ID   R1AB_BC279              Reviewed;        7079 AA.
AC   P0C6V9; Q0Q476;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=Leader protein;
DE   Contains:
DE     RecName: Full=Non-structural protein 2;
DE              Short=nsp2;
DE     AltName: Full=p65 homolog;
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   Contains:
DE     RecName: Full=Non-structural protein 4;
DE              Short=nsp4;
DE   Contains:
DE     RecName: Full=3C-like proteinase nsp5;
DE              Short=3CL-PRO;
DE              Short=3CLp;
DE              EC=3.4.22.-;
DE     AltName: Full=nsp5;
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   Contains:
DE     RecName: Full=Non-structural protein 8;
DE              Short=nsp8;
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   Contains:
DE     RecName: Full=Non-structural protein 10;
DE              Short=nsp10;
DE     AltName: Full=Growth factor-like peptide;
DE              Short=GFL;
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   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   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   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   Bat coronavirus 279/2005 (BtCoV) (BtCoV/279/2005).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Sarbecovirus;
OC   Severe acute respiratory syndrome coronavirus.
OX   NCBI_TaxID=389167;
OH   NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16840328; DOI=10.1128/jvi.00697-06;
RA   Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
RA   Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
RA   Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
RT   "Prevalence and genetic diversity of coronaviruses in bats from China.";
RL   J. Virol. 80:7481-7490(2006).
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: [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 (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=P0C6V9-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6F5-1; 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. {ECO:0000250}.
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: Bat coronavirus 279/2005 is highly similar to SARS-CoV
CC       (SARS-like).
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=ABG47068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DQ648857; ABG47068.1; ALT_INIT; Genomic_RNA.
DR   BMRB; P0C6V9; -.
DR   SMR; P0C6V9; -.
DR   Proteomes; UP000006573; 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:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
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; cd21516; betaCoV_Nsp2_SARS-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; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR   CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR   CDD; cd21562; Macro_cv_SUD-N_Nsp3-like; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR   CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1.
DR   CDD; cd22662; SARS-CoV-like_Nsp1_C; 1.
DR   CDD; cd21796; SARS-CoV-like_Nsp1_N; 1.
DR   CDD; cd21814; SARS-CoV-like_Nsp3_betaSM; 1.
DR   CDD; cd21822; SARS-CoV-like_Nsp3_NAB; 1.
DR   CDD; cd21591; SARS-CoV-like_RdRp; 1.
DR   CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR   CDD; cd21525; SUD_C_SARS-CoV_Nsp3; 1.
DR   CDD; cd21717; TM_Y_SARS-CoV-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; -; 1.
DR   Gene3D; 2.60.120.1680; -; 1.
DR   Gene3D; 3.10.20.350; -; 1.
DR   Gene3D; 3.10.20.540; -; 1.
DR   Gene3D; 3.40.50.11580; -; 1.
DR   Gene3D; 6.10.140.2090; -; 1.
DR   Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR   Gene3D; 3.40.30.150; Coronavirus polyprotein cleavage domain; 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; 3.40.220.20; Nsp3, SUD-M subdomain; 1.
DR   Gene3D; 3.40.220.30; Nsp3, SUD-N subdomain; 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; 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; 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; IPR021590; NSP1_glob_bCoV.
DR   InterPro; IPR038030; NSP1_glob_sf_bCoV.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR044389; NSP2_SARS-CoV-like.
DR   InterPro; IPR024375; NSP3_bCoV.
DR   InterPro; IPR047567; NSP3_G2M_bCoV.
DR   InterPro; IPR024358; NSP3_N_bCoV.
DR   InterPro; IPR032592; NSP3_NAB_bCoV.
DR   InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR   InterPro; IPR038166; NSP3_PL2pro_sf_bCoV.
DR   InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR   InterPro; IPR044864; NSP3_SUD-N_bCoV.
DR   InterPro; IPR044374; NSP3_SUD-N_SARS-CoV.
DR   InterPro; IPR043478; NSP3_SUD-N_sf_bCoV.
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; 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; IPR009469; RdRp_N_CoV.
DR   InterPro; IPR044351; RdRp_SARS-CoV-like.
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; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF16251; bCoV_NAB; 1.
DR   Pfam; PF11501; bCoV_NSP1; 1.
DR   Pfam; PF12379; bCoV_NSP3_N; 1.
DR   Pfam; PF12124; bCoV_SUD_C; 1.
DR   Pfam; PF11633; bCoV_SUD_M; 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; PF19211; CoV_NSP2_N; 1.
DR   Pfam; PF19218; CoV_NSP3_C; 1.
DR   Pfam; PF16348; CoV_NSP4_C; 1.
DR   Pfam; PF19217; CoV_NSP4_N; 1.
DR   Pfam; PF19213; CoV_NSP6; 1.
DR   Pfam; PF08716; CoV_NSP7; 1.
DR   Pfam; PF08717; CoV_NSP8; 1.
DR   Pfam; PF08710; CoV_NSP9; 1.
DR   Pfam; PF08715; CoV_peptidase; 1.
DR   Pfam; PF06478; CoV_RPol_N; 1.
DR   Pfam; PF01661; Macro; 1.
DR   Pfam; PF05409; Peptidase_C30; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; 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; SSF160099; SARS Nsp1-like; 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; PS51941; BCOV_NSP3C_M; 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; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51940; SARS_NSP3C_N; 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..179
FT                   /note="Host translation inhibitor nsp1"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289896"
FT   CHAIN           180..818
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289897"
FT   CHAIN           819..2746
FT                   /note="Papain-like proteinase nsp3"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289898"
FT   CHAIN           2747..3246
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289899"
FT   CHAIN           3247..3552
FT                   /note="3C-like proteinase nsp5"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289900"
FT   CHAIN           3553..3842
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289901"
FT   CHAIN           3843..3925
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289902"
FT   CHAIN           3926..4123
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289903"
FT   CHAIN           4124..4236
FT                   /note="Viral protein genome-linked nsp9"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289904"
FT   CHAIN           4237..4375
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289905"
FT   CHAIN           4376..5307
FT                   /note="RNA-directed RNA polymerase nsp12"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289906"
FT   CHAIN           5308..5908
FT                   /note="Helicase nsp13"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289907"
FT   CHAIN           5909..6435
FT                   /note="Guanine-N7 methyltransferase nsp14"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289908"
FT   CHAIN           6436..6781
FT                   /note="Uridylate-specific endoribonuclease nsp15"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289909"
FT   CHAIN           6782..7079
FT                   /note="2'-O-methyltransferase nsp16"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000289910"
FT   TRANSMEM        2209..2229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2310..2330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2357..2377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2761..2781
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2998..3018
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3028..3048
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3060..3080
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3083..3103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3111..3131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3148..3168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3570..3590
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3592..3612
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3618..3638
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3665..3684
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3691..3710
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3734..3754
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3762..3782
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          12..127
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          148..179
FT                   /note="BetaCoV Nsp1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT   DOMAIN          183..456
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          458..688
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          690..818
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          822..930
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1001..1167
FT                   /note="Macro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1213..1341
FT                   /note="Macro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1349..1476
FT                   /note="Macro 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1478..1544
FT                   /note="DPUP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT   DOMAIN          1548..1603
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1617..1881
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1894..2004
FT                   /note="Nucleic acid-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT   DOMAIN          2029..2138
FT                   /note="G2M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT   DOMAIN          2230..2300
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2378..2746
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          3148..3246
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          3247..3552
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3843..3925
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3926..4123
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          4124..4236
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          4237..4375
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   DOMAIN          4382..4636
FT                   /note="NiRAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT   DOMAIN          4641..4739
FT                   /note="Nsp12 Interface"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   DOMAIN          4740..5307
FT                   /note="Nsp12 RNA-dependent RNA polymerase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   DOMAIN          4987..5149
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          5308..5420
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   DOMAIN          5564..5745
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          5746..5915
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          5980..6195
FT                   /note="ExoN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   DOMAIN          6204..6435
FT                   /note="N7-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   DOMAIN          6436..6496
FT                   /note="Nsp15 N-terminal oligomerization"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT   DOMAIN          6497..6622
FT                   /note="AV-Nsp11N/CoV-Nsp15M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT   DOMAIN          6639..6778
FT                   /note="NendoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   DOMAIN          6783..7077
FT                   /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ZN_FING         1735..1772
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4310..4326
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4353..4366
FT                   /evidence="ECO:0000250"
FT   REGION          200..236
FT                   /note="C2H2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          323..344
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          370..416
FT                   /note="C2HC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          2098..2377
FT                   /note="HD1"
FT                   /evidence="ECO:0000250"
FT   REGION          2378..2468
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2382..2395
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2428..2438
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2469..2746
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2469..2563
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2564..2645
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2646..2746
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2761..3168
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3570..3782
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   REGION          4742..4956
FT                   /note="RdRp Fingers N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4957..4995
FT                   /note="RdRp Palm N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4996..5054
FT                   /note="RdRp Fingers C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5055..5190
FT                   /note="RdRp Palm C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5191..5307
FT                   /note="RdRp Thumb"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          6322..6336
FT                   /note="GpppA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   ACT_SITE        1657
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1818
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1832
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3287
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3391
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        5134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5135
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5998
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6000
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6099
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6669
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6684
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6724
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6827
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6911
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6951
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6984
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         370
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1735
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1738
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1770
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1772
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2387
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4366
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4584
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT   BINDING         4593
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT   BINDING         4670
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4676
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4681
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4685
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4862
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5017
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5020
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5021
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5340
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5346
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5379
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5589..5596
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         6115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6239..6245
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   SITE            179..180
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   SITE            818..819
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3246..3247
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3552..3553
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3842..3843
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3925..3926
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4123..4124
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4236..4237
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4375..4376
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            5307..5308
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            5908..5909
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6435..6436
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6781..6782
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   DISULFID        2246..2274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2265..2271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
SQ   SEQUENCE   7079 AA;  791654 MW;  CE92AE7AE019B902 CRC64;
     MESLALGVSE KTHVQLSLPV LQVRDVLVRG FGDSVEEALA EAREHLKNGT CGLVELEKGV
     LPQLEQPYVF IKRSDAQGTN HGYKVVELVA ELDGIQYGRS GTTLGVLVPH VGETPVAYRN
     VLLRKNGNKG AGGHSYGIDL KSYDLGVELG TDPIEDYEQN WNTKHGGGVL RELIRELNGG
     AFTRYVDNNF CGPDGYPLEC IKDLLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW
     FTERSEKSYE RQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
     RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV CEGPTTCGYL
     PANAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG GRTKCFGGCV FAYVGCYNKR
     AYWVPRASAN IGASHTGITG DNVETLNEDL MEILNRDRVN INIVGDFHLN EEVAIILASF
     SASTCAFVDT VKGLDYKTFK DIVESCGNFK VTRGRAKKGA WNIGQEKSIL TPLYGFPSQA
     AGVIRSIFTR ALDTANHSIP DLQRAAITIL DGISEQSLRL IDAMVYTSDL LTNSVIVMAY
     VTGGLVQQIT QWLSNMLGTT VDKLKPVFTW VEAKLSAGIE FLRDAWEILK FLVTGVFDIV
     KGQIQVASDN LKECVKAFLD VLNKALEMCI DQVIIAGAKL RTLNLGEVFI AQSKGLYRQC
     IRGKEQLQLL MPLRAPKEVT FFEGDSHDTV FTSEEVVLKN GELEALETPV DSFTNGAVIG
     TPVCVNGLML LELKDKEQYC ALSPGLLATN NVFSLKGGAP VKGVTFGEDT VLEVQGYKNV
     KITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
     WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEEYEDE EEIPEETCEH EYGTEDDYKG
     LPLEFGASTE IQQVDEEEEE DWLEEAIAAK PEPEPLPEEP VNQFTGYLKL TDNVAIKCVD
     IVKEAQHAKP TVIVNAANVH LKHGGGVAGA LNKATNGAMQ QESDDYIKKN GPLTVGGSCL
     LSGHNLAKKC MHVVGPNLNA GEDVQLLKAA YANFNSQDVL LAPLLSAGIF GAKPLQSLKM
     CVETVRTQVY FAVNDQDLYD HVVLGYLDSL KPKVETPTQE NLELKEQPAV ETLTQENLEL
     EELPVIEKPV DVKFKARIEE VNTSLEETKF LTSRLLLFAD INGKLYQDSQ NMLRGEDMFF
     LEKDAPYIVG DVISSGDITC VIIPAKKAGG TTEMLAKALK KVPVSEYITT YPGQGCAGYT
     LEEAKTALRK CKSVFYVLPS KTPNDKEEIL GTVSWNLREM LAHAEETRKL MLICMDVKAL
     MSTIHRRYKG IKVQEGIVDY GVRFFFYTSK EPVASIITKL NLLNEPLVTM PIGYVTHGLN
     LEEAARCMRS LKAPAVVSVS SPDAVTTYNG YLTSSSKTSE EHFIETVSLA GMYRDWSYSG
     QRTELGVEFL KRGDKVVYHT VGSPIQFHLD GEVLLLDKLK SLLSLREVRT IKVFTTVDNT
     NLHTQIVDMS MTYGQQFGPT YLDGADVTKI KPHAKHEGKT FFVLPSDDTL RSEAFEYYHT
     LDESFLGRYM SALNHTKKWK FPQIGGLTSI KWADNNCYLS SVLLALQQIE VKFNAPALQE
     AYYRARAGDA ANFCALILAY SNRTVGELGD VRETMTHLLQ HANLESAKRV LNVVCKTCGQ
     KSTTLTGVEA VMYMGTLSYE ELKTGVTIPC ICGRDATQYL VQQESSFVMM SAPPSEYTLQ
     QGAFLCANEY TGSYQCGHYT HVTVKETLYR IDGAYLTKMS EYKGPVTDVF YKEISYTTTI
     KPVSYKLDGV IYTEIQPKLD EYYKKDNAYY TEQPIDLVPT QPLPNASFDN FKLTCSNTKF
     ADDLNQMTGF KKPASRELSV TFFPDLNGDV VAIDYRHYSA SFKKGAKLLH KPIIWHINQT
     TNKTTYKPNT WCLRCLWSTK PVETSNSFEV LEVEDTQGMD NLACESQTPT SEEVVENPTI
     QKEVIECDVK TIEVVGNVIL KPSEEGVKVT QELGHEDLMA AYVEETSITI KKPNELSLAL
     GLRTLATHGA AAINSVPWSK ILAYVKPFLG QAAVTTTNCI KRCVQRVFNN YMPYVITLLF
     QLCTFTRSTN SRIRASLPTT IAKNSVKSVA KLCLDVCINY VKSPKFSKLF TIAMWLLLLS
     ICLGSLIYVT AAFGVLLSNL GIPSYCDGVR ESYVNSSNVT TMDFCEGSFL CSVCLNGLDS
     LDSYPALETI QVTISSYKLD LTSLGLAAEW FLAYMLFTKF FYLLGLSAIM QVFFGYFASH
     FISNSWLMWF IISIVQMAPV SAMVRMYIFF AFCYYVWKSY VHIMDGCTSS TCMMCYKRNR
     ATRVECTTIV NGMKRSFYVY ANGGRGFCKA HNWNCLNCDT FCAGSTFISD EVARDLSLQF
     KRPINPTDQS SYVVDSVAVK NGALHLYFDK AGQKTYERHP LSHFVNLDNL RANNTKGSLP
     INVIVFDGKS KCDESAAKSA SVYYSQLMCQ PILLLDQALV SDVGDSTEVS VKMFDAYVDT
     FSATFSVPME KLKALVATAH SELAKGVALD GVLSTFVSAA RQGVVDTDVD TKDVIECLKL
     SHHSDLEVTG DSCNNFMLTY NKVENMTPRD LGACIDCNAR HINAQVAKSH NVSLIWNVKD
     YMSLSEQLRK QIRSAAKKNN IPFRLTCATT RQVVNAITTK ISLKGGKIVS TWFKLMLKAT
     LLCVLAALFC YIIMPVHSLS VHDGYTNEII GYKAIQDGVT RDIMATDDCF ANKHAGFDSW
     FSQRGGSYRN DKSCPVVAAI ITREIGFIVP GLPGTVLRAI NGDFLHFLPR VFSAVGNICY
     TPSKLIEYSD FATSACVLAA ECTIFKDAMG KPVPYCYDTN LLEGSISYSE LRPDTRYVLM
     DGSIIQFPNT YLEGSVRVVT TFDAEYCRHG TCERSEAGVC LSTSGRWVLN NEHYRALPGV
     FCGVDAMNLI ANIFTPLVQP VGALDVSASV VAGGIIAILV TCAAYYFMKF RRAFGEYNHV
     VAANALLFLM SFTILCLAPA YSFLPGVYSI FYLYLTFYFT NDVSFLAHLQ WFAMFSPIVP
     FWITAIYVFC ISLKHCHWFF NNYLRKRVMF NGVTFSTFEE AALCTFLLNK EMYLKLRSET
     LLPLTQYNRY LALYNKYKYF SGALDTTSYR EAACCHLAKA LNDFSNSGAD VLYQPPQTSI
     TSAVLQSGFR KMAFPSGKVE GCMVQVTCGT TTLNGLWLDD TVYCPRHVIC TAEDMLNPNY
     EDLLIRKSNH SFLVQAGNVQ LRVIGHSMQN CLLRLKVDTS NPKTPKYKFV RIQPGQTFSV
     LACYNGSPSG VYQCAMRPNY TIKGSFLNGS CGSVGFNIDY DCVSFCYMHH MELPTGVHAG
     TDLEGKFYGP FVDRQTAQAA GTDTTITLNV LAWLYAAVIN GDRWFLNRFT TTLNDFNLVA
     MKYNYEPLTQ DHVDILGPLS AQTGIAVLDM CAALKELLQN GMNGRTILGS TILEDEFTPF
     DVVRQCSGVT FQGKFKKIVK GTHHWMLLTF LTSLLILVQS TQWSLFFFVY ENAFLPFTLG
     IMAIAACAML LVKHKHAFLC LFLLPSLATV AYFNMVYMPA SWVMRIMTWL ELADTSLSGY
     RLKDCVMYAS ALVLLVLMTA RTVYDDAARR VWTLMNVITL VYKVYYGNSL DQAISMWALV
     ISVTSNYSGV VTTIMFLARA IVFVCVEYYP LLFITGNTLQ CIMLVYCFLG YCCCCYFGLF
     CLLNRYFRLT LGVYDYLVST QEFRYMNSQG LLPPKSSIDA FKLNIKLLGI GGKPCIKVAT
     VQSKMSDVKC TSVVLLSVLQ QLRVESSSKL WAQCVQLHND ILLAKDTTEA FEKMVSLLSV
     LLSMQGAVDI NKLCEEMLDN RATLQAIASE FSSLPSYAAY ATAQEAYEQA VANGDSEVVL
     KKLKKSLNVA KSEFDRDAAM QRKLEKMADQ AMTQMYKQAR SEDKRAKVTS AMQTMLFTML
     RKLDNDALNN IINNARDGCV PLNIIPLTTA AKLMVVVPDY GTYKNTCDGN TFTYASALWE
     IQQVVDADSK IVQLSEINMD NSQNLAWPLI VTALRANSAV KLQNNELSPV ALRQMSCAAG
     TTQTACTDDN ALAYYNNSKG GRFVLALLSD HQDLKWARFP KSDGTGTIYT ELEPPCRFVT
     DTPRGPKVKY LYFIKGLNNL NRGMVLGSLA ATVRLQAGNA TEVPANSAVL SFCAFAVDPA
     KAYKDYLASG GQPITNCVKM LCTHTGTGQA ITVTPEANMD QESFGGASCC LYCRCHIDHP
     NPKGFCDLKG KYVQIPATCA NDPVGFTLKN TVCTVCGTWK GYGCSCDQLR EPMMQSADAS
     TFLNRVCGVS AARLTPCGTG TSTDVVYRAF DIYNERVAGF AKFLKTNCCR FQEKDEEGNL
     LDSYFVVKRH TMSNYQHEET IYNLVKECPA VAVHDFFKFR VDGDMVPHIS RQRLTKYTMA
     DLVYALRHFD EGNCDTLKEI LVTYNCCDDD YFNKKDWYDF VENPDILRVY ANLGERVRQA
     LLKTVQFCDA MRDAGIVGVL TLDNQDLNGN WYDFGDFVQV APGCGVPIVD SYYSLLMPIL
     TLTKALAAES HMDADLAKPL IKWDLLKYDF TEERLCLFDR YFKYWDQTYH PNCINCLDDR
     CILHCANFNV LFSTVFPPTS FGPLVRKIFV DGVPFVVSTG YHFRELGVVH NQDVNLHSSR
     LSFKELLVYA ADPAMHAASG NLLLDKRTTC FSVAALTNNV AFQTVKPGNF NKDFYDFAVS
     KGFFKEGSSV ELKHFFFAQD GNAAISDYDY YRYNLPTMCD IRQLLFVVEV VDKYFDCYDG
     GCINANQVIV NNLDKSAGFP FNKWGKARLY YDSMSYEDQD VLFAYTKRNV IPTITQMNLK
     YAISAKNRAR TVAGVSICST MTNRQFHQKL LKSIAATRGA TVVIGTSKFY GGWHNMLKTV
     YSDVETPHLM GWDYPKCDRA MPNMLRIMAS LVLARKHSTC CNLSHRFYRL ANECAQVLSE
     MVMCGGSLYV KPGGTSSGDA TTAYANSVFN ICQAVTANVN ALLSTDGNKI ADKYVRNLQH
     RLYECLYRNR DVDHEFVDEF YAYLRKHFSM MILSDDAVVC YNSNYAAQGL VASIKNFKAV
     HYYQNNVFMS EAKCWTETDL TKGPHEFCSQ HTMLVKQGDD YVYLPYPDPS RILGAGCFVD
     DIVKTDGTLM IERFVSLAID AYPLTKHPNQ EYADVFHLYL QYIRKLHDEL TGHMLDMYSV
     MLTNDNTSRY WEPEFYEAMY TPHTVLQAVG ACVLCNSQTS LRCGACIRRP FLCCKCCYDH
     VISTSHKLVL SVNPYVCNAP GCDVTDVTQL YLGGMSYYCK LHKPPISFPL CANGQVFGLY
     KNTCVGSDNV TDFNAIATCD WTNAGDYILA NTCTERLKLF AAETLKATEE TFKLSYGIAT
     VREVLSDREL HLSWEVGKPR PPLNRNYVFT GYRVTKNSKV QIGEYTFEKG DYGDAVVYRG
     TTTYKLNVGD YFVLTSHTVM PLSAPTLVPQ EHYVRITGLY PTLNISDEFS SNVANYQKVG
     MQKYSTLQGP PGTGKSHFAI GLALYYPSAR IVYTACSHAA VDALCEKALK YLPIDKCSRI
     IPARARVECF DKFKVNSTLE QYVFCTVNAL PETTADIVVF DEISMATNYD LSVVNARLRA
     KHYVYIGDPA QLPAPRTLLT KGTLEPEYFN SVCRLMKTIG PDMFLGTCRR CPAEIVDTVS
     ALVYDNKLKA HKEKSAQCFK MFYKGVITHD VSSAINRPQI GVVREFLTRN PAWRKAVFIS
     PYNSQNAVAS KILGLPTQTV DSSQGSEYDY VIFTQTTETA HSCNVNRFNV AITRAKIGIL
     CIMSDRDLYD KLQFTSLEVP RRNVATLQAE NVTGLFKDCS KIITGLHPTQ APTHLSVDTK
     FKTEGLCVDI PGIPKDMTYR RLISMMGFKM NYQVNGYPNM FITREEAIRH VRAWIGFDVE
     GCHATRDAVG TNLPLQLGFS TGVNLVAVPT GYVDTENNTE FTRVNAKPPP GDQFKHLIPL
     MYKGLPWNVV RIKIVQMLSD TLKGLSDRVV FVLWAHGFEL TSMKYFVKIG PERTCCLCDR
     RATCFSTSSD TYACWNHSVG FDYVYNPFMI DVQQWGFTGN LQSNHDQHCQ VHGNAHVASC
     DAIMTRCLAV HECFVKRVDW SVEYPIIGDE LKINAACRKV QHMVVKSALL ADKFSVLHDI
     GNPKAIKCVP QAEVDWKFYD AQPCSDKAYK IEELFYSYAT HHDKFTDGVC LFWNCNVDRY
     PANAIVCRFD TRVLSNLNLP GCDGGSLYVN KHAFHTPAFD KSAFTYLKQL PFFYYSDSPC
     ESHGKQVVSD IDYVPLKSAT CITRCNLGGA VCRRHANEYR QYLDAYNMMI SAGFSLWIYK
     QFDTYNLWNT FTRLQSLENV AYNVVNKGHF DGQIGEAPVS IINNAVYTKV DGNDVEIFEN
     KTTLPVNVAF ELWAKRNIKP VPEIKILNNL GVDIAANTVI WDYKREAPAH VSTIGVCTMT
     DIAKKPTESA CSSLTVLFDG RVEGQVDLFR NARNGVLITE GSVKGLTPSK GPAQASVNGV
     TLIGESVKTQ FNYFKKVDGI IQQLPETYFT QSRDLEDFKP RSKMETDFLE LAMDEFIQRY
     KLEGYAFEHI VYGDFSHGQL GGLHLMIGLA KRSQDSPLKL EDFIPTDSTV KNYFITDAQT
     GSSKCVCSVI DLLLDDFVEI IKSQDLSVIS KVVKVTIDYA EISFMLWCKD GHVETFYPKL
     QASQAWQPGV AMPNLYKMQR MLLEKCDLQN YGENAVIPKG IMMNVAKYTQ LCQYLNTLTL
     AVPYNMRVIH FGAGSDKGVA PGTAVLRQWL PTGALLVDSD LNDFVSDADS TLIGDCATVH
     TANKWDLIIS DMYDPKTKHV TKENDSKEGF FTYLCGFIKQ KLALGGSVAV KITEHSWNAD
     LYKLMGHFSW WTAFVTNVNA SSSEAFLIGV NYLGKLREQI DGYTMHANYI FWRNTNPIQL
     SSYSLFDMSK FPLKLRGTAV MSLKENQIND MIYSLLENGR LIIRENNRVV VSSDILVNN
//