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   27-MAR-2024, entry version 119.
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   Human coronavirus HKU1 (isolate N1) (HCoV-HKU1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus; Human coronavirus HKU1.
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 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;
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: [RNA-directed RNA polymerase nsp12]:
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       Multi-pass membrane protein. Host cytoplasm
CC       {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: [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.
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 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.
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=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   IntAct; P0C6X2; 1.
DR   DNASU; 3200429; -.
DR   GeneID; 3200429; -.
DR   KEGG; vg:3200429; -.
DR   SABIO-RK; P0C6X2; -.
DR   Proteomes; UP000008170; Segment.
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: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; 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; 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; 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; IPR044371; Macro_X_NSP3-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; 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; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 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; 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; 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; 1.
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.
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..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 nsp3"
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 nsp5"
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="Viral protein genome-linked nsp9"
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 nsp12"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_5000093343"
FT   CHAIN           5386..5988
FT                   /note="Helicase nsp13"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_5000093344"
FT   CHAIN           5989..6509
FT                   /note="Guanine-N7 methyltransferase nsp14"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_5000093345"
FT   CHAIN           6510..6883
FT                   /note="Uridylate-specific endoribonuclease nsp15"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_5000093346"
FT   CHAIN           6884..7182
FT                   /note="2'-O-methyltransferase nsp16"
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          2323..2384
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2471..2838
FT                   /note="CoV Nsp3 Y"
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          4719..4817
FT                   /note="Nsp12 Interface"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
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..5498
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          2471..2561
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2475..2488
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2521..2531
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2562..2838
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2562..2654
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2655..2737
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2738..2838
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2844..3223
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3651..3863
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   REGION          4820..5034
FT                   /note="RdRp Fingers N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5035..5073
FT                   /note="RdRp Palm N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5074..5132
FT                   /note="RdRp Fingers C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5133..5268
FT                   /note="RdRp Palm C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5269..5385
FT                   /note="RdRp Thumb"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
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        1323
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        1928
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                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         370
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         389
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1835
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1837
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1869
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1871
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2475
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2480
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2485
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2488
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2521
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2524
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2528
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2531
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4439
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4449
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4666
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT   BINDING         4675
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT   BINDING         4748
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4754
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4759
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4763
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4940
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5095
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5098
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5099
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5401
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5418
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5424
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5457
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5460
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
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="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6216
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
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="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6455
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6469
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
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"
FT   DISULFID        2339..2363
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2354..2360
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
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
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