R1AB_CVPPU
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 03-AUG-2022, entry version 94.
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 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.
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: 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_0000037393; PRO_0000037392 [P0C6Y5]: rep; NbExp=2; IntAct=EBI-25684354, EBI-26366034;
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=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 PRIDE; P0C6Y5; -.
DR EvolutionaryTrace; P0C6Y5; -.
DR Proteomes; UP000001440; 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..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="Non-structural protein 9"
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"
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 2279..2384
FT /note="CoV Nsp3 Y3"
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 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..5011
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"
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 2401..2766
FT /note="HD2"
FT REGION 3187..3414
FT /note="HD3"
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 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 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 /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 3937
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3940
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3946
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3953
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3979
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3982
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3990
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3992
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4932
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4935
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4943
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4946
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4953
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4956
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4966
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4977
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4982
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4999
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
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 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="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5735
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5751
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5754
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5782
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5786
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5789
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
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="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5988
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5999
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6002
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 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 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
