R1AB_PEDV7
ID R1AB_PEDV7 Reviewed; 6781 AA.
AC P0C6Y4; Q91AV2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Porcine epidemic diarrhea virus (strain CV777) (PEDV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Pedacovirus.
OX NCBI_TaxID=229032;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9782358; DOI=10.1007/978-1-4615-5331-1_101;
RA Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.;
RT "Further analysis of the genome of porcine epidemic diarrhea virus.";
RL Adv. Exp. Med. Biol. 440:781-786(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11724265; DOI=10.1023/a:1011831902219;
RA Kocherhans R., Bridgen A., Ackermann M., Tobler K.;
RT "Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome
RT sequence.";
RL Virus Genes 23:137-144(2001).
RN [3]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1), AND SUBCELLULAR LOCATION
RP (NON-STRUCTURAL PROTEIN 1).
RC STRAIN=USA/Colorado/2013;
RX PubMed=26773386; DOI=10.1016/j.virol.2015.12.010;
RA Zhang Q., Shi K., Yoo D.;
RT "Suppression of type I interferon production by porcine epidemic diarrhea
RT virus and degradation of CREB-binding protein by nsp1.";
RL Virology 489:252-268(2016).
RN [4]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1).
RC STRAIN=USA/Colorado/2013;
RX PubMed=28715653; DOI=10.1016/j.virol.2017.07.009;
RA Zhang Q., Ma J., Yoo D.;
RT "Inhibition of NF-kappaB activity by the porcine epidemic diarrhea virus
RT nonstructural protein 1 for innate immune evasion.";
RL Virology 510:111-126(2017).
CC -!- FUNCTION: The non-structural protein 1 (nsp1) protein plays a role in
CC the inhibition of host interferon and pro-inflammatory cytokines
CC production. Suppresses host RELA/p65 activation by blocking NFKBIA
CC phosphorylation (PubMed:28715653). Targets also the RLR pathway
CC downstream of the IRF3 activation by targeting host CREBBP to
CC proteasomal degradation (PubMed:26773386).
CC {ECO:0000269|PubMed:26773386, ECO:0000269|PubMed:28715653}.
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_0000037376; PRO_0000037375 [P0C6Y4]: rep; NbExp=3; IntAct=EBI-26366633, EBI-26366617;
CC PRO_0000037377; PRO_0000037377 [P0C6Y4]: rep; NbExp=3; IntAct=EBI-25590411, EBI-25590411;
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Host cytoplasm
CC {ECO:0000269|PubMed:26773386}. Host nucleus
CC {ECO:0000269|PubMed:26773386}.
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=P0C6Y4-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6V6-1; 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 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 -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK38661.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF353511; AAK38661.1; ALT_SEQ; Genomic_RNA.
DR RefSeq; NP_598309.2; NC_003436.1.
DR PDB; 5HIY; X-ray; 3.00 A; A/B/C=3858-3965.
DR PDB; 5HIZ; X-ray; 2.90 A; A/B=3858-3965.
DR PDBsum; 5HIY; -.
DR PDBsum; 5HIZ; -.
DR SMR; P0C6Y4; -.
DR IntAct; P0C6Y4; 1.
DR BindingDB; P0C6Y4; -.
DR MEROPS; C30.003; -.
DR PRIDE; P0C6Y4; -.
DR GeneID; 935181; -.
DR KEGG; vg:935181; -.
DR BRENDA; 3.4.22.B14; 8727.
DR BRENDA; 3.4.22.B50; 8727.
DR SABIO-RK; P0C6Y4; -.
DR Proteomes; UP000008159; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
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:0042025; C:host cell nucleus; IDA:UniProtKB.
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; IPI:IntAct.
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:0039644; P:suppression by virus of host NF-kappaB cascade; IDA:UniProtKB.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IDA:UniProtKB.
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; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 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; IPR011050; Pectin_lyase_fold/virulence.
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; 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 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; SSF51126; SSF51126; 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 nucleus; 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_0000037369"
FT CHAIN 111..895
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037370"
FT CHAIN 896..2516
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037371"
FT CHAIN 2517..2997
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037372"
FT CHAIN 2998..3299
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037373"
FT CHAIN 3300..3579
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037374"
FT CHAIN 3580..3662
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037375"
FT CHAIN 3663..3857
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037376"
FT CHAIN 3858..3965
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037377"
FT CHAIN 3966..4100
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037378"
FT CHAIN 4101..5027
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037379"
FT CHAIN 5028..5546
FT /note="Helicase"
FT /id="PRO_0000037380"
FT CHAIN 5547..6141
FT /note="Exoribonuclease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037381"
FT CHAIN 6142..6480
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037382"
FT CHAIN 6481..6781
FT /note="Putative 2'-O-methyl transferase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037383"
FT TRANSMEM 1959..1979
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2022..2042
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2105..2125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2127..2147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2150..2170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2528..2548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2619..2639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2654..2674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2754..2774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2787..2807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2814..2834
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2863..2883
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3336..3356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3361..3381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3399..3419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3431..3451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3454..3474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3476..3496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3500..3520
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..364
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 383..776
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 778..895
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 896..991
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1057..1296
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1297..1465
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1630..1685
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1691..1951
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 2412..2516
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 2902..2997
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 2998..3299
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3580..3662
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3663..3857
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3858..3965
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 3966..4103
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4106..4355
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4460..5027
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4707..4869
FT /note="RdRp catalytic"
FT DOMAIN 5028..5111
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5275..5466
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5467..5636
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5696..5910
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 5919..6140
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6142..6202
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6203..6320
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6337..6477
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6481..6777
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1162..1193
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4039..4055
FT /evidence="ECO:0000250"
FT ZN_FING 4081..4094
FT /evidence="ECO:0000250"
FT REGION 1009..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..2170
FT /note="HD1"
FT REGION 2528..2883
FT /note="HD2"
FT REGION 3336..3520
FT /note="HD3"
FT REGION 6031..6045
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1091
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1239
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1729
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1888
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3038
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3141
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 4854
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4855
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5716
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5896
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6609
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 4039
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4042
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4048
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4055
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4081
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4084
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 4094
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 5032
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5035
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5043
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
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 5053
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5056
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5060
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5066
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="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5082
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5099
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5310..5317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 5831
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5849
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5852
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5880
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5902
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5954..5960
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6069
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6086
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 6100
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 895..896
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 2516..2517
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 2997..2998
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3299..3300
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3579..3580
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3662..3663
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3857..3858
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3965..3966
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4100..4101
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5027..5028
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5546..5547
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6141..6142
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6480..6481
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT STRAND 3867..3874
FT /evidence="ECO:0007829|PDB:5HIZ"
FT STRAND 3879..3888
FT /evidence="ECO:0007829|PDB:5HIZ"
FT STRAND 3893..3903
FT /evidence="ECO:0007829|PDB:5HIZ"
FT STRAND 3907..3910
FT /evidence="ECO:0007829|PDB:5HIZ"
FT STRAND 3917..3921
FT /evidence="ECO:0007829|PDB:5HIZ"
FT STRAND 3925..3930
FT /evidence="ECO:0007829|PDB:5HIZ"
FT STRAND 3932..3943
FT /evidence="ECO:0007829|PDB:5HIZ"
FT HELIX 3948..3958
FT /evidence="ECO:0007829|PDB:5HIZ"
SQ SEQUENCE 6781 AA; 753158 MW; C5E29CBA752AD5BB CRC64;
MASNHVTLAF ANDAEISAFG FCTASEAVSY YSEAAASGFM QCRFVSLDLA DTVEGLLPED
YVMVVIGTTK LSAYVDTFGS RPRNICGWLL FSNCNYFLEE LELTFGRRGG NIVPVDQYMC
GADGKPVLQE SEWEYTDFFA DSEDGQLNIA GITYVKAWIV ERSDVSYASQ NLTSIKSITY
CSTYEHTFLD GTAMKVARTP KIKKNVVLSE PLATIYREIG SPFVDNGSDA RSIIRRPVFL
HAFVKCKCGS YHWTVGDWTS YVSTCCGFKC KPVLVASCSA MPGSVVVTRA GAGTGVKYYN
NMFLRHVADI DGLAFWRILK VQSKDDLACS GKFLEHHEEG FTDPCYFLND SSLATKLKFD
ILSGKFSDEV KQAIIAGHVV VGSALVDIVD DALGQPWFIR KLGDLASAPW EQLKAVVRGL
GLLSDEVVLF GKRLSCATLS IVNGVFEFLA DVPEKLAAAV TVFVNFLNEF FESACDCLKV
GGKTFNKVGS YVLFDNALVK LVKAKARGPR QAGICEVRYT SLVVGSTTKV VSKRVENANV
NLVVVDEDVT LNTTGRTVVV DGLAFFESDG FYRHLADADV VIEHPVYKSA CELKPVFECD
PIPDFPLPVA ASVAELCVQT DLLLKNYNTP YKTYSCVVRG DKCCITCTLQ FKAPSYVEDA
VNFVDLCTKN IGTAGFHEFY ITAHEQQDLQ GFLTTCCTMS GFECFMPTIP QCPAVLEEID
GGSIWRSFIT GLNTMWDFCK RLKVSFGLDG IVVTVARKFK RLGALLAEMY NTYLSTVVEN
LVLAGVSFKY YATSVPKIVL GGCFHSVKSV FASVFQIPVQ AGIEKFKVFL NCVHPVVPRV
IETSFVELEE TTFKPPALNG GIAIVDGFAF YYDGTLYYPT DGNSVVPICF KKKGGGDVKF
SDEVSVKTID PVYKVSLEFE FESETIMAVL NKAVGNRIKV TGGWDDVVEY INVAIEVLKD
HVEVPKYYIY DEEGGTDPNL PVMVSQWPLN DDTISQDLLD VEVVTDAPID SEGDEVDSSA
PEKVADVANS EPGDDGLPVA PETNVESEVE EVAATLSFIK DTPSTVTKDP FAFDFVSYGG
LKVLRQSHNN CWVTSTLVQL QLLGIVDDPA MELFSAGRVG PMVRKCYESQ KAILGSLGDV
SACLESLTKD LHTLKITCSV VCGCGTGERI YEGCAFRMTP TLEPFPYGAC AQCAQVLMHT
FKSIVGTGIF CRDTTALSLD SLVVKPLCAA AFIGKDSGHY VTNFYDAAMA IDGYGRHQIK
YDTLNTICVK DVNWTAPLVP AVDSVVEPVV KPFYSYKNVD FYQGDFSDLV KLPCDFVVNA
ANEKLSHGGG IAKAIDVYTK GMLQKCSNDY IKAHGPIKVG RGVMLEALGL KVFNVVGPRK
GKHAPELLVK AYKSVFANSG VALTPLISVG IFSVPLEESL SAFLACVGDR HCKCFCYGDK
EREAIIKYMD GLVDAIFKEA LVDTTPVQED VQQVSQKPVL PNFEPFRIEG AHAFYECNPE
GLMSLGADKL VLFTNSNLDF CSVGKCLNDV TSGALLEAIN VFKKSNKTVP AGNCVTLDCA
NMISITMVVL PFDGDANYDK NYARAVVKVS KLKGKLVLAV DDATLYSKLS HLSVLGFVST
PDDVERFYAN KSVVIKVTED TRSVKAVKVE STATYGQQIG PCLVNDTVVT DNKPVVADVV
AKVVPNANWD SHYGFDKAGE FHMLDHTGFT FPSEVVNGRR VIKTTDNNCW VNVTCLQLQF
ARFRFKSAGL QAMWESYCTG DVAMFVHWLY WLTGVDKGQP SDSENALNML SKYIVPAGSV
TIERVTHDGC CCSKRVVTAP VVNASVLKLG VEDGLCPHGL NYIGKVVVVK GTTIVVNVGK
PVVAPSHLFL KGVSYTTFLD NGNGVVGHYT VFDHGTGMVH DGDAFVPGDL NVSPVTNVVV
SEQTAVVIKD PVKKAELDAT KLLDTMNYAS ERFFSFGDFM SRNLITVFLY ILSILGLCFR
AFRKRDVKVL AGVPQRTGII LRKSMRYNAK ALGVFFKLKL YWFKVLGKFS LGIYALYALL
FMTIRFTPIG SPVCDDVVAG YANSSFDKNE YCNSVICKVC LYGYQELSDF SHTQVVWQHL
RDPLIGNVMP FFYLAFLAIF GGVYVKAITL YFIFQYLNSL GVFLGLQQSI WFLQLVPFDV
FGDEIVVFFI VTRVLMFIKH VCLGCDKASC VACSKSARLK RVPVQTIFQG TSKSFYVHAN
GGSKFCKKHN FFCLNCDSYG PGCTFINDVI ATEVGNVVKL NVQPTGPATI LIDKVEFSNG
FYYLYSGDTF WKYNFDITDS KYTCKEALKN CSIITDFIVF NNNGSNVNQV KNACVYFSQM
LCKPVKLVDS ALLASLSVDF GASLHSAFVS VLSNSFGKDL SSCNDMQDCK STLGFDDVPL
DTFNAAVAEA HRYDVLLTDM SFNNFTTSYA KPEEKFPVHD IATCMRVGAK IVNHNVLVKD
SIPVVWLVRD FIALSEETRK YIIRTTKVKG ITFMLTFNDC RMHTTIPTVC IANKKGAGLP
SFSKVKKFFW FLCLFIVAAF FALSFLDFST QVSSDSDYDF KYIESGQLKT FDNPLSCVHN
VFINFDQWHD AKFGFTPVNN PSCPIVVGVS DEARTVPGIP AGVYLAGKTL VFAINTIFGT
SGLCFDASGV ADKGACIFNS ACTTLSGLGG TAVYCYKNGL VEGAKLYSEL APHSYYKMVD
GNAVSLPEII SRGFGIRTIR TKAMTYCRVG QCVQSAEGVC FGADRFFVYN AESGSDFVCG
TGLFTLLMNV ISVFSKTVPV TVLSGQILFN CIIAFVAVAV CFLFTKFKRM FGDMSVGVFT
VGACTLLNNV SYIVTQNTLG MLGYATLYFL CTKGVRYMWI WHLGFLISYI LIAPWWVLMV
YAFSAIFEFM PNLFKLKVST QLFEGDKFVG SFENAAAGTF VLDMHAYERL ANSISTEKLR
QYASTYNKYK YYSGSASEAD YRLACFAHLA KAMMDYASNH NDTLYTPPTV SYNSTLQAGL
RKMAQPSGVV EKCIVRVCYG NMALNGLWLG DIVMCPRHVI ASSTTSTIDY DYALSVLRLH
NFSISSGNVF LGVVSATMRG ALLQIKVNQN NVHTPKYTYR TVRPGESFNI LACYDGAAAG
VYGVNMRSNY TIRGSFINGA CGSPGYNINN GTVEFCYLHQ LELGSGCHVG SDLDGVMYGG
YEDQPTLQVE GASSLFTENV LAFLYAALIN GSTWWLSSSR IAVDRFNEWA VHNGMTTVGN
TDCFSILAAK TGVDVQRLLA SIQSLHKNFG GKQILGHTSL TDEFTTGEVV RQMYGVNLQG
GYVSRACRNV LLVGSFLTFF WSELVSYTKF FWVNPGYVTP MFACLSLLSS LLMFTLKHKT
LFFQVFLIPA LIVTSCINLA FDVEVYNYLA EHFDYHVSLM GFNAQGLVNI FVCFVVTILH
GTYTWRFFNT PASSVTYVVA LLTAAYNYFY ASDILSCAMT LFASVTGNWF VGAVCYKVAV
YMALRFPTFV AIFGDIKSVM FCYLVLGYFT CCFYGILYWF NRFFKVSVGV YDYTVSAAEF
KYMVANGLRA PTGTLDSLLL SAKLIGIGGE RNIKISSVQS KLTDIKCSNV VLLGCLSSMN
VSANSTEWAY CVDLHNKINL CNDPEKAQEM LLALLAFFLS KNSAFGLDDL LESYFNDNSM
LQSVASTYVG LPSYVIYENA RQQYEDAVNN GSPPQLVKQL RHAMNVAKSE FDREASTQRK
LDRMAEQAAA QMYKEARAVN RKSKVVSAMH SLLFGMLRRL DMSSVDTILN LAKDGVVPLS
VIPAVSATKL NIVTSDIDSY NRIQREGCVH YAGTIWNIID IKDNDGKVVH VKEVTAQNAE
SLSWPLVLGC ERIVKLQNNE IIPGKLKQRS IKAEGDGIVG EGKALYNNEG GRTFMYAFIS
DKPDLRVVKW EFDGGCNTIE LEPPRKFLVD SPNGAQIKYL YFVRNLNTLR RGAVLGYIGA
TVRLQAGKQT EQAINSSLLT LCAFAVDPAK TYIDAVKSGH KPVGNCVKML ANGSGNGQAV
TNGVEASTNQ DSYGGASVCL YCRAHVEHPS MDGFCRLKGK YVQVPLGTVD PIRFVLENDV
CKVCGCWLSN GCTCDRSIMQ STDMAYLNRV RGSSAARLEP CNGTDTQHVY RAFDIYNKDV
ACLGKFLKVN CVRLKNLDKH DAFYVVKRCT KSAMEHEQSI YSRLEKCGAI AEHDFFTWKD
GRAIYGNVCR KDLTEYTMMD LCYALRNFDE NNCDVLKSIL IKVGACEESY FNNKVWFDPV
ENEDIHRVYA LLGTIVARAM LKCVKFCDAM VEQGIVGVVT LDNQDLNGDF YDFGDFTCSI
KGMGVPICTS YYSYMMPVMG MTNCLASECF VKSDIFGEDF KSYDLLEYDF TEHKTALFNK
YFKYWGLQYH PNCVDCSDEQ CIVHCANFNT LFSTTIPITA FGPLCRKCWI DGVPLVTTAG
YHFKQLGIVW NNDLNLHSSR LSINELLQFC SDPALLIASS PALVDQRTVC FSVAALGTGM
TNQTVKPGHF NKEFYDFLLE QGFFSEGSEL TLKHFFFAQK VDAAVKDFDY YRYNRPTVLD
ICQARVVYQI VQRYFDIYEG GCITAKEVVV TNLNKSAGYP LNKFGKAGLY YESLSYEEQD
ELYAYTKRNI LPTMTQLNLK YAISGKERAR TVGGVSLLST MTTRQYHQKH LKSIVNTRGA
SVVIGTTKFY GGWDNMLKNL IDGVENPCLM GWDYPKCDRA LPNMIRMISA MILGSKHTTC
CSSTDRFFRL CNELAQVLTE VVYSNGGFYL KPGGTTSGDA TTAYANSVFN IFQAVSANVN
KLLSVDSNVC HNLEVKQLQR KLYECCYRST IVDDQFVVEY YGYLRKHFSM MILSDDGVVC
YNNDYASLGY VADLNAFKAV LYYQNNVFMS ASKCWIEPDI NKGPHEFCSQ HTMQIVDKEG
TYYLPYPDPS RILSAGVFVD DVVKTDAVVL LERYVSLAID AYPLSKHENP EYKKVFYVLL
DWVKHLYKTL NAGVLESFSV TLLEDSTAKF WDESFYANMY EKSAVLQSAG LCVVCGSQTV
LRCGDCLRRP MLCTKCAYDH VIGTTHKFIL AITPYVCCAS DCGVNDVTKL YLGGLSYWCH
EHKPRLAFPL CSAGNVFGLY KNSATGSPDV EDFNRIATSD WTDVSDYRLA NDVKDSLRLF
AAETIKAKEE SVKSSYACAT LHEVVGPKEL LLKWEVGRPK PPLNRNSVFT CYHITKNTKF
QIGEFVFEKA EYDNDAVTYK TTATTKLVPG MVFVLTSHNV QPLRAPTIAN QERYSTIHKL
HPAFNIPEAY SSLVPYYQLI GKQKITTIQG PPGSGKSHCV IGLGLYYPGA RIVFTACSHA
AVDSLCVKAS TAYSNDKCSR IIPQRARVEC YDGFKSNNTS AQYLFSTVNA LPECNADIVV
VDEVSMCTNY DLSVINQRIS YRHVVYVGDP QQLPAPRVMI SRGTLEPKDY NVVTQRMCAL
KPDVFLHKCY RCPAEIVRTV SEMVYENQFI PVHPDSKQCF KIFCKGNVQV DNGSSINRRQ
LDVVRMFLAK NPRWSKAVFI SPYNSQNYVA SRLLGLQIQT VDSSQGSEYD YVIYAQTSDT
AHASNVNRFN VAITRAKKGI LCIMCDRSLF DLLKFFELKL SDLQANEGCG LFKDCSRGDD
LLPPSHANTF MSLADNFKTD QYLAVQIGVN GPIKYEHVIS FMGFRFDINI PNHHTLFCTR
DFAMRNVRGW LGFDVEGAHV VGSNVGTNVP LQLGFSNGVD FVVRPEGCVV TESGDYIKPV
RARAPPGEQF AHLLPLLKRG QPWDVVRKRI VQMCSDYLAN LSDILIFVLW AGGLELTTMR
YFVKIGPSKS CDCGKVATCY NSALHTYCCF KHALGCDYLY NPYCIDIQQW GYKGSLSLNH
HEHCNVHRNE HVASGDAIMT RCLAIHDCFV KNVDWSITYP FIGNEAVINK SGRIVQSHTM
RSVLKLYNPK AIYDIGNPKG IRCAVTDAKW FCFDKNPTNS NVKTLEYDYI THGQFDGLCL
FWNCNVDMYP EFSVVCRFDT RCRSPLNLEG CNGGSLYVNN HAFHTPAFDK RAFAKLKPMP
FFFYDDTECD KLQDSINYVP LRASNCITKC NVGGAVCSKH CAMYHSYVNA YNTFTSAGFT
IWVPTSFDTY NLWQTFSNNL QGLENIAFNV LKKGSFVGDE GELPVAVVND KVLVRDGTVD
TLVFTNKTSL PTNVAFELYA KRKVGLTPPI TILRNLGVVC TSKCVIWDYE AERPLTTFTK
DVCKYTDFEG DVCTLFDNSI VGSLERFSMT QNAVLMSLTA VKKLTGIKLT YGYLNGVPVN
THEDKPFTWY IYTRKNGKFE DYPDGYFTQG RTTADFSPRS DMEKDFLSMD MGLFINKYGL
EDYGFEHVVY GDVSKTTLGG LHLLISQVRL ACMGVLKIDE FVSSNDSTLK SCTVTYADNP
SSKMVCTYMD LLLDDFVSIL KSLDLSVVSK VHEVMVDCKM WRWMLWCKDH KLQTFYPQLQ
ASEWKCGYSM PSIYKIQRMC LEPCNLYNYG AGVKLPDGIM FNVVKYTQLC QYLNSTTMCV
PHHMRVLHLG AGSDKGVAPG TAVLRRWLPL DAIIVDNDSV DYVSDADYSV TGDCSTLYLS
DKFDLVISDM YDGKIKSCDG ENVSKEGFFP YINGVITEKL ALGGTVAIKV TEFSWNKKLY
ELIQKFEYWT MFCTSVNTSS SEAFLIGVHY LGDFASGAVI DGNTMHANYI FWRNSTIMTM
SYNSVLDLSK FNCKHKATVV VNLKDSSISD VVLGLLKNGK LLVRNNDAIC GFSNHLVNVN
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