R1AB_FIPV
ID R1AB_FIPV Reviewed; 6709 AA.
AC Q98VG9; Q4U5G1; Q4U5G2; Q52PA4;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
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 Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE Contains:
DE RecName: Full=Non-structural protein 11;
DE Short=nsp11;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=nsp12;
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 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 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 Feline coronavirus (strain FIPV WSU-79/1146) (FCoV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=33734;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16033972; DOI=10.1099/vir.0.80985-0;
RA Dye C., Siddell S.G.;
RT "Genomic RNA sequence of Feline coronavirus strain FIPV WSU-79/1146.";
RL J. Gen. Virol. 86:2249-2253(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Haijema B.J., de Groot-Mijnes J.D.F., Vennema H., Raamsman M.J.,
RA Rottier P.J.M., de Groot R.J.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2894-3215, AND MUTAGENESIS OF
RP HIS-2944; ASN-2967; GLY-2986; SER-3041; CYS-3047; TYR-3063; MET-3064 AND
RP HIS-3065.
RX PubMed=11842253; DOI=10.1099/0022-1317-83-3-581;
RA Hegyi A., Friebe A., Gorbalenya A.E., Ziebuhr J.;
RT "Mutational analysis of the active centre of coronavirus 3C-like
RT proteases.";
RL J. Gen. Virol. 83:581-593(2002).
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 -!- 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 [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function
CC (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}.
CC -!- FUNCTION: 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) (By similarity). {ECO:0000250}.
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: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
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]:
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: [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_5000140215; PRO_5000140214 [Q98VG9]: rep; NbExp=3; IntAct=EBI-26365785, EBI-26365769;
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 -!- 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=Q98VG9-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=Q98VG9-2; Sequence=VSP_032885;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
CC ribosomal frameshifting at the 1a-1b genes boundary.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
CC conventional translation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY16374.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ010921; AAY32594.1; -; Genomic_RNA.
DR EMBL; DQ010921; AAY32595.1; -; Genomic_RNA.
DR EMBL; AY994055; AAY16374.1; ALT_FRAME; Genomic_RNA.
DR EMBL; AF326575; AAK09095.1; -; Genomic_RNA.
DR PDB; 3ETI; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1331-1498.
DR PDB; 3EW5; X-ray; 3.10 A; A/B/C=1331-1498.
DR PDB; 3GZF; X-ray; 2.76 A; A/B/C/D/E=2808-2902.
DR PDB; 3JZT; X-ray; 3.91 A; A/B/C/D/E/F/G/H=1331-1498.
DR PDB; 3UB0; X-ray; 2.60 A; A/D=3583-3777, B/C/E/F=3500-3582.
DR PDB; 4ZRO; X-ray; 2.06 A; A/B/C/D=2904-3202.
DR PDB; 5EU8; X-ray; 2.45 A; A=2904-3205.
DR PDB; 6LP9; X-ray; 1.80 A; A/B/C/D=1-110.
DR PDBsum; 3ETI; -.
DR PDBsum; 3EW5; -.
DR PDBsum; 3GZF; -.
DR PDBsum; 3JZT; -.
DR PDBsum; 3UB0; -.
DR PDBsum; 4ZRO; -.
DR PDBsum; 5EU8; -.
DR PDBsum; 6LP9; -.
DR SMR; Q98VG9; -.
DR IntAct; Q98VG9; 5.
DR BindingDB; Q98VG9; -.
DR ChEMBL; CHEMBL4295624; -.
DR DrugBank; DB15797; GC-373.
DR DrugBank; DB15796; GC-376 free acid.
DR MEROPS; C30.004; -.
DR PRIDE; Q98VG9; -.
DR SABIO-RK; Q98VG9; -.
DR EvolutionaryTrace; Q98VG9; -.
DR Proteomes; UP000000835; Genome.
DR Proteomes; UP000140386; Genome.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004532; F:exoribonuclease activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus 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:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; cd21558; alphaCoV-Nsp6; 1.
DR CDD; cd21660; alphaCoV_Nsp14; 1.
DR CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR CDD; cd21588; alphaCoV_RdRp; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21514; cv_alpha_Nsp2_HCoV-229E-like; 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_beta_cv_Nsp15-like; 1.
DR CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.150.420; -; 1.
DR Gene3D; 1.10.1840.10; -; 1.
DR Gene3D; 1.10.8.1190; -; 2.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.30.30.1000; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.30.160.820; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR032039; A-CoV_nsp1.
DR InterPro; IPR038634; A-CoV_nsp1_sf.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR043611; CoV_NSP3_C.
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; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_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; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR009469; RNA_pol_N_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13087; AAA_12; 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; 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; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51962; COV_NSP1; 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_Y3; 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 Endonuclease; Exonuclease; Helicase; Host cytoplasm; Host membrane;
KW 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..6709
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000283825"
FT CHAIN 1..110
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140208"
FT CHAIN 111..879
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140209"
FT CHAIN 880..2413
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140210"
FT CHAIN 2414..2903
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140211"
FT CHAIN 2904..3205
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140212"
FT CHAIN 3206..3499
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140213"
FT CHAIN 3500..3582
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140214"
FT CHAIN 3583..3777
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140215"
FT CHAIN 3778..3888
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140216"
FT CHAIN 3889..4023
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140217"
FT CHAIN 4024..4952
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140219"
FT CHAIN 4024..4042
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140218"
FT CHAIN 4953..5551
FT /note="Helicase"
FT /evidence="ECO:0000250"
FT /id="PRO_5000140220"
FT CHAIN 5552..6070
FT /note="Exoribonuclease"
FT /evidence="ECO:0000255"
FT /id="PRO_5000140221"
FT CHAIN 6071..6409
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000255"
FT /id="PRO_5000140222"
FT CHAIN 6410..6709
FT /note="Putative 2'-O-methyl transferase"
FT /evidence="ECO:0000255"
FT /id="PRO_5000140223"
FT TRANSMEM 1860..1878
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1921..1941
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2006..2026
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2043..2065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2426..2446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2691..2711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2720..2740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2771..2791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3212..3232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3242..3262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3267..3287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3306..3326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3339..3359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3396..3416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3419..3439
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..345
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 1079..1330
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1329..1500
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1497..1553
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1561..1814
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 2304..2409
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 2808..2903
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 2904..3205
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3500..3582
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3583..3777
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3778..3888
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 3889..4029
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4018..4280
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4385..4952
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4632..4794
FT /note="RdRp catalytic"
FT DOMAIN 4953..5036
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5200..5391
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5392..5561
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5623..5837
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 5846..6067
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6071..6131
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6132..6249
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6266..6406
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6410..6706
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1188..1219
FT /note="C4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 1678..1707
FT /note="C4-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 3962..3978
FT /evidence="ECO:0000250"
FT ZN_FING 4004..4017
FT /evidence="ECO:0000250"
FT REGION 240..260
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 1005..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1860..2065
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2426..2791
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3212..3439
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 5958..5972
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT COMPBIAS 1005..1027
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1117
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1268
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1599
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1752
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 2944
FT /note="For 3CL-PRO activity"
FT ACT_SITE 3047
FT /note="For 3CL-PRO activity"
FT ACT_SITE 4779
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4780
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5742
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5818
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5823
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 3962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3965
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3971
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4004
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4007
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4015
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4017
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4957
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4968
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4971
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4981
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4985
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4991
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5002
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5007
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5024
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5235..5242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 5758
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5776
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5779
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5807
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5829
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5881..5887
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5996
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6013
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6024
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
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 2413..2414
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 2903..2904
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3053
FT /note="Important for substrate recognition"
FT SITE 3205..3206
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3499..3500
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3582..3583
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3777..3778
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3888..3889
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4023..4024
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4952..4953
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5551..5552
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6070..6071
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6409..6410
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT VAR_SEQ 4043..6709
FT /note="Missing (in isoform Replicase polyprotein 1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_032885"
FT VARIANT 162
FT /note="W -> C"
FT VARIANT 177
FT /note="D -> G"
FT VARIANT 388
FT /note="W -> C"
FT VARIANT 808
FT /note="K -> T"
FT VARIANT 1784
FT /note="A -> V"
FT VARIANT 2889
FT /note="M -> K"
FT VARIANT 3280
FT /note="A -> V"
FT VARIANT 3992
FT /note="Q -> R"
FT VARIANT 4304
FT /note="H -> Q"
FT VARIANT 5846
FT /note="Y -> H"
FT MUTAGEN 2944
FT /note="H->Y,R: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 2967
FT /note="N->A,D: Increase of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 2986
FT /note="G->A: 5% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 2986
FT /note="G->D: Increase of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 2986
FT /note="G->E: 50% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 2986
FT /note="G->P,V: 95% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 2986
FT /note="G->R,T,W: 70% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 3041
FT /note="S->A: 80% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 3041
FT /note="S->T: 40% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 3047
FT /note="C->A,S: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 3063
FT /note="Y->A,F,G,T: Almost complete loss of 3CL-PRO
FT activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 3064
FT /note="M->A: Increase of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT MUTAGEN 3065
FT /note="H->A: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253"
FT CONFLICT 1016..1092
FT /note="Missing (in Ref. 1; AAY32594)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6LP9"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:6LP9"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:6LP9"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6LP9"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:6LP9"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6LP9"
FT STRAND 59..75
FT /evidence="ECO:0007829|PDB:6LP9"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:6LP9"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:6LP9"
FT STRAND 1336..1339
FT /evidence="ECO:0007829|PDB:3ETI"
FT STRAND 1342..1347
FT /evidence="ECO:0007829|PDB:3ETI"
FT HELIX 1349..1356
FT /evidence="ECO:0007829|PDB:3ETI"
FT STRAND 1359..1365
FT /evidence="ECO:0007829|PDB:3ETI"
FT HELIX 1376..1382
FT /evidence="ECO:0007829|PDB:3ETI"
FT TURN 1383..1385
FT /evidence="ECO:0007829|PDB:3ETI"
FT HELIX 1386..1395
FT /evidence="ECO:0007829|PDB:3ETI"
FT STRAND 1405..1413
FT /evidence="ECO:0007829|PDB:3ETI"
FT STRAND 1416..1422
FT /evidence="ECO:0007829|PDB:3ETI"
FT HELIX 1431..1443
FT /evidence="ECO:0007829|PDB:3ETI"
FT STRAND 1449..1451
FT /evidence="ECO:0007829|PDB:3ETI"
FT HELIX 1463..1473
FT /evidence="ECO:0007829|PDB:3ETI"
FT STRAND 1479..1483
FT /evidence="ECO:0007829|PDB:3ETI"
FT HELIX 1486..1497
FT /evidence="ECO:0007829|PDB:3ETI"
FT HELIX 2818..2823
FT /evidence="ECO:0007829|PDB:3GZF"
FT STRAND 2826..2828
FT /evidence="ECO:0007829|PDB:3GZF"
FT HELIX 2830..2837
FT /evidence="ECO:0007829|PDB:3GZF"
FT TURN 2838..2840
FT /evidence="ECO:0007829|PDB:3GZF"
FT HELIX 2842..2850
FT /evidence="ECO:0007829|PDB:3GZF"
FT HELIX 2852..2856
FT /evidence="ECO:0007829|PDB:3GZF"
FT HELIX 2864..2884
FT /evidence="ECO:0007829|PDB:3GZF"
FT STRAND 2889..2891
FT /evidence="ECO:0007829|PDB:3GZF"
FT STRAND 2895..2899
FT /evidence="ECO:0007829|PDB:3GZF"
FT TURN 2914..2916
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 2917..2919
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 2920..2925
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 2928..2935
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 2938..2942
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 2943..2946
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 2950..2952
FT /evidence="ECO:0007829|PDB:5EU8"
FT HELIX 2956..2962
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 2965..2967
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 2968..2972
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 2975..2977
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 2979..2985
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 2988..2995
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 3013..3020
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 3023..3031
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 3050..3055
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 3058..3068
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 3074..3077
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 3079..3081
FT /evidence="ECO:0007829|PDB:5EU8"
FT HELIX 3084..3086
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 3089..3092
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 3103..3115
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 3129..3136
FT /evidence="ECO:0007829|PDB:4ZRO"
FT TURN 3137..3140
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 3147..3150
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 3151..3157
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 3161..3171
FT /evidence="ECO:0007829|PDB:4ZRO"
FT STRAND 3183..3185
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 3192..3200
FT /evidence="ECO:0007829|PDB:4ZRO"
FT HELIX 3510..3518
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3521..3523
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3525..3540
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3544..3561
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3568..3577
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3579..3581
FT /evidence="ECO:0007829|PDB:3UB0"
FT STRAND 3583..3585
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3587..3609
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3614..3652
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3663..3680
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3683..3693
FT /evidence="ECO:0007829|PDB:3UB0"
FT STRAND 3697..3702
FT /evidence="ECO:0007829|PDB:3UB0"
FT STRAND 3709..3714
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3717..3723
FT /evidence="ECO:0007829|PDB:3UB0"
FT STRAND 3728..3731
FT /evidence="ECO:0007829|PDB:3UB0"
FT STRAND 3734..3742
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3751..3753
FT /evidence="ECO:0007829|PDB:3UB0"
FT HELIX 3756..3761
FT /evidence="ECO:0007829|PDB:3UB0"
FT STRAND 3766..3772
FT /evidence="ECO:0007829|PDB:3UB0"
SQ SEQUENCE 6709 AA; 751196 MW; F26AC0FFF5FE27F9 CRC64;
MSSKQFKILV NEDYQVNVPS LPFRDALQEI KYCYRNGFDG YVFVPEYRRD LVDCNRKDHY
VIGVLGNGIS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF DLKFARTGNG AIYVDQYMCG
ADGKPVIEGE FKDYFGDEDV IIYEGEEYHC AWLTVRDEKP LWQQTLLTIR EIQYNLDIPH
KLPNCAIREV APPVKKNSKV VLSEEYRKLY DIFGSPFMGN GDSLNTCFDS LHFIAATLKC
PCGAESSGVG DWTGFKTACC GLHGKVKGVT LGAVKPGDAI VTSMSAGKGV KFFANSVLQY
AGDVENVSVW KVIKTFTVNE TVCTTDFEGE LNDFIRPEST SPVSCSIKRA FITGEVDDAV
HDCIIAGKLD LSTNLFGSAN LLFKKMPWFV QKCGAIFADA WKVVEELLCS LKLTYKQIYD
VVASLCTSAF TIMDYKPVFV VSSNSVKDLV DKCVKILVKA FDVFTQTITI AGVEAKCFVL
GSKYLLFNNA LVKLVSVKIL GKRQKGLDSA FFATNLIGAT VNVTPQRTES AYISLNKVDD
VVTPGGGHIV IIGDMAFYKS EEYYFMMASP DSVLVNNVFK AARVPSYNIV YDVNDDTKSK
MVVKIGTSFD FDGDLDAAIA KVNDLLIEFR QEKLCFRALK DGENILVEAY LKKYKMPVCL
KNHVGLWDII RQDSGKKGFL DTFNHLNELE DVKDIKIQTI KNIICPDLLL ELDFGAIWYR
CMPACSDKSI LGNVKIMLGN GVKVVCDGCH SFANRLTINY NKLCDTARKD IEIGGIPFST
FKTPSSSFID MKDAIYSVVE YGEALSFKTA SVPVTNSGII TTDDWSDPIL LEPADYVEPK
DNGDVIVIAG YTFYKDEDDH FYPYGSGMVV QKMYNKMGGG DKSVSFSDNV NVREIEPVTR
VRLEFEFDNE VVTQVLEKVI GTKYKFIGTT WEEFEDSISE KLDKIFDTLA EQGVELEGYF
IYDTCGGFDI NNPDGVMISQ YDLNTAADDK SDSDASVEDI SLISDNEDVE QIEEDNTSTD
DAEDVSSVEG ETVSVVDVED FVEQVSLVEE NNVLTPAVNP DEQLSSVEKK DEVSAKNDPW
AAAVDEQEAE QPKPSLTPFK TTNLNGKIIL KQQDNNCWIN ACCYQLQAFD FFNHDLWDGF
KKDDVMPFVD FCYAALTLKQ GDSGDAEYLL ETMLNDYSTA KVTLSAKCGC GVKEIVLERT
VFKLTPLRNE FKYGVCGDCK QINMCKFASV EGSGVFVHDR IEKQTPVSQF IVTPTMHAVY
TGTTQSGHYM IEDCIHDYCV DGMGIKPRKH KFYTSTLFLN ANVMTAKSKT MVEPPVPVED
KCVEDCQSPK DLILPFYKAG KVSFYQGDLD VLINFLEPDV LVNAANGDLR HVGGVARAID
VFTGGKLTKR SKEYLKSSKA IAPGNAVLFE NVLEHLSVLN AVGPRNGDSR VEGKLCNVYK
AIAKCDGKIL TPLISVGIFK VKLEVSLQCL LKTVTDRDLN VFVYTDQERV TIENFFNGTI
PIKVTEDTVN QKRVSVALDK TYGEQLKGTV VIKDKDVTNQ LPSVSDVGEK VVKALDVDWN
AYYGFPNAAA FSASSHDAYE FDVVTHNNFI VHKQTDNNCW VNAICLALQR LKPTWKFPGV
KSLWDAFLTR KTAGFVHMLY HISGLTKGQP GDAELTLHKL VDLMSSDSAV TVTHTTACDK
CAKVETFTGP VVAAPLLVCG TDEICVHGVH VNVKVTSIRG TVAITSLIGP VVGDVIDATG
YICYTGLNSR GHYTYYDNRN GLMVDADKAY HFEKNLLQVT TAIASNFVAN TPKKEIMPKT
QAKESKAKES NTARVFSEVE ENPKNIVRKE KLLAIESGVD YTITTLGKYA DVFFMAGDKI
LRFLLEVFKY LLVVFMCLRK SKMPKVKVKP PHVFRNLGAK VRTLNYVRQL NKPALWRYIK
LVLLLIALYH FFYLFVSIPV VHKLACSGSV QAYSNSSFVK SEVCGNSILC KACLASYDEL
ADFDHLQVSW DYKSDPLWNR VIQLSYFIFL AVFGNNYVRC LLMYFVSQYL NLWLSYFGYV
KYSWFLHVVN FESISVEFVI IVVVFKAVLA LKHIFLPCNN PSCKTCSKIA RQTRIPIQVV
VNGSMKTVYV HANGTGKLCK KHNFYCKNCD SYGFDHTFIC DEIVRDLSNS IKQTVYATDR
SYQEVTKVEC TDGFYRFYVG EEFTAYDYDV KHKKYSSQEV LKTMFLLDDF IVYNPSGSSL
ASVRNVCVYF SQLIGRPIKI VNSELLEDLS VDFKGALFNA KKNVIKNSFN VDVSECKNLE
ECYKLCNLDV TFSTFEMAIN NAHRFGILIT DRSFNNFWPS KIKPGSSGVS AMDIGKCMTF
DAKIVNAKVL TQRGKSVVWL SQDFSTLSST AQKVLVKTFV EEGVNFSLTF NAVGSDEDLP
YERFTESVSA KSGSGFFDVL KQLKQLFWCL VLFITLYGLC SVYSVATQSY IDSAEGYDYM
VIKNGVVQSF DDSINCVHNT YKGFAVWFKA KHGFVPTFDK SCPIVLGTVF DLGNMRPIPD
VPAYVALVGR SLVFAINAAF GVTNVCYDHT GAAVSKNSYF DTCVFNSACT TLTGIGGTVV
YCAKQGLVEG AKLYSELLPD YYYEHASGNM VKIPAIIRSF GLRFVKTQAT TYCRVGECTE
SQAGFCFGGD NWFVYDKEFG DGYICGSSTL GFFKNVFALF NSNMSVVATS GAMLANIVIA
CLAIAVCYGV LKFKKIFGDC TLLVVMIIVT LVVNNVSYFV TQNTFFMIVY AIIYYFTTRK
LAYPGVLDAG FIIAYLNMAP WYVLVLYIMV FLYDSLPSLF KLKVTTNLFE GDKFVGSFES
AAMGTFVIDM RSYETLVNST SLDRIKSYAN SFNKYKYYTG SMGEADYRMA CYAHLGKALM
DYSVSRNDML YTPPTVSVNS TLQSGLRKMA QPSGVVEPCI VRVAYGNNVL NGLWLGDEVI
CPRHVIASDT SRVINYENEL SSVRLHNFSI AKNNAFLGVV SAKYKGVNLV LKVNQVNPNT
PEHKFKSVRP GESFNILACY EGCPGSVYGV NMRSQGTIKG SFIAGTCGSV GYVLENGTLY
FVYMHHLELG NGSHVGSNLE GEMYGGYEDQ PSMQLEGTNV MSSDNVVAFL YAALINGERW
FVTNTSMTLE SYNAWAKTNS FTEIVSTDAF NMLAAKTGYS VEKLLECIVR LNKGFGGRTI
LSYGSLCDEF TPTEVIRQMY GVNLQSGKVK SIFYPMMTAI AILFAFWLEF FMYTPFTWIN
PTFVSVVLAI TTLVSVLLVA GIKHKMLFFM SFVMPSVILA TAHNVVWDMT YYESLQVLVE
NVNTTFLPVD MQGVMLALFC VVVFVICTIR FFTCKQSWFS LFATTIFVMF NIVKLLGMIG
EPWTDDHFLL CLVNMLTMLI SLTTKDWFVV FASYKVAYYI VVYVMQPAFV QDFGFVKCVS
IIYMACGYLF CCYYGILYWV NRFTCMTCGV YQFTVSPAEL KYMTANNLSA PKTAYDAMIL
SFKLMGIGGG RNIKISTVQS KLTEMKCTNV VLLGLLSKMH VESNSKEWNY CVGLHNEINL
CDDPDAVLEK LLALIAFFLS KHNTCDLSDL IESYFENTTI LQSVASAYAA LPSWIAYEKA
RADLEEAKKN DVSPQLLKQL TKACNIAKSE FEREASVQKK LDKMAEQAAA SMYKEARAVD
RKSKIVSAMH SLLFGMLKKL DMSSVNTIIE QARNGVLPLS IIPAASATRL IVVTPNLEVL
SKVRQENNVH YAGAIWSIVE VKDANGAQVH LKEVTAANEL NITWPLSITC ERTTKLQNNE
ILPGKLKEKA VKASATIDGD AYGSGKALMA SEGGKSFIYA FIASDSNLKY VKWESNNDVI
PIELEAPLRF YVDGVNGPEV KYLYFVKSLN TLRRGAVLGY IGATVRLQAG KPTEHPSNSG
LLTLCAFAPD PAKAYVDAVK RGMQPVTNCV KMLSNGAGNG MAITNGVESN TQQDSYGGAS
VCIYCRCHVE HPAIDGLCRF KGKFVQVPTG TQDPIRFCIE NEVCVVCGCW LTNGCMCDRT
SIQGTTIDQS YLNECGVLVQ LDLEPCNGTD PDHVSRAFDI YNKDVACIGK FLKTNCSRFR
NLDKHDAYYV VKRCTKSVMD HEQVCYNDLK DSGVVAEHDF FLYKEGRCEF GNVARKDLTK
YTMMDLCYAI RNFDEKNCEV LKEILVTLGA CNESFFENKD WFDPVENEAI HEVYARLGPI
VANAMLKCVA FCDAIVEKGY IGIITLDNQD LNGNFYDFGD FVKTTPGFGC ACVTSYYSYM
MPLMGMTSCL ESENFVKSDI YGADYKQYDL LAYDFTDHKE KLFHKYFKHW DRTYHPNCSD
CTSDECIIHC ANFNTLFSMT IPSTAFGPLV RKVHIDGVPV VVTAGYHFKQ LGIVWNLDVK
LDTMKLSMTD LLRFVTDPTL LVASSPALLD QRTVCFSIAA LSTGVTYQTV KPGHFNKDFY
DFITERGFFE EGSELTLKHF FFAQGGEAAM TDFNYYRYNR VTVLDICQAQ FVYKIVGKYF
ECYDGGCINA REVVVTNYDK SAGYPLNKFG KARLYYETLS YEEQDALFAL TKRNVLPTMT
QMNLKYAISG KARARTVGGV SLLSTMTTRQ YHQKHLKSIA ATRNATVVIG STKFYGGWDN
MLKNLMRDVD NGCLMGWDYP KCDRALPNMI RMASAMILGS KHVGCCTHSD RFYRLSNELA
QVLTEVVHCT GGFYFKPGGT TSGDGTTAYA NSAFNIFQAV SANVNKLLGV DSNACNNVTV
KSIQRKIYDN CYRSSSIDEE FVVEYFSYLR KHFSMMILSD DGVVCYNKDY ADLGYVADIN
AFKATLYYQN NVFMSTSKCW VEPDLSVGPH EFCSQHTLQI VGPDGDYYLP YPDPSRILSA
GVFVDDIVKT DNVIMLERYV SLAIDAYPLT KHPKPAYQKV FYTLLDWVKH LQKNLNAGVL
DSFSVTMLEE GQDKFWSEEF YASLYEKSTV LQAAGMCVVC GSQTVLRCGD CLRRPLLCTK
CAYDHVMGTK HKFIMSITPY VCSFNGCNVN DVTKLFLGGL SYYCMDHKPQ LSFPLCANGN
VFGLYKSSAV GSEDVEDFNK LAVSDWTNVE DYKLANNVKE SLKIFAAETV KAKEESVKSE
YAYAILKEVI GPKEIVLQWE ASKTKPPLNR NSVFTCFQIS KDTKIQLGEF VFEQSEYGSD
SVYYKSTSTY KLTPGMIFVL TSHNVSPLKA TILVNQEKYN TISKLYPVFN IAEAYNTLVP
YYQMIGKQKF TTIQGPPGSG KSHCVIGLGL YYPQARIVYT ACSHAAVDAL CEKAAKNFNV
DRCSRIIPQR IRVDCYTGFK PNNTNAQYLF CTVNALPEAS CDIVVVDEVS MCTNYDLSVI
NSRLSYKHIV YVGDPQQLPA PRTLINKGVL QPQDYNVVTQ RVCTLGPDVF LHKCYRCPAE
IVKTVSALVY ENKFVPVNPE SKQCFKMFVK GQVQIESNSS INNKQLEVVK AFLAHNPKWR
KAVFISPYNS QNYVARRLLG LQTQTVDSAQ GSEYDYVIYT QTSDTQHATN VNRFNVAITR
AKVGILCIMC DRTMYENLDF YELKDSKIGL QAKPETCGLF KDCSKSEQYI PPAYATTYMS
LSDNFKTSDG LAVNIGTKDV KYANVISYMG FRFEANIPGY HTLFCTRDFA MRNVRAWLGF
DVEGAHVCGD NVGTNVPLQL GFSNGVDFVV QTEGCVVTEK GNSIEVVKAR APPGEQFAHL
IPLMRKGQPW HIVRRRIVQM VCDYFDGLSD ILIFVLWAGG LELTTMRYFV KIGRPQKCEC
GKSATCYSSS QCVYACFKHA LGCDYLYNPY CIDIQQWGYT GSLSMNHHEV CNIHRNEHVA
SGDAIMTRCL AIHDCFVKRV DWSIVYPFID NEEKINKAGR IVQSHVMKAA LKIFNPAAIH
DVGNPKGIRC ATTPIPWFCY DRDPINNNVR CLEYDYMVHG QMNGLMLFWN CNVDMYPEFS
IVCRFDTRTR SKLSLEGCNG GALYVNNHAF HTPAYDRRAF AKLKPMPFFY YDDSNCELVD
GQPNYVPLKS NVCITKCNIG GAVCKKHAAL YRAYVEDYNM FMQAGFTIWC PQNFDTYMLW
HGFVNSKALQ SLENVAFNVV KKGAFTGLKG DLPTAVIADK IMVRDGPTDK CIFTNKTSLP
TNVAFELYAK RKLGLTPPLT ILRNLGVVAT YKFVLWDYEA ECPFSNFTKQ VCSYTDLDSE
VVTCFDNSIA GSFERFTTTK DAVLISNNAV KGLSAIKLQY GFLNDLPVST VGNKPVTWYI
YVRKNGEYVE QIDSYYTHGR TFETFKPRST MEEDFLSMDT TLFIQKYGLE DYGFEHVVFG
DVSKTTIGGM HLLISQVRLA KMGLFSVQEF MTNSDSTLKS CCITYADDPS SKNVCTYMDI
LLDDFVTIIK SLDLNVVSKV VDVIVDCKAW RWMLWCENSQ IKTFYPQLQS AEWNPGYSMP
TLYKIQRMCL ERCNLYNYGA QVRLPDGITT NVVKYTQLCQ YLNTTTVCVP HKMRVLHLGA
AGASGVAPGS TVLRRWLPDD AILVDNDLRD YVSDADFSVT GDCTSLYIED KFDLLISDLY
DGSTKSIDGE NTSKDGFFTY INGFIKEKLS LGGSAAIKIT EFSWNKDLYE LIQRFEYWTV
FCTSVNTSSS EGFLIGINYL GPYCDKAIVD GNIMHANYIF WRNSTIMALS HNSVLDTPKF
KCRCNNALIV NLKEKELNEM VVGLLRKGKL LIRNNGKLLN FGNHLVNVP
