R1AB_CVHN1
ID R1AB_CVHN1 Reviewed; 7182 AA.
AC P0C6X2; Q5MQD2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Host translation inhibitor nsp1;
DE Short=nsp1;
DE AltName: Full=p28;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p65;
DE Contains:
DE RecName: Full=Papain-like proteinase;
DE Short=PL-PRO;
DE EC=3.4.19.12;
DE EC=3.4.22.-;
DE AltName: Full=Non-structural protein 3;
DE Short=nsp3;
DE AltName: Full=p210;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE AltName: Full=Peptide HD2;
DE AltName: Full=p44;
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=p27;
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=p10;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE AltName: Full=p22;
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=p15;
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=p67;
DE Contains:
DE RecName: Full=Guanine-N7 methyltransferase;
DE Short=ExoN;
DE EC=2.1.1.-;
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=p35;
DE Contains:
DE RecName: Full=2'-O-methyltransferase;
DE EC=2.1.1.57;
DE AltName: Full=nsp16;
GN Name=rep; ORFNames=1a-1b;
OS Human coronavirus HKU1 (isolate N1) (HCoV-HKU1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=443239;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15613317; DOI=10.1128/jvi.79.2.884-895.2005;
RA Woo P.C.Y., Lau S.K.P., Chu C.-M., Chan K.-H., Tsoi H.-W., Huang Y.,
RA Wong B.H.L., Poon R.W.S., Cai J.J., Luk W.-K., Poon L.L.M., Wong S.S.Y.,
RA Guan Y., Peiris J.S.M., Yuen K.-Y.;
RT "Characterization and complete genome sequence of a novel coronavirus,
RT coronavirus HKU1, from patients with pneumonia.";
RL J. Virol. 79:884-895(2005).
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:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation
CC by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome
CC complex further induces an endonucleolytic cleavage near the 5'UTR of
CC host mRNAs, targeting them for degradation. Viral mRNAs are not
CC susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the
CC presence of a 5'-end leader sequence and are therefore protected from
CC degradation. By suppressing host gene expression, nsp1 facilitates
CC efficient viral gene expression in infected cells and evasion from host
CC immune response. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
CC of host cell survival signaling pathway by interacting with host PHB
CC and PHB2. Indeed, these two proteins play a role in maintaining the
CC functional integrity of the mitochondria and protecting cells from
CC various stresses. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Papain-like proteinase]: Responsible for the cleavages
CC located at the N-terminus of the replicase polyprotein. In addition,
CC PL-PRO possesses a deubiquitinating/deISGylating activity and processes
CC both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular
CC substrates. Participates together with nsp4 in the assembly of virally-
CC induced cytoplasmic double-membrane vesicles necessary for viral
CC replication. Antagonizes innate immune induction of type I interferon
CC by blocking the phosphorylation, dimerization and subsequent nuclear
CC translocation of host IRF3. Prevents also host NF-kappa-B signaling.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 4]: Participates in the assembly of
CC virally-induced cytoplasmic double-membrane vesicles necessary for
CC viral replication. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [3C-like proteinase]: Cleaves the C-terminus of replicase
CC polyprotein at 11 sites. Recognizes substrates containing the core
CC sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-
CC phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE-
CC ProRule:PRU00772}.
CC -!- FUNCTION: [Non-structural protein 6]: Plays a role in the initial
CC induction of autophagosomes from host reticulum endoplasmic. Later,
CC limits the expansion of these phagosomes that are no longer able to
CC deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 9]: May participate in viral
CC replication by acting as a ssRNA-binding protein.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
CC 2'-O-methyltransferase activities. Therefore plays an essential role in
CC viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
CC and transcription of the viral RNA genome.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Helicase]: Multi-functional protein with a zinc-binding
CC domain in N-terminus displaying RNA and DNA duplex-unwinding activities
CC with 5' to 3' polarity. Activity of helicase is dependent on magnesium.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Guanine-N7 methyltransferase]: Enzyme possessing two
CC different activities: an exoribonuclease activity acting on both ssRNA
CC and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase
CC activity. {ECO:0000250|UniProtKB:P0C6X7}.
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 -!- FUNCTION: [2'-O-methyltransferase]: Methyltransferase that mediates
CC mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
CC mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16.
CC Therefore plays an essential role in viral mRNAs cap methylation which
CC is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
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: [Papain-like proteinase]:
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: [2'-O-methyltransferase]:
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: Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as
CC monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the
CC homodimer shows catalytic activity. Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts
CC with nsp14 and nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Papain-like proteinase]: Host membrane; Multi-
CC pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-
CC pass membrane protein. Host cytoplasm. Note=Localizes in virally-
CC induced cytoplasmic double-membrane vesicles.
CC {ECO:0000250|UniProtKB:P0C6X7}.
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.
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.
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.
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.
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.
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=P0C6X2-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6U3-1; 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: Isolate N1 belongs to genotype A.
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; AY597011; AAT98578.1; -; Genomic_RNA.
DR RefSeq; YP_173236.1; NC_006577.2.
DR SMR; P0C6X2; -.
DR PRIDE; P0C6X2; -.
DR DNASU; 3200429; -.
DR GeneID; 3200429; -.
DR KEGG; vg:3200429; -.
DR SABIO-RK; P0C6X2; -.
DR Proteomes; UP000008170; 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: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: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:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
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:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21519; cv_beta_Nsp2_MHV-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21593; HCoV_HKU1-like_RdRp; 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; cd21467; Ubl1_cv_Nsp3_N-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; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 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; 3.40.50.11020; -; 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; IPR022570; B-CoV_A_NSP1.
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; IPR022733; DPUP_SUD_C_bCoV.
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; IPR044315; NSP14_betaCoV.
DR InterPro; IPR009466; NSP14_CoV.
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; IPR044384; NSP2_MHV-like.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044367; NSP6_betaCoV.
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; IPR002705; Pept_C30/C16_B_coronavir.
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; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR044347; RdRp_HCoV_HKU1-like.
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; PF16251; bCoV_NAR; 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; 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; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF11963; DUF3477; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF01831; Peptidase_C16; 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; SSF159936; SSF159936; 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; PS51963; BCOV_NSP1_C; 1.
DR PROSITE; PS51942; BCOV_NSP3C_C; 1.
DR PROSITE; PS51994; BCOV_NSP3E_G2M; 1.
DR PROSITE; PS51945; BCOV_NSP3E_NAB; 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 3: Inferred from homology;
KW Activation of host autophagy by virus; ATP-binding;
KW Decay of host mRNAs by virus; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
KW Host cytoplasm; Host gene expression shutoff by virus; Host membrane;
KW Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 by virus; Inhibition of host NF-kappa-B 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..222
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093333"
FT CHAIN 223..809
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093334"
FT CHAIN 810..2838
FT /note="Papain-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093335"
FT CHAIN 2839..3334
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093336"
FT CHAIN 3335..3637
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093337"
FT CHAIN 3638..3924
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093338"
FT CHAIN 3925..4016
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093339"
FT CHAIN 4017..4210
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093340"
FT CHAIN 4211..4320
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093341"
FT CHAIN 4321..4457
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093342"
FT CHAIN 4458..5385
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093343"
FT CHAIN 5386..5988
FT /note="Helicase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093344"
FT CHAIN 5989..6509
FT /note="Guanine-N7 methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093345"
FT CHAIN 6510..6883
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093346"
FT CHAIN 6884..7182
FT /note="2'-O-methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_5000093347"
FT TRANSMEM 2226..2246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2287..2307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2318..2338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2401..2421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2443..2463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2844..2864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3119..3139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3151..3171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3178..3198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3203..3223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3651..3671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3676..3696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3701..3721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3744..3764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3772..3792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3800..3820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3843..3863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 54..174
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 192..222
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 226..488
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 493..681
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 697..809
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 811..923
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REPEAT 945..954
FT /note="1"
FT REPEAT 955..964
FT /note="2"
FT REPEAT 965..974
FT /note="3"
FT REPEAT 975..984
FT /note="4"
FT REPEAT 985..994
FT /note="5"
FT REPEAT 995..1004
FT /note="6"
FT REPEAT 1005..1014
FT /note="7"
FT REPEAT 1015..1024
FT /note="8"
FT REPEAT 1025..1034
FT /note="9"
FT REPEAT 1035..1044
FT /note="10"
FT REPEAT 1045..1054
FT /note="11"
FT REPEAT 1055..1064
FT /note="12"
FT REPEAT 1065..1074
FT /note="13"
FT REPEAT 1075..1084
FT /note="14"
FT DOMAIN 1123..1373
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1351..1522
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1578..1649
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1649..1704
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1718..1978
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1992..2093
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2108..2257
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2735..2838
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3237..3334
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3335..3637
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3925..4013
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 4014..4210
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4211..4320
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4321..4458
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4463..4718
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4818..5385
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 5065..5227
FT /note="RdRp catalytic"
FT DOMAIN 5386..5469
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5641..5822
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5823..5992
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 6059..6274
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6283..6509
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6510..6570
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6571..6691
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6741..6880
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6885..7179
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1238..1266
FT /note="C4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 1835..1871
FT /note="C4-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4394..4410
FT /evidence="ECO:0000250"
FT ZN_FING 4436..4449
FT /evidence="ECO:0000250"
FT REGION 365..389
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 945..1084
FT /note="14 X 10 AA tandem repeat of N-[DN]-D-E-D-V-V-T-G-D"
FT REGION 946..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2226..2463
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2844..3223
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3651..3863
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 6396..6410
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1161
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1312
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1757
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1914
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3375
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3479
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 5212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 6077
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6079
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6786
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6929
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 7013
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 7053
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 7086
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 5390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5666..5673
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 6194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6318..6324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 222..223
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 809..810
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 2838..2839
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 3334..3335
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3637..3638
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3924..3925
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4016..4017
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4210..4211
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4320..4321
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4457..4458
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5385..5386
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6509..6510
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6883..6884
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
SQ SEQUENCE 7182 AA; 810941 MW; 663B34161D6248BC CRC64;
MIKTSKYGLG FKWAPEFRWL LPDAAEELAS PMKSDEGGLC PSTGQAMESV GFVYDNHVKI
DCRCILGQEW HVQSNLIRDI FVHEDLHVVE VLTKTAVKSG TAILIKSPLH SLGGFPKGYV
MGLFRSYKTK RYVVHHLSMT TSTTNFGEDF LGWIVPFGFM PSYVHKWFQF CRLYIEESDL
IISNFKFDDY DFSVEDAYAE VHAEPKGKYS QKAYALLRQY RGIKPVLFVD QYGCDYSGKL
ADCLQAYGHY SLQDMRQKQS VWLANCDFDI VVAWHVVRDS RFVMRLQTIA TICGIKYVAQ
PTEDVVDGDV VIREPVHLLS ADAIVLKLPS LMKVMTHMDD FSIKSIYNVD LCDCGFVMQY
GYVDCFNDNC DFYGWVSGNM MDGFSCPLCC TVYDSSEVKA QSSGVIPENP VLFTNSTDTV
NHDSFNLYGY SVTPFGSCIY WSPRPGLWIP IIKSSVKSYD DLVYSGVVGC KSIVKETALI
THALYLDYVQ CKCGNLEQNH ILGVNNSWCR QLLLNRGDYN MLLKNIDLFV KRRADFACKF
AVCGDGFVPF LLDGLIPRSY YLIQSGIFFT SLMSQFSQEV SDMCLKMCIL FMDRVSVATF
YIEHYVNRLV TQFKLLGTTL VNKMVNWFNT MLDASAPATG WLLYQLLNGL FVVSQANFNF
VALIPDYAKI LVNKFYTFFK LLLECVTVDV LKDMPVLKTI NGLVCIVGNK FYNVSTGLIP
GFVLPCNAQE QQIYFFEGVA ESVIVEDDVI ENVKSSLSSY EYCQPPKSVE KICIIDNMYM
GKCGDKFFPI VMNDKNICLL DQAWRFPCAG RKVNFNEKPV VMEIPSLMTV KVMFDLDSTF
DDILGKVCSE FEVEKGVTVD DFVAVVCDAI ENALNSCKEH PVVGYQVRAF LNKLNENVVY
LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
VTGDNNDEEI VTGDNDDQIV VTGDDVDDIE SIYDFDTYKA LLVFNDVYND ALFVSYGSSV
ETETYFKVNG LWSPTITHTN CWLRSVLLVM QKLPFKFKDL AIENMWLSYK VGYNQSFVDY
LLTTIPKAIV LPQGGFVADF AYWFLNQFDI NAYANWCCLK CGFSFDLNGL DALFFYGDIV
SHVCKCGHNM TLIAADLPCT LHFSLFDDNF CAFCTPKKIF IAACAVDVNV CHSVAVIGDE
QIDGKFVTKF SGDKFDFIVG YGMSFSMSSF ELPQLYGLCI TPNVCFVKGD IINVARLVKA
DVIVNPANGH MLHGGGVAKA IAVAAGKKFS KETAAMVKSK GVCQVGDCYV STGGKLCKTI
LNIVGPDARQ DGRQSYVLLA RAYKHLNNYD CCLSTLISAG IFSVPADVSL TYLLGVVDKQ
VILVSNNKED FDIIQKCQIT SVVGTKALAV RLTANVGRVI KFETDAYKLF LSGDDCFVSN
SSVIQEVLLL RHDIQLNNDV RDYLLSKMTS LPKDWRLINK FDVINGVKTV KYFECPNSIY
ICSQGKDFGY VCDGSFYKAT VNQVCVLLAK KIDVLLTVDG VNFKSISLTV GEVFGKILGN
VFCDGIDVTK LKCSDFYADK ILYQYENLSL ADISAVQSSF GFDQQQLLAY YNFLTVCKWS
VVVNGPFFSF EQSHNNCYVN VACLMLQHIN LKFNKWQWQE AWYEFRAGRP HRLVALVLAK
GHFKFDEPSD ATDFIRVVLK QADLSGAICE LELICDCGIK QESRVGVDAV MHFGTLAKTD
LFNGYKIGCN CAGRIVHCTK LNVPFLICSN TPLSKDLPDD VVAANMFMGV GVGHYTHLKC
GSPYQHYDAC SVKKYTGVSG CLTDCLYLKN LTQTFTSMLT NYFLDDVEMV AYNPDLSQYY
CDNGKYYTKP IIKAQFKPFA KVDGVYTNFK LVGHDICAQL NDKLGFNVDL PFVEYKVTVW
PVATGDVVLA SDDLYVKRYF KGCETFGKPV IWFCHDEASL NSLTYFNKPS FKSENRYSVL
SVDSVSEESQ GNVVTSVMES QISTKEVKLK GVRKTVKIED AIIVNDENSS IKVVKSLSLV
DVWDMYLTGC DYVVWVANEL SRLVKSPTVR EYIRYGIKPI TIPIDLLCLR DDNQTLLVPK
IFKARAIEFY GFLKWLFIYV FSLLHFTNDK TIFYTTEIAS KFTFNLFCLA LKNAFQTFRW
SIFIKGFLVV ATVFLFWFNF LYINVIFSDF YLPNISVFPI FVGRIVMWIK ATFGLVTICD
FYSKLGVGFT SHFCNGSFIC ELCHSGFDML DTYAAIDFVQ YEVDRRVLFD YVSLVKLIVE
LVIGYSLYTV WFYPLFCLIG LQLFTTWLPD LFMLETMHWL IRFIVFVANM LPAFVLLRFY
IVVTAMYKVV GFIRHIVYGC NKAGCLFCYK RNCSVRVKCS TIVGGVIRYY DITANGGTGF
CVKHQWNCFN CHSFKPGNTF ITVEAAIELS KELKRPVNPT DASHYVVTDI KQVGCMMRLF
YDRDGQRVYD DVDASLFVDI NNLLHSKVKV VPNLYVVVVE SDADRANFLN AVVFYAQSLY
RPILLVDKKL ITTACNGISV TQTMFDVYVD TFMSHFDVDR KSFNNFVNIA HASLREGVQL
EKVLDTFVGC VRKCCSIDSD VETRFITKSM ISAVAAGLEF TDENYNNLVP TYLKSDNIVA
ADLGVLIQNG AKHVQGNVAK AANISCIWFI DAFNQLTADL QHKLKKACVK TGLKLKLTFN
KQEASVPILT TPFSLKGGVV LSNLLYILFF VSLICFILLW ALLPTYSVYK SDIHLPAYAS
FKVIDNGVVR DISVNDLCFA NKFFQFDQWY ESTFGSVYYH NSMDCPIVVA VMDEDIGSTM
FNVPTKVLRH GFHVLHFLTY AFASDSVQCY TPHIQISYND FYASGCVLSS LCTMFKRGDG
TPHPYCYSDG VMKNASLYTS LVPHTRYSLA NSNGFIRFPD VISEGIVRIV RTRSMTYCRV
GACEYAEEGI CFNFNSSWVL NNDYYRSMPG TFCGRDLFDL FYQFFSSLIR PIDFFSLTAS
SIFGAILAIV VVLVFYYLIK LKRAFGDYTS VVVINVVVWC INFLMLFVFQ VYPICACVYA
CFYFYVTLYF PSEISVIMHL QWIVMYGAIM PFWFCVTYVA MVIANHVLWL FSYCRKIGVN
VCSDSTFEET SLTTFMITKD SYCRLKNSVS DVAYNRYLSL YNKYRYYSGK MDTAAYREAA
CSQLAKAMET FNHNNGNDVL YQPPTASVST SFLQSGIVKM VSPTSKIEPC IVSVTYGSMT
LNGLWLDDKV YCPRHVICSS SNMNEPDYSA LLCRVTLGDF TIMSGRMSLT VVSYQMQGCQ
LVLTVSLQNP YTPKYTFGNV KPGETFTVLA AYNGRPQGAF HVTMRSSYTI KGSFLCGSCG
SVGYVLTGDS VKFVYMHQLE LSTGCHTGTD FTGNFYGPYR DAQVVQLPVK DYVQTVNVIA
WLYAAILNNC AWFVQNDVCS TEDFNVWAMA NGFSQVKADL VLDALASMTG VSIETLLAAI
KRLYMGFQGR QILGSCTFED ELAPSDVYQQ LAGVKLQSKT KRFIKETIYW ILISTFLFSC
IISAFVKWTI FMYINTHMIG VTLCVLCFVS FMMLLVKHKH FYLTMYIIPV LCTLFYVNYL
VVYKEGFRGF TYVWLSYFVP AVNFTYVYEV FYGCILCVFA IFITMHSINH DIFSLMFLVG
RIVTLISMWY FGSNLEEDVL LFITAFLGTY TWTTILSLAI AKIVANWLSV NIFYFTDVPY
IKLILLSYLF IGYILSCYWG FFSLLNSVFR MPMGVYNYKI SVQELRYMNA NGLRPPRNSF
EAILLNLKLL GIGGVPVIEV SQIQSKLTDV KCANVVLLNC LQHLHVASNS KLWQYCSVLH
NEILSTSDLS VAFDKLAQLL IVLFANPAAV DTKCLASIDE VSDDYVQDST VLQALQSEFV
NMASFVEYEV AKKNLADAKN SGSVNQQQIK QLEKACNIAK SVYERDKAVA RKLERMADLA
LTNMYKEARI NDKKSKVVSA LQTMLFSMVR KLDNQALNSI LDNAVKGCVP LSAIPALAAN
TLTIVIPDKQ VFDKVVDNVY VTYAGSVWHI QTVQDADGIN KQLTDISVDS NWPLVIIANR
YNEVANAVMQ NNELMPHKLK IQVVNSGSDM NCNIPTQCYY NNGSSGRIVY AVLSDVDGLK
YTKIMKDDGN CVVLELDPPC KFSIQDVKGL KIKYLYFIKG CNTLARGWVV GTLSSTIRLQ
AGVATEYAAN SSILSLCAFS VDPKKTYLDY IQQGGVPIIN CVKMLCDHAG TGMAITIKPE
ATINQDSYGG ASVCIYCRAR VEHPDVDGIC KLRGKFVQVP LGIKDPILYV LTHDVCQVCG
FWRDGSCSCV GSSVAVQSKD LNFLNRVRGT SVNARLVPCA SGLSTDVQLR AFDICNTNRA
GIGLYYKVNC CRFQRIDDDG NKLDKFFVVK RTNLEVYNKE KTYYELTKSC GVVAEHDFFT
FDIDGSRVPH IVRRNLSKYT MLDLCYALRH FDRNDCSILC EILCEYADCK ESYFSKKDWY
DFVENPDIIN IYKKLGPIFN RALLNTVIFA DTLVEVGLVG VLTLDNQDLY GQWYDFGDFI
QTAPGFGVAV ADSYYSYMMP MLTMCHVLDC ELFVNDSYRQ FDLVQYDFTD YKLELFNKYF
KYWGMKYHPN TVDCDNDRCI IHCANFNILF SMVLPNTCFG PLVRQIFVDG VPFVVSIGYH
YKELGVVMNL DVDTHRYRLS LKDLLLYAAD PAMHVASASA LLDLRTCCFS VAAITSGIKF
QTVKPGNFNQ DFYEFVKSKG LFKEGSTVDL KHFFFTQDGN AAITDYNYYK YNLPTMVDIK
QLLFVLEVVY KYFEIYDGGC IPASQVIVNN YDKSAGYPFN KFGKARLYYE ALSFEEQNEI
YAYTKRNVLP TLTQMNLKYA ISAKNRARTV AGVSILSTMT GRMFHQKCLK SIAATRGVPV
VIGTTKFYGG WDDMLRHLIK DVDNPVLMGW DYPKCDRAMP NILRIVSSLV LARKHEFCCS
HGDRFYRLAN ECAQVLSEIV MCGGCYYVKP GGTSSGDATT AFANSVFNIC QAVTANVCSL
MACNGHKIED LSIRNLQKRL YSNVYRTDYV DYTFVNEYYE FLCKHFSMMI LSDDGVVCYN
SDYASKGYIA NISVFQQVLY YQNNVFMSES KCWVENDITN GPHEFCSQHT MLVKIDGDYV
YLPYPDPSRI LGAGCFVDDL LKTDSVLLIE RFVSLAIDAY PLVHHENEEY QKVFRVYLEY
IKKLYNDLGT QILDSYSVIL STCDGLKFTE ESFYKNMYLK SAVMQSVGAC VVCSSQTSLR
CGSCIRKPLL CCKCCYDHVM ATNHKYVLSV SPYVCNAPNC DVSDVTKLYL GGMSYYCENH
KPHYSFKLVM NGMVFGLYKQ SCTGSPYIDD FNKIASCKWT EVDDYVLANE CIERLKLFAA
ETQKATEEAF KQSYASATIQ EIVSDREVIL CWETGKVKPP LNKNYVFTGY HFTSTGKTVL
GEYVFDKSEL TNGVYYRATT TYKLSIGDVF VLTSHSVASL SAPTLVPQEN YASIRFSSVY
SVPLVFQNNV ANYQHIGMKR YCTVQGPPGT GKSHLAIGLA VYYYTARVVY TAASHAAVDA
LCEKAYKFLN INDCTRIIPA KVRVDCYDKF KINDTTCKYV FTTINALPEL VTDIVVVDEV
SMLTNYELSV INARIKAKHY VYIGDPAQLP APRVLLSKGS LEPRHFNSIT KIMCCLGPDI
FLGNCYRCPK EIVETVSALV YDNKLKAKND NSSLCFKVYF KGQTTHESSS AVNIQQIYLI
SKFLKANPVW NSAVFISPYN SQNYVAKRVL GVQTQTVDSA QGSEYDYVIY SQTAETAHSV
NVNRFNVAIT RAKKGIFCVM SNMQLFESLN FITLPLDKIQ NQTLPRLHCT TNLFKDCSKS
CLGYHPAHAP SFLAVDDKYK VNENLAVNLN ICEPVLTYSR LISLMGFKLD LTLDGYSKLF
ITKDEAIKRV RGWVGFDVEG AHATRENIGT NFPLQIGFST GVDFVVEATG LFAERDCYTF
KKTVAKAPPG EKFKHLIPLM SKGQKWDIVR IRIVQMLSDY LLDLSDSVVF ITWSASFELT
CLRYFAKLGR ELNCNVCSNR ATCYNSRTGY YGCWRHSYTC DYVYNPLIVD IQQWGYTGSL
TSNHDIICNV HKGAHVASAD AIMTRCLAIY DCFCKSVNWN LEYPIISNEV SINTSCRLLQ
RVMLKAAMLC NRYNLCYDIG NPKGLACVKD YEFKFYDAFP VAKSVKQLFY VYDVHKDNFK
DGLCMFWNCN VDKYPSNSIV CRFDTRVLNK LNLPGCNGGS LYVNKHAFHT NPFTRTVFEN
LKPMPFFYYS DTPCVYVDGL ESKQVDYVPL RSATCITRCN LGGAVCSKHA EEYCNYLESY
NIVTTAGFTF WVYKNFDFYN LWNTFTTLQS LENVIYNLVN VGHYDGRTGE LPCAIMNDKV
VVKINNVDTV IFKNNTSFPT NIAVELFTKR SIRHHPELKI LRNLNIDICW KHVLWDYVKD
SLFCSSTYGV CKYTDLKFIE NLNILFDGRD TGALEAFRKA RNGVFISTEK LSRLSMIKGP
QRADLNGVIV DKVGELKVEF WFAMRKDGDD VIFSRTDSLC SSHYWSPQGN LGGNCAGNVI
GNDALTRFTI FTQSRVLSSF EPRSDLERDF IDMDDNLFIA KYGLEDYAFD HIVYGSFNHK
VIGGLHLLIG LFRRKKKSNL LIQEFLQYDS SIHSYFITDQ ECGSSKSVCT VIDLLLDDFV
SIVKSLNLSC VSKVVNINVD FKDFQFMLWC NDNKIMTFYP KMQATNDWKP GYSMPVLYKY
LNVPLERVSL WNYGKPINLP TGCMMNVAKY TQLCQYLNTT TLAVPVNMRV LHLGAGSDKE
VAPGSAVLRQ WLPSGSILVD NDLNPFVSDS LVTYFGDCMT LPFDCHWDLI ISDMYDPLTK
NIGDYNVSKD GFFTYICHLI RDKLSLGGSV AIKITEFSWN ADLYKLMSCF AFWTVFCTNV
NASSSEGFLI GINYLGKSSF EIDGNVMHAN YLFWRNSTTW NGGAYSLFDM TKFSLKLAGT
AVVNLRPDQL NDLVYSLIER GKLLVRDTRK EIFVGDSLVN TC
