ID   R1AB_CVM2               Reviewed;        7124 AA.
AC   P0C6X8; Q9PYA2; Q9PYA3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
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 nsp3;
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 nsp5;
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=Viral protein genome-linked nsp9;
DE     AltName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE     AltName: Full=RNA-capping enzyme subunit 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 nsp12;
DE              Short=Pol;
DE              Short=RdRp;
DE              EC=2.7.7.48;
DE              EC=2.7.7.50;
DE     AltName: Full=nsp12;
DE     AltName: Full=p100;
DE   Contains:
DE     RecName: Full=Helicase nsp13;
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 nsp14;
DE              Short=ExoN;
DE              EC=2.1.1.56;
DE              EC=3.1.13.-;
DE     AltName: Full=nsp14;
DE   Contains:
DE     RecName: Full=Uridylate-specific endoribonuclease nsp15;
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 nsp16;
DE              EC=2.1.1.57;
DE     AltName: Full=nsp16;
GN   Name=rep; ORFNames=1a-1b;
OS   Murine coronavirus (strain 2) (MHV-2) (Murine hepatitis virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus; Murine coronavirus.
OX   NCBI_TaxID=76344;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Das Sarma J., Hingley S.T., Lai M.M.C., Weiss S.R., Lavi E.;
RT   "Pathogenesis and sequence analysis of mouse hepatitis virus type 2: an
RT   experimental model system of acute meningitis and hepatitis in mice.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8291254; DOI=10.1006/viro.1994.1088;
RA   Bonilla P.J., Gorbalenya A.E., Weiss S.R.;
RT   "Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: heterogeneity
RT   among MHV strains.";
RL   Virology 198:736-740(1994).
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 nsp3]: 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 nsp5]: Cleaves the C-terminus of
CC       replicase polyprotein at 11 sites. Recognizes substrates containing the
CC       core 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: [Viral protein genome-linked nsp9]: Forms a primer, NSP9-pU,
CC       which is utilized by the polymerase for the initiation of RNA chains.
CC       Interacts with ribosome signal recognition particle RNA (SRP). Together
CC       with NSP8, suppress protein integration into the cell membrane, thereby
CC       disrupting host immune defenses. {ECO:0000250|UniProtKB:P0DTD1}.
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 nsp12]: RNA-directed RNA
CC       polymerase that catalyzes the transcription of viral genomic and
CC       subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both
CC       the minus and positive strands of genomic RNA. The kinase-like NiRAN
CC       domain of NSP12 attaches one or more nucleotides to the amino terminus
CC       of NSP9, forming a covalent RNA-protein intermediate that serves as
CC       transcription/replication primer. Subgenomic RNAs (sgRNAs) are formed
CC       by discontinuous transcription: The polymerase has the ability to pause
CC       at transcription-regulating sequences (TRS) and jump to the leader TRS,
CC       resulting in a major deletion. This creates a series of subgenomic RNAs
CC       that are replicated, transcribed and translated. In addition, Nsp12 is
CC       a subunit of the viral RNA capping enzyme that catalyzes the RNA
CC       guanylyltransferase reaction for genomic and sub-genomic RNAs.
CC       Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core
CC       cap structure GpppA-RNA. {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- FUNCTION: [Helicase nsp13]: Multi-functional protein with a zinc-
CC       binding domain in N-terminus displaying RNA and DNA duplex-unwinding
CC       activities with 5' to 3' polarity. Activity of helicase is dependent on
CC       magnesium. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Guanine-N7 methyltransferase nsp14]: Plays a role in viral
CC       RNA synthesis through two distinct activities. The N7-guanine
CC       methyltransferase activity plays a role in the formation of the cap
CC       structure GpppA-RNA. The proofreading exoribonuclease reduces the
CC       sensitivity of the virus to RNA mutagens during replication. This
CC       activity acts on both ssRNA and dsRNA in a 3'-5' direction.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Uridylate-specific endoribonuclease nsp15]: Plays a role in
CC       viral transcription/replication and prevents the simultaneous
CC       activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR
CC       (By 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 nsp16]: Methyltransferase that
CC       mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of
CC       viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of
CC       nsp16. Therefore plays an essential role in viral mRNAs cap methylation
CC       which is essential to evade immune system.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY: [Helicase nsp13]:
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 nsp13]:
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 nsp3]:
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 nsp16]:
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 nsp15]:
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   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]:
CC       Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC         end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC         Evidence={ECO:0000250|UniProtKB:P0DTD1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC         Evidence={ECO:0000250|UniProtKB:P0DTD1};
CC   -!- CATALYTIC ACTIVITY: [Guanine-N7 methyltransferase nsp14]:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC         S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC         COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC         ChEBI:CHEBI:167617; EC=2.1.1.56;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67009;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC   -!- COFACTOR: [Uridylate-specific endoribonuclease nsp15]:
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   -!- COFACTOR: [Non-structural protein 10]:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0DTD1};
CC   -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [Non-structural protein 4]: Interacts with papain-like
CC       protease nsp3 and non-structural protein 6.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [3C-like proteinase nsp5]: Monomer. Homodimer. Only the
CC       homodimer shows catalytic activity. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [Non-structural protein 7]: Interacts with nsp8 and nsp12 to
CC       form the replication-transcription complex (RTC): nsp12, nsp7, two
CC       subunits of nsp8, and up to two subunits of nsp13.
CC       {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- SUBUNIT: [Non-structural protein 8]: Interacts with nsp7, nsp13 and
CC       nsp12 to form the replication-transcription complex (RTC): nsp12, nsp7,
CC       two subunits of nsp8, and up to two subunits of nsp13.
CC       {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- SUBUNIT: [Viral protein genome-linked nsp9]: Interacts with nsp12.
CC       {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- SUBUNIT: [Non-structural protein 10]: Interacts with proofreading
CC       exoribonuclease nsp14 and 2'-O-methyltransferase nsp16; these
CC       interactions enhance nsp14 and nsp16 enzymatic activities.
CC       {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase nsp12]: Interacts with nsp7 and
CC       nsp8 to form the replication-transcription complex (RTC): nsp12, nsp7,
CC       two subunits of nsp8, and up to two subunits of nsp13. Interacts with
CC       nsp9. {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- SUBUNIT: [Helicase nsp13]: Interacts with nsp8 to form the replication-
CC       transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC       to two subunits of nsp13. {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- SUBCELLULAR LOCATION: [Papain-like proteinase nsp3]: 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: [Viral protein genome-linked nsp9]: Host
CC       cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9
CC       and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
CC       in infection, they merge into confluent complexes (By similarity).
CC       {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 nsp13]: Host endoplasmic reticulum-
CC       Golgi intermediate compartment {ECO:0000305}. Note=The helicase
CC       interacts with the N protein in membranous complexes and colocalizes
CC       with sites of synthesis of new viral RNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease nsp15]: 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=P0C6X8-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6U9-1; 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=AAF19383.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF19384.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF201929; AAF19383.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; AF201929; AAF19384.1; ALT_SEQ; Genomic_RNA.
DR   SMR; P0C6X8; -.
DR   Proteomes; UP000139707; 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:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
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-dependent 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:0006351; P:DNA-templated transcription; 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:0039648; P:modulation by symbiont 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:0019082; P:viral protein processing; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR   CDD; cd21901; alpha_betaCoV_Nsp10; 1.
DR   CDD; cd21560; betaCoV-Nsp6; 1.
DR   CDD; cd21722; betaCoV_Nsp13-helicase; 1.
DR   CDD; cd21659; betaCoV_Nsp14; 1.
DR   CDD; cd21519; betaCoV_Nsp2_MHV-like; 1.
DR   CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR   CDD; cd21827; betaCoV_Nsp7; 1.
DR   CDD; cd21831; betaCoV_Nsp8; 1.
DR   CDD; cd21898; betaCoV_Nsp9; 1.
DR   CDD; cd21732; betaCoV_PLPro; 1.
DR   CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21524; DPUP_MHV_Nsp3; 1.
DR   CDD; cd21593; HCoV_HKU1-like_RdRp; 1.
DR   CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR   CDD; cd21879; MHV-like_Nsp1; 1.
DR   CDD; cd21812; MHV-like_Nsp3_betaSM; 1.
DR   CDD; cd21824; MHV-like_Nsp3_NAB; 1.
DR   CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR   CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1.
DR   CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR   CDD; cd21714; TM_Y_MHV-like_Nsp3_C; 1.
DR   CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR   CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR   Gene3D; 1.10.8.1190; -; 2.
DR   Gene3D; 2.60.120.1680; -; 1.
DR   Gene3D; 3.10.20.350; -; 1.
DR   Gene3D; 3.10.20.540; -; 1.
DR   Gene3D; 3.40.50.11580; -; 1.
DR   Gene3D; 6.10.140.2090; -; 1.
DR   Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR   Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR   Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR   Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR   Gene3D; 3.40.50.11020; Replicase polyprotein, nucleic acid-binding domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR046443; a/bCoV_NSP1_glob.
DR   InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR   InterPro; IPR022570; B-CoV_A_NSP1.
DR   InterPro; IPR046442; bCoV_NSP1_C.
DR   InterPro; IPR043608; CoV_NSP15_M.
DR   InterPro; IPR043606; CoV_NSP15_N.
DR   InterPro; IPR043613; CoV_NSP2_C.
DR   InterPro; IPR047573; CoV_NSP2_M.
DR   InterPro; IPR043611; CoV_NSP3_C.
DR   InterPro; IPR047566; CoV_NSP3_Y3.
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; IPR022733; DPUP_SUD_C_bCoV.
DR   InterPro; IPR037227; EndoU-like.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR046435; N7_MTase_CoV.
DR   InterPro; IPR043609; NendoU_nidovirus.
DR   InterPro; IPR044863; NIRAN.
DR   InterPro; IPR046438; NIV_2_O_MTASE.
DR   InterPro; IPR046436; NIV_EXON.
DR   InterPro; IPR036333; NSP10_sf_CoV.
DR   InterPro; IPR047570; NSP12_IF_CoV.
DR   InterPro; IPR044343; NSP13_1B_dom_CoV.
DR   InterPro; IPR048673; NSP13_stalk_CoV.
DR   InterPro; IPR048672; NSP13_ZBD_CoV.
DR   InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR   InterPro; IPR044315; NSP14_betaCoV.
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; IPR044384; NSP2_MHV-like.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR044381; NSP3_DPUP_MHV.
DR   InterPro; IPR047567; NSP3_G2M_bCoV.
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; IPR046441; RdRp_CoV.
DR   InterPro; IPR044347; RdRp_HCoV_HKU1-like.
DR   InterPro; IPR009469; RdRp_N_CoV.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF530; HELICASE MAGATAMA 3-RELATED; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF13604; AAA_30; 1.
DR   Pfam; PF11963; B-CoV_A_NSP1; 1.
DR   Pfam; PF16251; bCoV_NAB; 1.
DR   Pfam; PF06471; CoV_ExoN; 1.
DR   Pfam; PF06460; CoV_Methyltr_2; 1.
DR   Pfam; PF09401; CoV_NSP10; 1.
DR   Pfam; PF20631; CoV_NSP13_1B; 1.
DR   Pfam; PF20633; CoV_NSP13_stalk; 1.
DR   Pfam; PF20632; CoV_NSP13_ZBD; 1.
DR   Pfam; PF19215; CoV_NSP15_C; 1.
DR   Pfam; PF19216; CoV_NSP15_M; 1.
DR   Pfam; PF19219; CoV_NSP15_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; 1.
DR   Pfam; PF06478; CoV_RPol_N; 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; SSF144246; Coronavirus NSP10-like; 1.
DR   SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR   SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF142877; EndoU-like; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF159936; NSP3A-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF101816; Replicase NSP9; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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; PS51993; COV_3ECTO; 1.
DR   PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR   PROSITE; PS51954; COV_N7_MTASE; 1.
DR   PROSITE; PS51962; COV_NSP1; 1.
DR   PROSITE; PS52000; COV_NSP12_IF; 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_Y; 1.
DR   PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR   PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR   PROSITE; PS51946; COV_NSP4C; 1.
DR   PROSITE; PS51949; COV_NSP7; 1.
DR   PROSITE; PS51950; COV_NSP8; 1.
DR   PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR   PROSITE; PS51653; CV_ZBD; 1.
DR   PROSITE; PS51442; M_PRO; 1.
DR   PROSITE; PS51154; MACRO; 1.
DR   PROSITE; PS51958; NENDOU; 1.
DR   PROSITE; PS51947; NIRAN; 1.
DR   PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR   PROSITE; PS51953; NIV_EXON; 1.
DR   PROSITE; PS51124; PEPTIDASE_C16; 2.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Activation of host autophagy by virus; ATP-binding;
KW   Decay of host mRNAs by virus; Disulfide bond; 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   Interferon antiviral system evasion; Lyase; Manganese; Membrane;
KW   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..247
FT                   /note="Host translation inhibitor nsp1"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037323"
FT   CHAIN           248..832
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037324"
FT   CHAIN           833..2783
FT                   /note="Papain-like proteinase nsp3"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037325"
FT   CHAIN           2784..3279
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037326"
FT   CHAIN           3280..3582
FT                   /note="3C-like proteinase nsp5"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037327"
FT   CHAIN           3583..3869
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037328"
FT   CHAIN           3870..3961
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037329"
FT   CHAIN           3962..4155
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037330"
FT   CHAIN           4156..4265
FT                   /note="Viral protein genome-linked nsp9"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037331"
FT   CHAIN           4266..4402
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037332"
FT   CHAIN           4403..5330
FT                   /note="RNA-directed RNA polymerase nsp12"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037333"
FT   CHAIN           5331..5930
FT                   /note="Helicase nsp13"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037334"
FT   CHAIN           5931..6451
FT                   /note="Guanine-N7 methyltransferase nsp14"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037335"
FT   CHAIN           6452..6825
FT                   /note="Uridylate-specific endoribonuclease nsp15"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037336"
FT   CHAIN           6826..7124
FT                   /note="2'-O-methyltransferase nsp16"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000037337"
FT   TRANSMEM        2232..2252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2260..2280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2346..2366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2388..2408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2789..2809
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2869..2889
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3042..3062
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3064..3084
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3096..3116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3123..3143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3148..3168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3591..3611
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3621..3641
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3647..3667
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3690..3710
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3717..3737
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3744..3764
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3788..3808
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          54..196
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          217..247
FT                   /note="BetaCoV Nsp1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT   DOMAIN          251..511
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          518..706
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          726..832
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          834..946
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1031..1268
FT                   /note="Peptidase C16 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1269..1429
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1484..1556
FT                   /note="DPUP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT   DOMAIN          1555..1610
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1625..1884
FT                   /note="Peptidase C16 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1898..1999
FT                   /note="Nucleic acid-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT   DOMAIN          2053..2202
FT                   /note="G2M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT   DOMAIN          2268..2329
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2416..2783
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          3182..3279
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          3280..3582
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3870..3958
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3959..4155
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          4156..4265
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          4266..4403
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   DOMAIN          4408..4663
FT                   /note="NiRAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT   DOMAIN          4664..4762
FT                   /note="Nsp12 Interface"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   DOMAIN          4763..5330
FT                   /note="Nsp12 RNA-dependent RNA polymerase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   DOMAIN          5010..5172
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          5331..5443
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   DOMAIN          5586..5767
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          5768..5937
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          6001..6216
FT                   /note="ExoN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   DOMAIN          6225..6451
FT                   /note="N7-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   DOMAIN          6452..6512
FT                   /note="Nsp15 N-terminal oligomerization"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT   DOMAIN          6513..6633
FT                   /note="AV-Nsp11N/CoV-Nsp15M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT   DOMAIN          6683..6822
FT                   /note="NendoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   DOMAIN          6827..7121
FT                   /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ZN_FING         1145..1173
FT                   /note="C4-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         1741..1777
FT                   /note="C4-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4339..4355
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4381..4394
FT                   /evidence="ECO:0000250"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..414
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          2232..2408
FT                   /note="HD1"
FT   REGION          2416..2506
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2420..2433
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2466..2476
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2507..2783
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2507..2599
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2600..2682
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2683..2783
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2789..3168
FT                   /note="HD2"
FT   REGION          3525..3808
FT                   /note="HD3"
FT   REGION          4765..4979
FT                   /note="RdRp Fingers N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4980..5018
FT                   /note="RdRp Palm N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5019..5077
FT                   /note="RdRp Fingers C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5078..5213
FT                   /note="RdRp Palm C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5214..5330
FT                   /note="RdRp Thumb"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          6338..6352
FT                   /note="GpppA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   ACT_SITE        1068
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1219
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1230
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1663
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1820
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1834
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3320
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3424
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        5157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        6019
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6021
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6713
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6728
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6768
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6871
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6955
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6995
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        7028
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1741
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1743
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1775
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1777
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2469
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2473
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4611
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT   BINDING         4620
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT   BINDING         4693
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4699
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4704
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4708
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4885
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5040
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5043
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5044
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5346
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5363
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5380
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5385
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5405
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5611..5618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         6136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6260..6266
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   SITE            247..248
FT                   /note="Cleavage; by PL1-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            832..833
FT                   /note="Cleavage; by PL1-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            2783..2784
FT                   /note="Cleavage; by PL2-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3279..3280
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3582..3583
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3869..3870
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3961..3962
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4155..4156
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4265..4266
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4402..4403
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            5330..5331
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            5930..5931
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6451..6452
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6825..6826
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   DISULFID        2284..2308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2299..2305
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
SQ   SEQUENCE   7124 AA;  797625 MW;  C120EF6972F622AF CRC64;
     MAKMGKYGLG FKWAPEFPWM LPNASEKLGS PERSEEDGFC PSAAQEPKTK GKTLINHVRV
     DCSRLPALEC CVQSAIIRDI FVDEDPLNVE ASTMMALQFG SAVLVKPSKR LSIQAWAKLG
     VLPKTPAMGL FKRFCLCNTR ECVCDAHVAF QLFTVQPDGV CLGNGRFIGW FVPVTAIPAY
     AKQWLQPWSI LLRKGGNKGS VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSRKAYA
     LLKGYRGVKS ILFLDQYGCD YTGRLAKGLE DYGDCTLEEM KELFPVWCDS LDNEVVVAWH
     VDRDPRAVMR LQTLATIRSI GYVGQPTEDL VDGDVVVREP AHLLAANAIV KRLPRLVETM
     LYTDSSVTEF CYKTKLCDCG FITQFGYVDC CGDACDFRGW VPGNMMDGFL CPGCSKSYMP
     WELEAQSSGV IPKGGVLFTQ STDTVNRESF KLYGHAVVPF GSAVYWSPYP GMWLPVIWSS
     VKSYADLTYT GVVGCKAIVQ ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN
     RGDYSLLLEN VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN
     FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT EWFDLAVDTA
     ASAAGWLCYQ LVNGLFAVAN GGITFLSDVP ELVKNFVDKF KVFFKVLIDS MSVSVLSGLT
     VVKTASNRVC LAGCKVYEVV QKRLSAYVMP VGCNEATCLV GEIEPAVVED DVVDVVKAPL
     TYQGCCKPPT SFEKICVVDK LYMAKCGDQF YPVVVDNDTI GVLDQCWRFP CAGKKVEFND
     KPKVKEIPST RKIKINFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
     KEHDVIGTKV CALLNRLAED YVYLFDEGGE EVIAPKMYCS FSAPDDEDCV AADVVDADEN
     QGDDADDSAA LVTDTQEEDG VAKGQVGVAE SDARLDQVEA FDIEKVEDPI LNELSAELNA
     PADKTYEDVL AFDAIYSEAL SAFYAVPGDE THFKVCGFYS PAIERTNCWL RSTLIVMQSL
     PLEFKDLEMQ KLWLSYKSSY NKEFVDKLVK SVPKSIILPQ GGYVADFAYF FLSQCSFKAY
     ANWRCLKCDM DLKLQGLDAM FFYGDVVSHV CKCGTGMTLL SADIPYTLHF GLRDDKFCAF
     YTPRKVFRAA CVVDVNDCHS MAVVDGKQID GKVVTKFNGD KYDFMVGHGM AFSMSAFEIA
     QLYGSCITPN VCFVKGDVIK VLRRVGAEVI VNPANGRMAH GAGVAGAIAK AAGKSFIKET
     ADMVKNQGVC QVGECYESTG GNLCKTVLNI VGPDARGHGK QCYSFLERAY QHINKCDDVV
     TTLISAGIFS VPTDVSLTYL IGVVTKNVIL VSNNKDDFDV IEKCQVTSIA GTKALSLQLA
     KNLCRDVKFE TNACDSLFSD SCFVSSYDVL QEVELLRHDI QLDDDARVFV QAHMDNLPAD
     WRLVNKFDSV DGVRTVKYFE CPGEIFVSSQ GKKFGYVQNG SFKVASVSQI RALLANKVDV
     LCTVDGVNFR SCCVAEGEVF GKTLGSVFCD GINVTKVRCS AIHKGKVFFQ YSGLSAADLV
     AVTDAFGFDE PQLLKYYNML GMCKWPVVVC GNYFAFKQSN NNCYINVACL MLQHLSLKFH
     KWQWQEAWNE FRSGKPLRFV SLVLAKGSFK FNEPSDSTDF MRVVLREADL SGATCDFEFV
     CKCGVKQEQR KGVDAVMHFG TLDKGDLAKG YTIACTCGNK LVHCTQLNVP FLICSNKPEG
     KKLPDDVVAA NIFTGGSLGH YTHVKCKPKY QLYDACNVSK VSEAKGNFTD CLYLKNLKQT
     FSSKLTTFYL DDVKCVEYNP DLSQYYCESG KYYTKPIIKA QFRTFEKVEG VYTNFKLVGH
     SIAEKFNAKL GFDCNSPFTE YKITEWPTAT GDVVLASDDL YVSRYSGGCV TFGKPVIWLG
     HEEASLKSLT YFNRPSVVCE NKFNVLPVDV SEPTDKGPVP AAVLVTGALS GAATAPGTAK
     EQKVCASDSV VDQVVSGFLS DLSGATVDVK EVKLNGVKKP IKVEDSVVVN DPTSETKVVK
     SLSIVDVYDM FLTGCRYVVW MANELSRLVN SPTVREYVKW GMTKIVIPAK LVLLRDEKQE
     FVAPKVVKAK VIACYSAVKW FFLYCFSWIK FNTDNKVIYT TEVASKLTFN LCCLAFKNAL
     QTFNWNVVSR GFFLVATVFL LWFNFLYANV ILSDFYLPNI GFFPTFVGQI VAWVKTTFGI
     FTLCDLYQVS DVGYRSSFCN GSMVCELCFS GFDMLDNYDA INVVQHVVDR RVSFDYISLF
     KLVVELVIGY SLYTVCFYPL FGLIGMQLLT TWLPEFFMLE TMHWSARFFV FVANMLPAFT
     LLRFYIVVTA MYKIFCLCRH VMYGCSRPGC LFCYKRNRSV RVKCSTVVGG TLRYYDVMAN
     GGTGFCAKHQ WNCLNCSAFG PGNTFITHEA AADLSKELKR PVNPTDSAYY LVTEVKQVGC
     SMRLFYERDG QRVYDDVSAS LFVDMNGLLH SKVKGVPETH VVVVENEADK AGFLNAAVFY
     AQSLYRPMLL VEKKLITTAN TGLSVSQTMF DLYVDSLLGV LDVDRKSLTS FVNAAHNSLK
     EGVQLEQVMD TFIGCARRKC AIDSDVETKS ITKSIMSAVN AGVDFTDESC NNLVPTYVKS
     DTIVAADLGV LIQNNAKHVQ ANVAKAANVA CIWSVDAFNQ LSADLQHRLR KACSKTGLKI
     KLTYNKQEAN VPILTTPFSL KGGAVFSKVL QWLFVVNLIC FIVLWALMPT YAVHKSDMQL
     PLYASFKVID NGVLRDVTVT DACFANKFIQ FDQWYESTFG LVYYRNSRAC PVVVAVIDQD
     IGYTLFNVPT KVLRYGFHVL HFITHAFATD SVQCYTPHMQ IPYDNFYASG CVLSSLCTML
     AHADGTPHPY CYTEGIMHNA SLYDSLAPHV RYNLANSNGY IRFPEVVSEG IVRIVRTRSM
     TYCRVGLCED AEEGVCFNFN SSWVLNNPYY RAMPGTFCGR NAFDLIHQVL GGLVRPIDFF
     ALTASSVAGA ILAIIVVLAF YYLIKLKRAF GDYTSVVVIN VIVWCINFLM LFVFQVYPTL
     SCLYACFYFY TTLYFPSEIS VVMHLQWLVM YGAIMPLWFC IIYVAVVVSN HALWLFSYCR
     KLGTEVRSDG TFEEMSLTTF MITKESYCKL KNSVSDVAFN RYLSLYNKYR YFSGKMDTAA
     YREAACSQLA KAMETFNHNN GNDVLYQPPT ASVTTSFLQS GIVKMVFPTS KVEPCVVSVT
     YGNMTLNGLW LDDKVYCPRH VICSSADMTD PDYSNLLCRV ISSDFCVMSG RMSLTVMSYQ
     MQGSLLVLTV TLQNPNTPKY SFGVVKPGET FTVLAAYNGK SQGAFHVTMR SSYTIKGSFL
     CGSCGSVGYV LTGDSVRFVY MHQLELSTGC HTGTDFSGNF YGPYRDAQVV QLPVQDYTQT
     VNVVAWLYAA ILNRCNWFVQ SDSCSLEEFN VWAMTNGFSS IKADLVLDAL ASMTGVTVEQ
     ILAAIKRLYS GFQGKQILGS CVLEDELTPS DVYQQLAGVK LQSKRTRVVK GTCCWILAST
     LLFCSIISAF VKWTMFMYVT THMLGVTLCA LCFVSFAMLL VKHKHLYLTM FIMPVLCTLF
     YTNYLVVYKQ SFRGLAYAWL SHFVPAVDYT YMDEVLYGVV LLVAMVFVTM RSINHDVFSV
     MFLVGRLVSL VSMWYFGANL EEEVLLFLTS LFGTYTWTTM LSLATAKVIA KWLAVNVLYF
     TDVPQVKLVL LSYLCIGYVC CCYWGVLSLL NSIFRMPLGV YNYKISVQEL RYMNANGLRP
     PRNSFEALVL NFKLLGIGGV PVIEVSQIQS RLTDVKCVNV VLLNCLQHLH IASSSKLWQY
     CSTLHNEILA TSDLSVAFDK LAQLLVVLFA NPAAVDSKCL ASIEEVSDDY VRDSTVLQAL
     QSEFVNMASF VEYELAKKNL DEAKASGSAN QQQIKQLEKA CNIAKSAYER DRAVARKLER
     MADLALTNMY KEARINDKKS KVVSALQTML FSMIRKLDNQ ALNSILDNAV KGCVPLNAIP
     SLTSNTLTII VPDKQVFDQV VDNVYVTYAG NVWHIQSIQD ADGAVKQLNE IDVNITWPLV
     IAANRHNEVS SVVLQNNELM PQKLRTQVVN SGSDMNCNTP TQCYYNTTGM GKIVYAILSD
     CDGLKYTKIV KEDGNCVVLE LDPPCKFSVQ DVKGLKIKYL YFVKGCNTLA RGWVVGTLSS
     TVRLQAGTAT EYASNSAIRS LCAFSVDPKK TYLDYIQQGG APVTNCVKML CDHAGTGMAI
     TIKPEATTNQ DSYGGASVCI YCRSRVEHPD VDGLCKLRGK FVQVPLGIKD PVSYVLTHDV
     CQVCGFWRDG SCSCVGTGSQ FQSKDTNFLN RVRGTSVNAR LVPCASGLDT DVQLRAFDIC
     NANRAGIGLY YKVNCCRFQR ADEDGNTLDK FFVIKRTNLE VYNKEKECYE LTKECGVVAE
     HEFFTFDVEG SRVPHIVRKD LSKYTMLDLC YALRHFDRND CSTLKEILLT YAECDESYFQ
     KKDWYDFVEN SDIINVYKKL GPIFNRALLN TAKFADTLVE AGLVGVLTLD NQDLYGQWYD
     FGDFVKTVPG CGVAVADSYY SYMMPMLTMC HALDSELFIN GTYREFDLVQ YDFTDFKLEL
     FNKYFKYWSM TYHPNTCECE DDRCIIHCAN FNILFSMVLP KTCFGPLVRQ IFVDGVPFVV
     SIGYHYKELG VVMNMDVDTH RYRLSLKDLL LYAADPALHV ASASALLDLR TCCFSVAAIT
     SGVKFQTVKP GNFNQDFYEF ILSKGLLKEG SSVDLKHFFF TQDGNAAITD YNYYKYNLPT
     MVDIKQLLFV LEVVNKYFEI YDGGCIPATQ VIVNNYDKSA GYPFNKFGKA RLYYEALSFE
     EQDEVYAYTK RNVLPTLTQM NLKYAISAKN RARTVAGVSI LSTMTGRMFH QKCLKSIAAT
     RGVPVVIGTT KFYGGWDDML RRLIKDVDSP VLMGWDYPKC DRAMPNILRI ISSLVLARKH
     DSCCSHTDRF YRLANECAQV LSEIVMCGGC YYVKPGGTSS GDATTAFANS VFNICQAVSA
     NVCSLMACNG HKIEDLSIRE LQKRLYSNVY RADHVDPAFV NEYYEFLNKH FSMMILSDDG
     VVCYNSEFAS KGYIANISAF QQVLYYQNNV FMSEAKCWVE TDIEKGPHEF CSQHTMLVKM
     DGDEVYLPYP DPSRILGAGC FVDDLLKTDS VLLIERFVSL AIDAYPLVYH ENPEYQNVFR
     VYLEYIKKLY NDLGNQILDS YSVILSTCDG QKFTDETFYK NMYLRSAVMQ SVGACVVCSS
     QTSLRCGSCI RKPLLCCKCA YDHVMSTDHK YVLSVSPYVC NSPGCDVNDV TKLYLGGMSY
     YCEDHKPQYS FKLVMNGMVF GLYKQSCTGS PYIEDFNKIA SCKWTEVDDY VLANECTERL
     KLFAAETQKA TEESFKQCYA SATIREIVSD RELILSWEIG KVRPPLNKNY VFTGYHFTSN
     GKTVLGEYVF DKSELTNGVY YRATTTYKLS VGDVFILTSH AVSSLSAPTL VPQENYTSIR
     FASVYSVPET FQNNVPNYQH IGMKRYCTVQ GPPGTGKSHL AIGLAVYYCT ARVVYTAASH
     AAVDALCEKA YKFLNINDCT RIVPAKVRVD CYDKFKVNDT TRKYVFTTIN ALPELVTDII
     VVDEVSMLTN YELSVINSRV RAKHYVYIGD PAQLPAPRVL LNKGTLEPRY FNSVTKLMCC
     LGPDIFLGTC YRCPKEIVDT VSALVYHNKL KAKNDNSSMC FKVYYKGQTT HESSSAVNMQ
     QIYLISKFLK ANPSWSNAVF ISPYNSQNYV AKRVLGLQTQ TVDSAQGSEY DFVIYSQTAE
     TAHSVNVNRF NVAITRAKKG ILCVMSSMQL FESLNFSTLT LDKINNPRLQ CTTNLFKDCS
     RSYAGYHPAH APSFLAVDDK YKVGGDLAVC LNVADSAVTY SRLISLMGFK LDLTLDGYCK
     LFITRDEAIR RVRAWVGFDA EGAHATRDSI GTNFPLQLGF STGIDFVVEA TGMFAERDGY
     VFKKAVARAP PGEQFKHLVP LMSRGQKWDV VRIRIVQMLS DHLVDLADSV VLVTWAASFE
     LTCLRYFAKV GKEVVCSVCN KRATCFNSRT GYYGCWRHSY SCDYLYNPLI VDIQQWGYTG
     SLTSNHDLIC SVHKGAHVAS SDAIMTRCLA VHDCFCKSVN WSLEYPIISN EVSVNTSCRL
     LQRVMFRAAM LCNRYDVCYD IGNPKGLACV KGYDFKFYDA SPVVKSVKQF VYKYEAHKDQ
     FLDGLCMFWN CNVDKYPANA VVCRFDTRVL NKLNLPGCNG GSLYVNKHAF HTSPFTRAAF
     ENLKPMPFFY YSDTPCVYME GMESKQVDYV PLRSATCITR CNLGGAVCLK HAEDYREYLE
     SYNTATTAGF TFWVYKTFDF YNLWNTFTRL QSLENVVYNL VNAGHFDGRA GELPCAVIGE
     KVIAKIQNED VVVFKNNTPF PTNVAVELFA KRSIRPHPEL KLFRNLNIDV CWSHVLWDYA
     KDSVFCSSTY KVCKYTDLQC IESLNVLFDG RDNGALEAFK KCRDGVYINT TKIKSLSMIK
     GPQRADLNGV VVEKVGDSDV EFWFAMRRDG DDVIFSRTGS LEPSHYRSPQ GNPGGNRVGD
     LSGNEALARG TIFTQSRFLS SFAPRSEMEK DFMDLDEDVF IAKYSLQDYA FEHVVYGSFN
     QKIIGGLHLL IGLARRQQKS NLVIQEFVPY DSSIHSYFIT DENSGSSKSV CTVIDLLLDD
     FVDIVKSLNL NCVSKVVNVN VDFKDFQFML WCNEEKVMTF YPRLQAAADW KPGYVMPVLY
     KYLESPLERV NLWNYGKPIT LPTGCLMNVA KYTQLCQYLN TTTLAVPANM RVLHLGAGSD
     KDVAPGSAVL RQWLPAGSIL VDNDINPFVS DSVASYYGNC ITLPIACQWD LIISDMYDPL
     TKNIGEYNVS KDGFFTYLCH LIRDKLALGG SVAIKITEFS WNAELYSLMG KFAFWTIFCT
     NVNASSSEGF LIGINWLNRT RTEIDGKTMH ANYLFWRNST MWNGGAYSLF DMSKFPLKVA
     GTAVVSLKPD QINDLVLSLI EKGKLLVRDT RKEVFVGDSL VNVK
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