R1AB_BC512
ID R1AB_BC512 Reviewed; 6793 AA.
AC P0C6W0; Q0Q467;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Non-structural protein 9;
DE Short=nsp9;
DE AltName: Full=p12;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE AltName: Full=p14;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
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 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 Bat coronavirus 512/2005 (BtCoV) (BtCoV/512/2005).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Pedacovirus.
OX NCBI_TaxID=693999;
OH NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16840328; DOI=10.1128/jvi.00697-06;
RA Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
RA Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
RA Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
RT "Prevalence and genetic diversity of coronaviruses in bats from China.";
RL J. Virol. 80:7481-7490(2006).
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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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 -!- 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=P0C6W0-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6F6-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Bat coronavirus 512/2005 is highly similar to porcine
CC epidemic diarrhea virus (PEDV).
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; DQ648858; ABG47077.1; -; Genomic_RNA.
DR RefSeq; YP_001351683.1; NC_009657.1. [P0C6W0-1]
DR SMR; P0C6W0; -.
DR MEROPS; C30.003; -.
DR PRIDE; P0C6W0; -.
DR GeneID; 11266518; -.
DR KEGG; vg:11266518; -.
DR Proteomes; UP000113079; 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:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; 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; 2.40.10.10; -; 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; 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; IPR045055; DNA2/NAM7-like.
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; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR009469; RNA_pol_N_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR Pfam; PF13087; AAA_12; 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; 1.
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.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus; ATP-binding; Endonuclease;
KW 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; Repeat;
KW 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_0000289911"
FT CHAIN 111..897
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289912"
FT CHAIN 898..2530
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289913"
FT CHAIN 2531..3012
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289914"
FT CHAIN 3013..3314
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289915"
FT CHAIN 3315..3590
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289916"
FT CHAIN 3591..3673
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289917"
FT CHAIN 3674..3868
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289918"
FT CHAIN 3869..3976
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289919"
FT CHAIN 3977..4111
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289920"
FT CHAIN 4112..5038
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289921"
FT CHAIN 5039..5557
FT /note="Helicase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289922"
FT CHAIN 5558..6153
FT /note="Exoribonuclease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289923"
FT CHAIN 6154..6492
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289924"
FT CHAIN 6493..6793
FT /note="Putative 2'-O-methyl transferase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000289925"
FT TRANSMEM 1973..1993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2036..2056
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2119..2139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2141..2161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2164..2184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2543..2563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2634..2654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2669..2689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2769..2789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2802..2822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2829..2849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2878..2898
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3351..3371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3376..3396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3414..3434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3443..3463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3466..3486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3488..3507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3511..3531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2..109
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 112..368
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 396..785
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 776..897
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 898..993
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1069..1302
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1303..1467
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1638..1693
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1699..1965
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 2426..2530
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 2917..3012
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3013..3314
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3591..3673
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3674..3868
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3869..3976
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 3977..4115
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4117..4366
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4471..5038
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4718..4880
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5039..5122
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5296..5477
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5478..5647
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5707..5921
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 5930..6151
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6154..6214
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6215..6332
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6349..6489
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6493..6789
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1174..1205
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4050..4066
FT /evidence="ECO:0000250"
FT ZN_FING 4092..4105
FT /evidence="ECO:0000250"
FT REGION 1973..2184
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2543..2898
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3351..3531
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 6042..6056
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1103
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1252
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1737
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1902
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3053
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3156
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 4865
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4866
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5725
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5727
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5902
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5907
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6621
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 4050
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4053
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4059
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4066
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4095
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 5043
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5046
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5054
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5057
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5064
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5067
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5071
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5077
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5088
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5093
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5321..5328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 5842
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5844
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5863
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5913
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5965..5971
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6080
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6097
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6111
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 897..898
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 2530..2531
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 3012..3013
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3314..3315
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3590..3591
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3673..3674
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3868..3869
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3976..3977
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4111..4112
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5038..5039
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5557..5558
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6153..6154
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6492..6493
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
SQ SEQUENCE 6793 AA; 757262 MW; 6C76171F3E67FE1D CRC64;
MASNHISLAF ANDEEISAIG FGSVEEAVSY YSDAAVNGFD QCRFVSLGLQ DAVVGVEDDD
VVMLITGVTQ LRAYLGTFGD RPLNLRGWLL FSNCNYFLEE LDLVFGRCGG TTIPVDQFMC
GADGAPVIQE GDWTFMDYFQ DSNQFTLNGI TYVKAWDVDR KPNDYAKQNV TCIRRITYIT
DHRHVLADGT TMKTARHPKV NKSVVLDSPF DQIYKEVGSP FMGNGSTFVE MLKDPAFFHA
LITCECGRSE WTVGDWKGYN SLCCNIKCKP ITIVTPKAVP GAVVITKAGI GAGLKCYNNV
FLKHIIDLVV PGTNLGWGVW RIAKVQSKDD VATSGNVLVD DPEDRLDPCY FGNDGPFATK
FKFQLLANSF DDEVKGAIVQ GVVHVNTAIC DVVKDILGLP WFVKKLGSLV TVMWDQFVAG
VQSMKICTLK VVQLAKALSC ATMSVVKGVI TLVAEVPEIF KRLFYTLTSA LKSLCTSSCD
ALVVAGKSFA KIGDYVLLPS ALVRLVSSKV KGKAQSGIKQ LQFATVVLGD THKVESDRVE
FSSVNLKMVD EEFPLNPVGH TVAVGNQAFF CSDGLYRFMA DRDLVITSPI FKPELELEPI
FECDAIPGFP KVAASNVAEL CVKVDTLLFN YDKIYKKYST IIKGDRCYIQ CTHTFKAPSY
YFDDDEFVEL CTKYYKLPDF DAFYNAVHAA TDMDQFCALC TSGFEVFIPR VPDCPPILND
IDGGSIWTSF ILSVRSATDF IKTLKIDLGL NGVVVFVTKK FRKAGALLQK LYNAFLDTVT
SFIKVAGVAF KYCATCVPKI VINGCYHTVT RLFAKDLQIP TEDGVADFNT FNHCVFPVNP
TRIETDSLEL EEVDFVEPGV DGKLVILDDY SFYSDGTNYY PSDGKGVVAS CFKKKGGGVV
TISDEVQVRT IDPVYKVRLE YEFEDETLVK VCEKAIGTKL KVTGDWSNLL ETLEKAMDVV
RQHLDVPDYF VYDEEGGTDL NLTIMVSQWP LSSDSEDDFK AVDDEPNANT DETVDTFAED
VAETQNVQQD VTQDEVEAVC DLVVKATEEG PIEHEELSED QKEVQQALAF IEDKPVVVKP
DVFAFSYASY GGLKVLNQSS NNCWVSSALV QLQLTGLLDS DEMQLFNAGR VSPMVKRCYE
SQRAIFGSLG DVSACLESLL KDRDGMSITC TIDCGCGPGV RVYENAIFRF TPLKTAFPMG
RCLICSKTLM HTITQMKGTG IFCRDATALD VDTLVVKPLC AAVYVGAQDG GHYLTNMYDA
NMAVDGHGRH PIKFNTINTL CYKDVDWEVS NGSCDVKPFL TYKNIEFYQG ELSALLSVNH
DFVVNAANEQ LSHGGGIAKA LDDLTKGELQ VLSNQYVSRN GSIKVGSGVL IKCKEHSILN
VVGPRKGKHA AELLTKAYTF VFKQKGVPLM PLLSVGIFKV PITESLAAFL ACVGDRVCKC
FCYTDKERLA IQNFVTSFQT EQPVEPLPVI QEVKGVQLEK PVPDVKVENP CEPFRIEGDA
KFYDLTPSMV QSLQVTRLVS FTNSDLCLGS FVRDCDGYVQ GSLGGAIANY KKSNPVLPAG
NCVTLKCDGF ISFTFVILPK EGDTNYEKNF NRAIAKFLKL KGSLLVVVED SSVFNKISHA
SVAGYVAKPA LVDTLFEAKP VQVVVTQDQR SFHTVELSTS QTYGQQLGDC VVEDKKVTNL
KPVSKDKVVS VVPNVDWDKH YGFVDAGIFH TLDHTMFVFD NNVVNGKRVL RTSDNNCWIN
AVCLQLQFAN AKFKPKGLQQ LWESYCTGDV AMFVHWLYWI TGVEKGEPSD AENTLNIISR
FLKPQGSVEM LRATSTTCDG TCSTKRVVST PVVNASVLKV GLDDGNCVHG LPLVDRVVSV
NGTVIITNVG DTPGKPVVAT ENLLLDGVSY TVFQDSTTGV GHYTVFDKEA KLMFDGDVLK
PCDLNVSPVT SVVVCNNKKI VVQDPVKRVE LDASKFLDTM NVASEKFFTF GDFVSRNIIV
LIVYLFSLLA ICFRALKKRD MKVMAGVPER TGIILKRSVK YNYKALKFFF RLKFQYIKVF
LKFSLVLYTL YALMFMFIRF TPVGTPICKR YTDGYANSTF DKNDYCGNVL CKICLYGYEE
LSDFTHTRVI WQHLKDPLIG NILPLFYLVF LIIFGGFFVR IGITYFIMQY INAAGVALGY
QDNVWLLHLL PFNSMGNIIV VAFIVTRILL FLKHVLFGCD KPSCIACSKS AKLTRVPLQT
ILQGVTKSFY VNANGGKKFC KKHNFFCVDC DSYGYGCTFI NDVIAPELSN VTKLNVIPTG
PATIIIDKVE FSNGFYYLYS GSTFWKYNFD ITEAKYACKD VLKNCNILTD FVVFNNSGSN
VTQVKNACVY FSQLLCKPIK LVDSALLASL NVDFSANLHK AFVEVLSNSF GKDLSNCSNM
NECRESLGLS DVPEEEFSAA VSEAHRYDVL ISDVSFNNLI VSYAKPEEKL AVHDIANCMR
VGAKVVNHNV LTKDNVPVVW LAKDFIALSE EARKYIVRTT KTKGINFMLT FNDRRMHLTI
PTISVANKKG AGLPSLFTRL YSFFWHLCVL IVVLFVATSL LDFSAQVTSD TQYDFKYIEN
GVLKVFEKPL DCVHNAFVNF NEWHNAKFGS IPTNSRRCPI VVGTSDEVRY IPGVPAGVFL
YGKSLIFAMS TIFGTSGLCF DDRGLTDPDS CIFNSACTTL SGIGGRNVYC YREGVVDNAK
LYSSLLPHSY YRLMDGNHIV LPEIITRGFG IRTIKTQAMT YCRTGECIDS QAGVCVGLDR
FFVYSKTPGS DYVCGTGFFS LLFNVIGMFS NSIPVTVMSG QILLNCVVAF TAVMACFAFT
KFKRLFGDMS FGVLSVGLCT VVNNLSYVVT QNSIGMLAYA TLYFLCTKGV RYSWVWHVGF
AISYCFLAPW WVVLAYLICA LLEFLPNLFK LKVSTQLFEG DKFVGSFESA ASGTFVLDMH
SYQKLANSIS TEKLKQYCAS YNRYKYYSGS ASEADYRLAC FAHLAKAMSD FANDHMDKLY
TPPTVSYNST LQAGLRKMAQ PSGIVEGCIV RVSYGNLTLN GLWLGDTVIC PRHVIASNTT
NVIDYDHAMS LVRLHNFSIS SGNMFLGVIS ASMRGTLLHI KVNQSNVNTP NYTYKVLKPG
DSFNILACYD GSAAGVYGVN MRTNYTIRGS FISGACGSPG YNINNGVVEF CYMHHLELGS
GCHVGSDMDG TMYGKYEDQP TLQIEGASNL VTENVCSWLY GALINGDRWW LSSVSVGVDT
YNEWALRNGM TALKNVDCFS LLVAKTGVDV GRLLASIQKL HGNFGGKSIL GCTSLCDEFT
LSEVVKQMYG VTLQSGKVSR AFRNASIVCC LLFLFLSEML NHSKLFWINP GYITPVFLAI
IVASSALMLL VKHKLLFLQL YLLPSLCIVS GYNIFKDYHF YTYMLEEFDY KVPFGGFNVT
GVLNISLCCF VMGLHTFRFL QTPNKIFSYV VAVLTVLYTY YYSTDVLGLI LTSMSGFTNY
WFIGTATYKL ATYVLPHTSL LDSFDAIKAV VFLYLLLGYC NCVYYGSLYW INRFCKLTLG
CYEFKVSAAE FKYMVANGLR APTGVFDALI LSLKLIGVGG RKTIKISSVQ SKLTDLKCTN
VVLLGCLSNM NIAANSREWA YCVDLHNKIN LCNDAEAAQE MLLALLAFFL SKNSAFGVDE
LLDSYFNDSS VLQSVAATYV NLPSYLAYET ARQSYEDALA NGSPPQLVKQ LRHAMNVAKS
EFDREASTQR KLDRMAEQAA SQMYKEARAV NRKSKVVSAM HSLLFGMLRR LDMSSVDTIL
SLAKDGVVPL SIIPAVSATK LNIVVSDIES YSKIQREGCV HYAGVIWSVV DIKDNDGKPV
HAKEVVTSNV ESLAWPLFLN CERIIKLQNN EIIPSKIKQR PIKAEGEGVV ADGNALYSNE
GGRTFMYAFI SDKPDLKVVK WEFDGGSNAI ELEPPCKFLV EAPSGPVVKY LYFVRNLNNL
RRGAVLGFIG ATVRLQAGKQ TEQATNSSLL TLCAFAVDPP KTYLDAVKSG HRPVGNCVKM
LANGSGNGQA ITNGVEASTN QDSYGGASVC LYCRAHVEHP DMDGFCKLRG KYVQVPLGTL
DPIRFVLENT VCKVCGCWQA NGCTCDRAVI QSVDSGYLNR VRGSSAARLE PLNGSDTHHV
FRAFDVYNRD VACISKFLKV NCVRLKNLDK HDAFWIVKKC TKSVMEHEQS IYNLISDCGA
VAKHDFFTWK EGRSVYGNVC RQDLTEYTMM DLCYALRNFD ENNCETLKKI LVVVGACDES
YFDNKLWFDP VENEDVHRVY AKLGTIVARA MLKCVKYCDA MVEQGIVGVI TLDNQDLNGD
FYDFGDFVTS VKGMGVPICT SYYSYMMPVM GMTNCLASEC FIKSDIFGED FRTFDLLAYD
FTEHKVNLFN KYFKHWGQTY HPNCEDCHDE SCIVHCANFN TLFATTIPIT AFGPLCRKCW
IDGVPLVTTA GYHFKQLGIV WNKDLNLHSS RLTINELLQF CADPSLLIAS SPALVDKRTV
CFSVAALGTG MTNQTVKPGH FNREFYDFLR SQGFFEEGSE LTLKHFFFAQ KGDAAVRDFD
YYRYNRTTVL DICQARVVYQ IVQCYFGMYE GGCITAKEVI VNNLNKSAGY PFNKFGKAGL
YYDSLSYEEQ DDLYAYTKRN IIPTMTQLNL KYAISGKDRA RTVGGVSLLS TMTTRQYHQK
HLKSIVNTRG ASVVIGTTKF YGGWDNMLKT LIKDVENPHL MGWDYPKCDR ALPNMIRMIS
AMILGSKHVN CCSSSDRYYR LCNELAQVLT EMVYSNGGFY VKPGGTTSGD ATTAYANSVF
NIFQATSANV NRLLSVDSNT CNNIEVKQLQ RKLYDCCYRS SSVDQSFVEE YFGYLRKHFS
MMILSDDGVV CYNSEYAALG YVADLNAFKA VLYYQNNVFM SASKCWIEPD INKGPHEFCS
QHTMQIVDKD GTYYLPYPDP SRILSAGVFV DDIVKTDPVI LLERYVSLAI DAYPLSKHDN
PEYRRVFTVM LDWVKHLYKT LNQGVLDSFS VTLLEDATAK FWDESFYASM YEQSSVLQSA
GLCVVCSSQT VLRCGDCIRR PMLCTKCAYD HVVSTSHKFI LAITPYVCCS SGCGVSDVTK
LYLGGLSYWC VDHKPRLSFP LCSSGNVFGL YKNSATGSPD VDDFNTLATS DWTDVKDYKL
ANDVKDSLRL FAAETIKAKE ESVKSSYACA TIHEVVGPKE LVLKWEVGKP RPPLSRNSVF
TCYHITKNTK FQVGEFTFEK LDYDNDAVSY KSTATTKLVP GMVFVLTSHN VQPLRAPTII
NQERYSTLHK LRPAFNIHED YSNLIPYYQL IGKQKLTTIQ GPPGSGKSHC VIGLGLYFPG
ARIVFTACSH AAVDSLCVKA ATAYSSDRCS RIIPQKARIE CYDGFKSNNT SAQYLFSTVN
ALPEVNADIC VVDEVSMCTN YDLSVINQRV NYRHIVYVGD PQQLPAPRVM ITRGVLVPED
YNVVTRRMCV LKPDIFLHKC YRCPAEIVNT VSEMVYENQF VPVKSESKEC FKIYCRGNVQ
VDNGSSINRR QLEVVRMFLA KNPKWAKAVF ISPYNSQNYV AGRVLGLQIQ TVDSSQGSEY
DYVIYTQTSD TAHASNVNRF NVAITRAKKG ILCIMCDREL FDILKFYELK LSDLQVGDGC
GLFKDCYKGE DNLPPSHAPT FMSLSDNFKT DKDLAVQIGV NGPVKYEHVI SFMGFRFDIN
VPNQHTLFCT RDFAMRNARG WLGFDVEGAH VIGSNVGTNV PLQLGFSNGV DFVVRPEGCV
STEVGDVIQP VRARAPPGDQ FTHLLPLLRK GQPWSVIRRR IVQMCSDYLA NLSDTLIFVL
WSGGLELTTM RYFVKLGPVQ TCDCGKRATC YNSTNHTFSC FRHALGSDYI YNCYCIDIQQ
WGYTGSLSMN HHEVCNIHRN EHVASGDAAM TRCLAIHDCF VKNVDWSITY PFIANEQAIN
KSGRLVQSHV MRAVLKLYNP KAIHDVGNPK GIRCVVTDAS WYCYDKNPTN TNVKMLEYDY
ITHGQLDGLC LFWNCNVDMY PEFSVVCRFD TRMRSTLNLE GCNGGSLYVN NHAFHTPAYD
KRAFAKLKAM PFFFYDDSEC EKLQDAVNYV PLRASNCITR CNVGGAVCSK HCALYHNYVM
AYNTFTTAGF TIWVPNSFDM FNLWQTFKNS NVQGLENIAY NVVKKGSFVG VEGELPVAVV
NDKVMVRDGV SDNVVFVNNT SLPTNVAFEL YAKRKVGLTP PLTILKNLGV VCTSKCVLWD
YEASRPLTTF TKDVCKYTDF DGDVCTLFDN SVPGAFERFT VTKNAVLISL TAVKKLTAIK
LTYGYLNGVP VFTHEDKPFT WYIYTRKDGA FVEYPDGYFT QGRVISDFQP RSNMEEDFLN
MDMGLFISKY GLEDYGFEHV VFGDVSKTTL GGLHLLISQI RLSKIGVLKV EDFVSSSDST
LKSCTVTYVD NPSSKMVCTY VDLLLDDFVN ILKSVDLSVV SKVHEVVIDC KVWRWMLWCK
DHKVQTFYPQ LQSAEWKCGY SMPSIYKIQR MCLEPCNLYN YGSGLKLPDG IMFNVVKYTQ
LCQYLNSTTM CVPHHMRVLH LGAGSDKGVA PGTAVLRRWL PLDAVIVDND VNDYVSDADF
SYTGDCASMY LTDKFDLVIS DMYDGRTKSC DGDNVSKEGF FPYINGVITE KLALGGTVAI
KITEFSWNKK LYELIQKFEY WTLFCTSVNT SSSEAFLIGV HFLGDFSTNA IIDGNIMHAN
YIFWRNSTIM TMSYNSVLDL SKFSCKHKAT VVVNLKDSSV TDLVLGLLKN GKLLIRNNGV
VCGFSNHLVN STK
