAYKF EVVTHSNFIV HKQTDNNCWI NAICLALQRL KPQWKFPGVR GLWNEFLERK
     TQGFVHMLYH ISGVKKGEPG DAELMLHKLG DLMDNDCEII VTHTTACDKC AKVEKFVGPV
     VAAPLAIHGT DETCVHGVSV NVKVTQIKGT VAITSLIGPI IGEVLEATGY ICYSGSNRNG
     HYTYYDNRNG LVVDAEKAYH FNRDLLQVTT AIASNFVVKK PQAEERPKNC AFNKVAASPK
     IVQEQKLLAI ESGANYALTE FGRYADMFFM AGDKILRLLL EVFKYLLVLF MCLRSTKMPK
     VKVKPPLAFK DFGAKVRTLN YMRQLNKPSV WRYAKLVLLL IAIYNFFYLF VSIPVVHKLT
     CNGAVQAYKN SSFIKSAVCG NSILCKACLA SYDELADFQH LQVTWDFKSD PLWNRLVQLS
     YFAFLAVFGN NYVRCFLMYF VSQYLNLWLS YFGYVEYSWF LHVVNFESIS AEFVIVVIVV
     KAVLALKHIV FACSNPSCKT CSRTARQTRI PIQVVVNGSM KTVYVHANGT GKFCKKHNFY
     CKNCDSYGFE NTFICDEIVR DLSNSVKQTV YATDRSHQEV TKVECSDGFY RFYVGDEFTS
     YDYDVKHKKY SSQEVLKSML LLDDFIVYSP SGSALANVRN ACVYFSQLIG KPIKIVNSDL
     LEDLSVDFKG ALFNAKKNVI KNSFNVDVSE CKNLDECYRA CNLNVSFSTF EMAVNNAHRF
     GILITDRSFN NFWPSKVKPG SSGVSAMDIG KCMTSDAKIV NAKVLTQRGK SVVWLSQDFA
     ALSSTAQKVL VKTFVEEGVN FSLTFNAVGS DDDLPYERFT ESVSPKSGSG FFDVITQLKQ
     IVILVFVFIF ICGLCSVYSV ATQSYIESAE GYDYMVIKNG IVQPFDDTIS CVHNTYKGFG
     DWFKAKYGFI PTFGKSCPIV VGTVFDLENM RPIPDVPAYV SIVGRSLVFA INAAFGVTNM
     CYDHTGNAVS KDSYFDTCVF NTACTTLTGL GGTIVYCAKQ GLVEGAKLYS DLMPDYYYEH
     ASGNMVKLPA IIRGLGLRFV KTQATTYCRV GECIDSKAGF CFGGDNWFVY DNEFGNGYIC
     GNSVLGFFKN VFKLFNSNMS VVATSGAMLV NIIIACLAIA MCYGVLKFKK IFGDCTFLIV
     MIIVTLVVNN VSYFVTQNTF FMIIYAIVYY FITRKLAYPG ILDAGFIIAY INMAPWYVIT
     AYILVFLYDS LPSLFKLKVS TNLFEGDKFV GNFESAAMGT FVIDMRSYET IVNSTSIARI
     KSYANSFNKY KYYTGSMGEA DYRMACYAHL GKALMDYSVN RTDMLYTPPT VSVNSTLQSG
     LRKMAQPSGL VEPCIVRVSY GNNVLNGLWL GDEVICPRHV IASDTTRVIN YENEMSSVRL
     HNFSVSKNNV FLGVVSARYK GVNLVLKVNQ VNPNTPEHKF KSIKAGESFN ILACYEGCPG
     SVYGVNMRSQ GTIKGSFIAG TCGSVGYVLE NGILYFVYMH HLELGNGSHV GSNFEGEMYG
     GYEDQPSMQL EGTNVMSSDN VVAFLYAALI NGERWFVTNT SMSLESYNTW AKTNSFTELS
     STDAFSMLAA KTGQSVEKLL DSIVRLNKGF GGRTILSYGS LCDEFTPTEV IRQMYGVNLQ
     AGKVKSFFYP IMTAMTILFA FWLEFFMYTP FTWINPTFVS IVLAVTTLIS TVFVSGIKHK
     MLFFMSFVLP SVILVTAHNL FWDFSYYESL QSIVENTNTM FLPVDMQGVM LTVFCFIVFV
     TYSVRFFTCK QSWFSLAVTT ILVIFNMVKI FGTSDEPWTE NQIAFCFVNM LTMIVSLTTK
     DWMVVIASYR IAYYIVVCVM PSAFVSDFGF MKCISIVYMA CGYLFCCYYG ILYWVNRFTC
     MTCGVYQFTV SAAELKYMTA NNLSAPKNAY DAMILSAKLI GVGGKRNIKI STVQSKLTEM
     KCTNVVLLGL LSKMHVESNS KEWNYCVGLH NEINLCDDPE IVLEKLLALI AFFLSKHNTC
     DLSELIESYF ENTTILQSVA SAYAALPSWI ALEKARADLE EAKKNDVSPQ ILKQLTKAFN
     IAKSDFEREA SVQKKLDKMA EQAAASMYKE ARAVDRKSKI VSAMHSLLFG MLKKLDMSSV
     NTIIDQARNG VLPLSIIPAA SATRLVVITP SLEVFSKIRQ ENNVHYAGAI WTIVEVKDAN
     GSHVHLKEVT AANELNLTWP LSITCERTTK LQNNEIMPGK LKERAVRASA TLDGEAFGSG
     KALMASESGK SFMYAFIASD NNLKYVKWES NNDIIPIELE APLRFYVDGA NGPEVKYLYF
     VKNLNTLRRG AVLGYIGATV RLQAGKPTEH PSNSSLLTLC AFSPDPAKAY VDAVKRGMQP
     VNNCVKMLSN GAGNGMAVTN GVEANTQQDS YGGASVCIYC RCHVEHPAID GLCRYKGKFV
     QIPTGTQDPI RFCIENEVCV VCGCWLNNGC MCDRTSMQSF TVDQSYLNEC GVLVQLD
//