ID   R1AB_CVPPU              Reviewed;        6684 AA.
AC   P0C6Y5; Q88508; Q9IW05; Q9IW06;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Replicase polyprotein 1ab;
DE            Short=pp1ab;
DE   AltName: Full=ORF1ab 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=Viral protein genome-linked nsp9;
DE     AltName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE     AltName: Full=RNA-capping enzyme subunit 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=RNA-directed RNA polymerase nsp12;
DE              Short=Pol;
DE              Short=RdRp;
DE              EC=2.7.7.48;
DE              EC=2.7.7.50;
DE     AltName: Full=nsp12;
DE     AltName: Full=p100;
DE   Contains:
DE     RecName: Full=Helicase;
DE              Short=Hel;
DE              EC=3.6.4.12;
DE              EC=3.6.4.13;
DE     AltName: Full=nsp13;
DE     AltName: Full=p66;
DE     AltName: Full=p66-HEL;
DE   Contains:
DE     RecName: Full=Exoribonuclease;
DE              Short=ExoN;
DE              EC=3.1.13.-;
DE     AltName: Full=nsp14;
DE   Contains:
DE     RecName: Full=Uridylate-specific endoribonuclease;
DE              EC=4.6.1.-;
DE     AltName: Full=NendoU;
DE     AltName: Full=nsp15;
DE     AltName: Full=p41;
DE   Contains:
DE     RecName: Full=Putative 2'-O-methyl transferase;
DE              EC=2.1.1.57;
DE     AltName: Full=nsp16;
GN   Name=rep; ORFNames=1a-1b;
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] (ORF1A).
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   FUNCTION OF NSP1.
RX   PubMed=21047955; DOI=10.1128/jvi.01806-10;
RA   Huang C., Lokugamage K.G., Rozovics J.M., Narayanan K., Semler B.L.,
RA   Makino S.;
RT   "Alphacoronavirus transmissible gastroenteritis virus nsp1 protein
RT   suppresses protein translation in mammalian cells and in cell-free HeLa
RT   cell extracts but not in rabbit reticulocyte lysate.";
RL   J. Virol. 85:638-643(2011).
RN   [5]
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   [6]
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 replicase polyprotein of coronaviruses is a
CC       multifunctional protein: it contains the activities necessary for the
CC       transcription of negative stranded RNA, leader RNA, subgenomic mRNAs
CC       and progeny virion RNA as well as proteinases responsible for the
CC       cleavage of the polyprotein into functional products.
CC       {ECO:0000269|PubMed:21047955}.
CC   -!- FUNCTION: Non-structural protein 1 inhibits host translation. By
CC       suppressing host gene expression, nsp1 facilitates efficient viral gene
CC       expression in infected cells and evasion from host immune response.
CC       {ECO:0000269|PubMed:21047955}.
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. {ECO:0000269|PubMed:21047955}.
CC   -!- FUNCTION: The helicase which contains a zinc finger structure displays
CC       RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase
CC       activity is strongly stimulated by poly(U), poly(dT), poly(C),
CC       poly(dA), but not by poly(G). {ECO:0000269|PubMed:21047955}.
CC   -!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3' to
CC       5' direction. {ECO:0000250}.
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: [Viral protein genome-linked nsp9]: Forms a primer, NSP9-pU,
CC       which is utilized by the polymerase for the initiation of RNA chains.
CC       Interacts with ribosome signal recognition particle RNA (SRP). Together
CC       with NSP8, suppress protein integration into the cell membrane, thereby
CC       disrupting host immune defenses. {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase nsp12]: RNA-directed RNA
CC       polymerase that catalyzes the transcription of viral genomic and
CC       subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both
CC       the minus and positive strands of genomic RNA. The kinase-like NiRAN
CC       domain of NSP12 attaches one or more nucleotides to the amino terminus
CC       of NSP9, forming a covalent RNA-protein intermediate that serves as
CC       transcription/replication primer. Subgenomic RNAs (sgRNAs) are formed
CC       by discontinuous transcription: The polymerase has the ability to pause
CC       at transcription-regulating sequences (TRS) and jump to the leader TRS,
CC       resulting in a major deletion. This creates a series of subgenomic RNAs
CC       that are replicated, transcribed and translated. In addition, Nsp12 is
CC       a subunit of the viral RNA capping enzyme that catalyzes the RNA
CC       guanylyltransferase reaction for genomic and sub-genomic RNAs.
CC       Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core
CC       cap structure GpppA-RNA. {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- FUNCTION: [Uridylate-specific endoribonuclease]: Plays a role in viral
CC       transcription/replication and prevents the simultaneous activation of
CC       host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By
CC       similarity). Acts by degrading the 5'-polyuridines generated during
CC       replication of the poly(A) region of viral genomic and subgenomic RNAs.
CC       Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-
CC       cP) is first generated by 2'-O transesterification, which is then
CC       hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded,
CC       poly(U) RNA would hybridize with poly(A) RNA tails and activate host
CC       dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- CATALYTIC ACTIVITY: [Non-structural protein 3]:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48;
CC   -!- CATALYTIC ACTIVITY: [Helicase]:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- CATALYTIC ACTIVITY: [Helicase]:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]:
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:P0DTD1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC         Evidence={ECO:0000250|UniProtKB:P0DTD1};
CC   -!- CATALYTIC ACTIVITY: [Putative 2'-O-methyl transferase]:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC         Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC         EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC   -!- CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease]:
CC       Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC         2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC         RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC         COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC         ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC   -!- COFACTOR: [Uridylate-specific endoribonuclease]:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC       Note=Likely affects Nsp15 binding to RNA.
CC       {ECO:0000250|UniProtKB:P0C6X7};
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   -!- INTERACTION:
CC       PRO_0000037392; PRO_0000037393 [P0C6Y5]: rep; NbExp=2; IntAct=EBI-26366034, EBI-25684354;
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: [Viral protein genome-linked 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   -!- SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi
CC       intermediate compartment {ECO:0000305}. Note=The helicase interacts
CC       with the N protein in membranous complexes and colocalizes with sites
CC       of synthesis of new viral RNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
CC       cytoplasm, host perinuclear region {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6Y5-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6V2-1; 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 1ab]: Produced by -1
CC       ribosomal frameshifting at the 1a-1b genes boundary.
CC   -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC       {ECO:0000305}.
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DR   EMBL; Z34093; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AJ271965; CAB91143.1; ALT_SEQ; 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; 6IVC; X-ray; 1.80 A; A/B/E/F=1-109.
DR   PDBsum; 1LVO; -.
DR   PDBsum; 1P9U; -.
DR   PDBsum; 2AMP; -.
DR   PDBsum; 6IVC; -.
DR   SMR; P0C6Y5; -.
DR   IntAct; P0C6Y5; 7.
DR   MEROPS; C30.004; -.
DR   EvolutionaryTrace; P0C6Y5; -.
DR   Proteomes; UP000001440; Segment.
DR   GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
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:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase 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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; 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; cd21409; 1B_cv_Nsp13-like; 1.
DR   CDD; cd21901; alpha_betaCoV_Nsp10; 1.
DR   CDD; cd21558; alphaCoV-Nsp6; 1.
DR   CDD; cd21723; alphaCoV_Nsp13-helicase; 1.
DR   CDD; cd21660; alphaCoV_Nsp14; 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; cd21588; alphaCoV_RdRp; 1.
DR   CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR   CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1.
DR   CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR   CDD; cd21687; TGEV-like_alphaCoV_Nsp1; 1.
DR   CDD; cd21712; TM_Y_alphaCoV_Nsp3_C; 1.
DR   CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR   Gene3D; 1.10.8.1190; -; 2.
DR   Gene3D; 3.10.20.540; -; 1.
DR   Gene3D; 3.40.50.11580; -; 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; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR   Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR   Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR032039; A-CoV_nsp1.
DR   InterPro; IPR038634; A-CoV_nsp1_sf.
DR   InterPro; IPR046443; a/bCoV_NSP1_glob.
DR   InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR   InterPro; IPR043608; CoV_NSP15_M.
DR   InterPro; IPR043606; CoV_NSP15_N.
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; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR037227; EndoU-like.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR044371; Macro_X_NSP3-like.
DR   InterPro; IPR046435; N7_MTase_CoV.
DR   InterPro; IPR043609; NendoU_nidovirus.
DR   InterPro; IPR044863; NIRAN.
DR   InterPro; IPR046438; NIV_2_O_MTASE.
DR   InterPro; IPR046436; NIV_EXON.
DR   InterPro; IPR036333; NSP10_sf_CoV.
DR   InterPro; IPR047570; NSP12_IF_CoV.
DR   InterPro; IPR044343; NSP13_1B_dom_CoV.
DR   InterPro; IPR047912; Nsp13_helicase_alphaCoV.
DR   InterPro; IPR048673; NSP13_stalk_CoV.
DR   InterPro; IPR048672; NSP13_ZBD_CoV.
DR   InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR   InterPro; IPR044313; NSP14_alphaCoV.
DR   InterPro; IPR009466; NSP14_CoV.
DR   InterPro; IPR044330; NSP15_alpha_betaCoV_N.
DR   InterPro; IPR044322; NSP15_M_alpha_beta_CoV.
DR   InterPro; IPR043174; NSP15_middle_sf.
DR   InterPro; IPR042515; NSP15_N_CoV.
DR   InterPro; IPR044401; NSP15_NendoU_CoV.
DR   InterPro; IPR009461; NSP16_CoV-like.
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; IPR027417; P-loop_NTPase.
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; IPR044356; RdRp_alphaCoV.
DR   InterPro; IPR046441; RdRp_CoV.
DR   InterPro; IPR009469; RdRp_N_CoV.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF13245; AAA_19; 1.
DR   Pfam; PF16688; CNV-Replicase_N; 1.
DR   Pfam; PF06471; CoV_ExoN; 1.
DR   Pfam; PF06460; CoV_Methyltr_2; 1.
DR   Pfam; PF09401; CoV_NSP10; 1.
DR   Pfam; PF20631; CoV_NSP13_1B; 1.
DR   Pfam; PF20633; CoV_NSP13_stalk; 1.
DR   Pfam; PF20632; CoV_NSP13_ZBD; 1.
DR   Pfam; PF19215; CoV_NSP15_C; 1.
DR   Pfam; PF19216; CoV_NSP15_M; 1.
DR   Pfam; PF19219; CoV_NSP15_N; 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; PF06478; CoV_RPol_N; 1.
DR   Pfam; PF01661; Macro; 1.
DR   Pfam; PF05409; Peptidase_C30; 1.
DR   Pfam; PF00680; RdRP_1; 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; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF142877; EndoU-like; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF101816; Replicase NSP9; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR   PROSITE; PS51993; COV_3ECTO; 1.
DR   PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR   PROSITE; PS51954; COV_N7_MTASE; 1.
DR   PROSITE; PS51962; COV_NSP1; 1.
DR   PROSITE; PS52000; COV_NSP12_IF; 1.
DR   PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR   PROSITE; PS51960; COV_NSP15_NTD; 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; PS51653; CV_ZBD; 1.
DR   PROSITE; PS51442; M_PRO; 1.
DR   PROSITE; PS51154; MACRO; 1.
DR   PROSITE; PS51958; NENDOU; 1.
DR   PROSITE; PS51947; NIRAN; 1.
DR   PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR   PROSITE; PS51953; NIV_EXON; 1.
DR   PROSITE; PS51124; PEPTIDASE_C16; 2.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Disulfide bond; Endonuclease; Exonuclease; Helicase; Host cytoplasm;
KW   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   Lyase; Membrane; Metal-binding; Methyltransferase;
KW   Modulation of host ubiquitin pathway by viral deubiquitinase;
KW   Modulation of host ubiquitin pathway by virus; Nuclease;
KW   Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW   Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW   Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..110
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037386"
FT   CHAIN           111..879
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037387"
FT   CHAIN           880..2388
FT                   /note="Non-structural protein 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037388"
FT   CHAIN           2389..2878
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037389"
FT   CHAIN           2879..3180
FT                   /note="3C-like proteinase"
FT                   /id="PRO_0000037390"
FT   CHAIN           3181..3474
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037391"
FT   CHAIN           3475..3557
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037392"
FT   CHAIN           3558..3752
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037393"
FT   CHAIN           3753..3863
FT                   /note="Viral protein genome-linked nsp9"
FT                   /id="PRO_0000037394"
FT   CHAIN           3864..3998
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037395"
FT   CHAIN           3999..4927
FT                   /note="RNA-directed RNA polymerase nsp12"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037396"
FT   CHAIN           4928..5526
FT                   /note="Helicase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037397"
FT   CHAIN           5527..6045
FT                   /note="Exoribonuclease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037398"
FT   CHAIN           6046..6384
FT                   /note="Uridylate-specific endoribonuclease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037399"
FT   CHAIN           6385..6684
FT                   /note="Putative 2'-O-methyl transferase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037400"
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   DOMAIN          4006..4255
FT                   /note="NiRAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT   DOMAIN          4261..4359
FT                   /note="Nsp12 Interface"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   DOMAIN          4360..4927
FT                   /note="Nsp12 RNA-dependent RNA polymerase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   DOMAIN          4607..4769
FT                   /note="RdRp catalytic"
FT   DOMAIN          4928..5040
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   DOMAIN          5175..5366
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          5367..5536
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          5598..5812
FT                   /note="ExoN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   DOMAIN          5821..6042
FT                   /note="N7-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   DOMAIN          6046..6106
FT                   /note="Nsp15 N-terminal oligomerization"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT   DOMAIN          6107..6224
FT                   /note="AV-Nsp11N/CoV-Nsp15M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT   DOMAIN          6241..6381
FT                   /note="NendoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   DOMAIN          6385..6681
FT                   /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
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   REGION          4362..4576
FT                   /note="RdRp Fingers N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4577..4615
FT                   /note="RdRp Palm N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4616..4674
FT                   /note="RdRp Fingers C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4675..4810
FT                   /note="RdRp Palm C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4811..4927
FT                   /note="RdRp Thumb"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5933..5947
FT                   /note="GpppA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
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   ACT_SITE        4754
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        4755
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        4756
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5616
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5618
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5717
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5793
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5798
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6286
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6327
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6429
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6513
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6553
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6586
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
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   BINDING         4290
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4482
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4637
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4640
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4641
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4932
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4935
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4943
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4946
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4953
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4956
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4960
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4966
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4977
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4982
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4999
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5002
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5210..5217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         5733
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5735
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5751
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5754
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5782
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5786
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5789
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5804
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5856..5862
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         5971
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         5988
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         5999
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6002
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
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   SITE            4927..4928
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            5526..5527
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6045..6046
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6384..6385
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   VARIANT         5276
FT                   /note="P -> A (in strain: Isolate Purdue-115)"
FT   VARIANT         6054
FT                   /note="V -> I (in strain: Isolate Purdue-115)"
FT   VARIANT         6421
FT                   /note="D -> V (in strain: Isolate Purdue-115)"
FT   VARIANT         6426..6427
FT                   /note="NV -> KF (in strain: Isolate Purdue-115)"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:6IVC"
FT   HELIX           23..36
FT                   /evidence="ECO:0007829|PDB:6IVC"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:6IVC"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:6IVC"
FT   STRAND          59..75
FT                   /evidence="ECO:0007829|PDB:6IVC"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:6IVC"
FT   STRAND          96..104
FT                   /evidence="ECO:0007829|PDB:6IVC"
FT   TURN            2889..2891
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           2892..2894
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2895..2900
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2903..2910
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2913..2917
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           2918..2921
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           2931..2936
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           2940..2942
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2944..2947
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2950..2952
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2954..2960
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2963..2970
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2978..2980
FT                   /evidence="ECO:0007829|PDB:2AMP"
FT   STRAND          2988..2995
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          2998..3006
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          3025..3030
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          3033..3043
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          3049..3052
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           3059..3061
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          3064..3066
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           3078..3090
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           3104..3111
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   TURN            3112..3115
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           3123..3125
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           3126..3132
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           3136..3146
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   STRAND          3158..3160
FT                   /evidence="ECO:0007829|PDB:1LVO"
FT   HELIX           3167..3173
FT                   /evidence="ECO:0007829|PDB:1LVO"
SQ   SEQUENCE   6684 AA;  748912 MW;  88468A64F84E35A2 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 TVDQSYLNRV RGSSAARLEP
     CNGTDPDHVS RAFDIYNKDV ACIGKFLKTN CSRFRNLDKH DAYYIVKRCT KTVMDHEQVC
     YNDLKDSGAV AEHDFFTYKE GRCEFGNVAR RNLTKYTMMD LCYAIRNFDE KNCEVLKEIL
     VTVGACTEEF FENKDWFDPV ENEAIHEVYA KLGPIVANAM LKCVAFCDAI VEKGYIGVIT
     LDNQDLNGNF YDFGDFVKTA PGFGCACVTS YYSYMMPLMG MTSCLESENF VKSDIYGSDY
     KQYDLLAYDF TEHKEYLFQK YFKYWDRTYH PNCSDCTSDE CIIHCANFNT LFSMTIPMTA
     FGPLVRKVHI DGVPVVVTAG YHFKQLGIVW NLDVKLDTMK LSMTDLLRFV TDPTLLVASS
     PALLDQRTVC FSIAALSTGI TYQTVKPGHF NKDFYDFITE RGFFEEGSEL TLKHFFFAQG
     GEAAMTDFNY YRYNRVTVLD ICQAQFVYKI VGKYFECYDG GCINAREVVV TNYDKSAGYP
     LNKFGKARLY YETLSYEEQD ALFALTKRNV LPTMTQMNLK YAISGKARAR TVGGVSLLST
     MTTRQYHQKH LKSIAATRNA TVVIGSTKFY GGWDNMLKNL MRDVDNGCLM GWDYPKCDRA
     LPNMIRMASA MILGSKHVGC CTHNDRFYRL SNELAQVLTE VVHCTGGFYF KPGGTTSGDG
     TTAYANSAFN IFQAVSANVN KLLGVDSNAC NNVTVKSIQR KIYDNCYRSS SIDEEFVVEY
     FSYLRKHFSM MILSDDGVVC YNKDYADLGY VADINAFKAT LYYQNNVFMS TSKCWVEPDL
     SVGPHEFCSQ HTLQIVGPDG DYYLPYPDPS RILSAGVFVD DIVKTDNVIM LERYVSLAID
     AYPLTKHPKP AYQKVFYTLL DWVKHLQKNL NAGVLDSFSV TMLEEGQDKF WSEEFYASLY
     EKSTVLQAAG MCVVCGSQTV LRCGDCLRRP LLCTKCAYDH VMGTKHKFIM SITPYVCSFN
     GCNVNDVTKL FLGGLSYYCM NHKPQLSFPL CANGNVFGLY KSSAVGSEAV EDFNKLAVSD
     WTNVEDYKLA NNVKESLKIF AAETVKAKEE SVKSEYAYAV LKEVIGPKEI VLQWEASKTK
     PPLNRNSVFT CFQISKDTKI QLGEFVFEQS EYGSDSVYYK STSTYKLTPG MIFVLTSHNV
     SPLKAPILVN QEKYNTISKL YPVFNIAEAY NTLVPYYQMI GKQKFTTIQG PPGSGKSHCV
     IGLGLYYPQA RIVYTACSHA AVDALCEKAA KNFNVDRCSR IIPQRIRVDC YTGFKPNNTN
     AQYLFCTVNA LPEASCDIVV VDEVSMCTNY DLSVINSRLS YKHIVYVGDP QQLPAPRTLI
     NKGVLQPQDY NVVTKRMCTL GPDVFLHKCY RCPAEIVKTV SALVYENKFV PVNPESKQCF
     KMFVKGQVQI ESNSSINNKQ LEVVKAFLAH NPKWRKAVFI SPYNSQNYVA RRLLGLQTQT
     VDSAQGSEYD YVIYTQTSDT QHATNVNRFN VAITRAKVGI LCIMCDRTMY ENLDFYELKD
     SKIGLQAKPE TCGLFKDCSK SEQYIPPAYA TTYMSLSDNF KTSDGLAVNI GTKDVKYANV
     ISYMGFRFEA NIPGYHTLFC TRDFAMRNVR AWLGFDVEGA HVCGDNVGTN VPLQLGFSNG
     VDFVVQTEGC VITEKGNSIE VVKARAPPGE QFAHLIPLMR KGQPWHIVRR RIVQMVCDYF
     DGLSDILIFV LWAGGLELTT MRYFVKIGRP QKCECGKSAT CYSSSQSVYA CFKHALGCDY
     LYNPYCIDIQ QWGYTGSLSM NHHEVCNIHR NEHVASGDAI MTRCLAIHDC FVKRVDWSIV
     YPFIDNEEKI NKAGRIVQSH VMKAALKIFN PAAIHDVGNP KGIRCATTPI PWFCYDRDPI
     NNNVRCLDYD YMVHGQMNGL MLFWNCNVDM YPEFSIVCRF DTRTRSKLSL EGCNGGALYV
     NNHAFHTPAY DRRAFAKLKP MPFFYYDDSN CELVDGQPNY VPLKSNVCIT KCNIGGAVCK
     KHAALYRAYV EDYNIFMQAG FTIWCPQNFD TYMLWHGFVN SKALQSLENV AFNVVKKGAF
     TGLKGDLPTA VIADKIMVRD GPTDKCIFTN KTSLPTNVAF ELYAKRKLGL TPPLTILRNL
     GVVATYKFVL WDYEAERPFS NFTKQVCSYT DLDSEVVTCF DNSIAGSFER FTTTRDAVLI
     SNNAVKGLSA IKLQYGLLND LPVSTVGNKP VTWYIYVRKN GEYVEQIDSY YTQGRTFETF
     KPRSTMEEDF LSMDTTLFIQ KYGLEDYGFE HVVFGDVSKT TIGGMHLLIS QVRLAKMGLF
     SVQEFMNNSD STLKSCCITY ADDPSSKNVC TYMDILLDDF VTIIKSLDLN VVSKVVDVIV
     DCKAWRWMLW CENSHIKTFY PQLQSAEWNP GYSMPTLYKI QRMCLERCNL YNYGAQVKLP
     DGITTNVVKY TQLCQYLNTT TLCVPHKMRV LHLGAAGASG VAPGSTVLRR WLPDDAILVD
     NDLRDYVSDA DFSVTGDCTS LYIEDKFDLL VSDLYDGSTK SIDGENTSKD GFFTYINGFI
     KEKLSLGGSV AIKITEFSWN KDLYELIQRF EYWTVFCTSV NTSSSEGFLI GINYLGPYCD
     KAIVDGNIMH ANYIFWRNST IMALSHNSVL DTPKFKCRCN NALIVNLKEK ELNEMVIGLL
     RKGKLLIRNN GKLLNFGNHF VNTP
//