ID   R1AB_BCHK9              Reviewed;        6930 AA.
AC   P0C6W5; A3EXG5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 106.
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 HKU9 (BtCoV) (BtCoV/HKU9).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Nobecovirus.
OX   NCBI_TaxID=694006;
OH   NCBI_TaxID=9408; Rousettus leschenaultii (Leschenault's rousette).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate HKU9-1;
RX   PubMed=17121802; DOI=10.1128/jvi.02182-06;
RA   Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA   Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA   Zheng B.-J., Yuen K.-Y.;
RT   "Comparative analysis of twelve genomes of three novel group 2c and group
RT   2d coronaviruses reveals unique group and subgroup features.";
RL   J. Virol. 81:1574-1585(2007).
RN   [2]
RP   FUNCTION OF NSP1.
RX   PubMed=19264783; DOI=10.1128/jvi.02485-08;
RA   Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K., Makino S.;
RT   "Suppression of host gene expression by nsp1 proteins of group 2 bat
RT   coronaviruses.";
RL   J. Virol. 83:5282-5288(2009).
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       ECO:0000269|PubMed:19264783}.
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=P0C6W5-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6T6-1; 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: [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; EF065513; ABN10910.1; -; Genomic_RNA.
DR   RefSeq; YP_001039970.1; NC_009021.1. [P0C6W5-1]
DR   PDB; 5UTV; NMR; -; A=1345-1418.
DR   PDBsum; 5UTV; -.
DR   SMR; P0C6W5; -.
DR   IntAct; P0C6W5; 1.
DR   BindingDB; P0C6W5; -.
DR   GeneID; 4836014; -.
DR   KEGG; vg:4836014; -.
DR   Proteomes; UP000006576; 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; cd21596; batCoV-HKU9-like_RdRp; 1.
DR   CDD; cd21560; betaCoV-Nsp6; 1.
DR   CDD; cd21722; betaCoV_Nsp13-helicase; 1.
DR   CDD; cd21659; betaCoV_Nsp14; 1.
DR   CDD; cd21518; betaCoV_Nsp2_HKU9-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; cd21877; HKU9-like_Nsp1; 1.
DR   CDD; cd21813; HKU9-like_Nsp3_betaSM; 1.
DR   CDD; cd21825; HKU9-like_Nsp3_NAB; 1.
DR   CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR   CDD; cd21563; Macro_cv_SUD-M_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; cd21689; stalk_CoV_Nsp13-like; 1.
DR   CDD; cd21537; SUD_C_HKU9_CoV_Nsp3; 1.
DR   CDD; cd21715; TM_Y_HKU9-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; 3.40.220.10; 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; 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; IPR044386; NSP2_HKU9-like.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR024375; NSP3_bCoV.
DR   InterPro; IPR047567; NSP3_G2M_bCoV.
DR   InterPro; IPR032592; NSP3_NAB_bCoV.
DR   InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR   InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR   InterPro; IPR044352; Nsp3_SUD_C_HKU9_CoV.
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; IPR044349; RdRp_batCoV_HKU9-like.
DR   InterPro; IPR046441; RdRp_CoV.
DR   InterPro; IPR009469; RdRp_N_CoV.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; 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; PF13604; AAA_30; 1.
DR   Pfam; PF16251; bCoV_NAB; 1.
DR   Pfam; PF11501; bCoV_NSP1; 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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; 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; Reference proteome;
KW   Repeat; 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..175
FT                   /note="Host translation inhibitor nsp1"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291350"
FT   CHAIN           176..772
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291351"
FT   CHAIN           773..2609
FT                   /note="Papain-like proteinase nsp3"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291352"
FT   CHAIN           2610..3103
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291353"
FT   CHAIN           3104..3409
FT                   /note="3C-like proteinase nsp5"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291354"
FT   CHAIN           3410..3699
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291355"
FT   CHAIN           3700..3782
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291356"
FT   CHAIN           3783..3982
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291357"
FT   CHAIN           3983..4094
FT                   /note="Viral protein genome-linked nsp9"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291358"
FT   CHAIN           4095..4233
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291359"
FT   CHAIN           4234..5165
FT                   /note="RNA-directed RNA polymerase nsp12"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291360"
FT   CHAIN           5166..5766
FT                   /note="Helicase nsp13"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291361"
FT   CHAIN           5767..6296
FT                   /note="Guanine-N7 methyltransferase nsp14"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291362"
FT   CHAIN           6297..6633
FT                   /note="Uridylate-specific endoribonuclease nsp15"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291363"
FT   CHAIN           6634..6930
FT                   /note="2'-O-methyltransferase nsp16"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT                   /id="PRO_0000291364"
FT   TRANSMEM        2015..2035
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2040..2060
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2081..2101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2162..2182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2183..2203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2218..2238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2621..2641
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2719..2739
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2865..2885
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2887..2907
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2916..2936
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2946..2966
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2970..2990
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3423..3443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3449..3469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3474..3494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3517..3537
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3569..3589
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3592..3612
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3620..3640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          10..131
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          149..175
FT                   /note="BetaCoV Nsp1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT   DOMAIN          177..431
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          432..644
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          646..772
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          775..885
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          930..1097
FT                   /note="Macro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1216..1340
FT                   /note="Macro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1345..1417
FT                   /note="DPUP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT   DOMAIN          1423..1478
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1492..1757
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1770..1870
FT                   /note="Nucleic acid-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT   DOMAIN          1883..2012
FT                   /note="G2M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT   DOMAIN          2105..2162
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2239..2610
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          3007..3103
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          3104..3409
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3700..3782
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3783..3982
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          3983..4094
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          4095..4233
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   DOMAIN          4239..4494
FT                   /note="NiRAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT   DOMAIN          4499..4597
FT                   /note="Nsp12 Interface"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   DOMAIN          4598..5165
FT                   /note="Nsp12 RNA-dependent RNA polymerase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   DOMAIN          4845..5007
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          5166..5278
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   DOMAIN          5412..5603
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          5604..5778
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          5838..6056
FT                   /note="ExoN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   DOMAIN          6065..6296
FT                   /note="N7-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   DOMAIN          6297..6357
FT                   /note="Nsp15 N-terminal oligomerization"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT   DOMAIN          6358..6476
FT                   /note="AV-Nsp11N/CoV-Nsp15M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT   DOMAIN          6493..6630
FT                   /note="NendoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   DOMAIN          6635..6928
FT                   /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ZN_FING         1610..1647
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4168..4184
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4211..4224
FT                   /evidence="ECO:0000250"
FT   REGION          312..333
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          1188..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2015..2238
FT                   /note="HD1"
FT                   /evidence="ECO:0000250"
FT   REGION          2239..2329
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2243..2256
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2289..2299
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2330..2610
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2330..2425
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2426..2509
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2510..2610
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2621..2990
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3423..3640
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   REGION          4600..4814
FT                   /note="RdRp Fingers N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4815..4853
FT                   /note="RdRp Palm N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4854..4912
FT                   /note="RdRp Fingers C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4913..5048
FT                   /note="RdRp Palm C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5049..5165
FT                   /note="RdRp Thumb"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          6180..6194
FT                   /note="GpppA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   ACT_SITE        1533
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1694
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1708
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3144
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3248
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        4992
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        4993
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        4994
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5856
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5858
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5957
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6037
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6042
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6523
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6537
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6576
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6679
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6763
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6803
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6836
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1610
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1613
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1645
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1647
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4442
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT   BINDING         4451
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT   BINDING         4528
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4534
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4539
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4543
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4720
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4875
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4878
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4879
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5237
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5447..5454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         5973
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5976
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5992
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5995
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6026
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6030
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6033
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6048
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6100..6106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   SITE            175..176
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            772..773
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            2609..2610
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3103..3104
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3409..3410
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3699..3700
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3782..3783
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            3982..3983
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4094..4095
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            4233..4234
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            5165..5166
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            5766..5767
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            6296..6297
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   SITE            6633..6634
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000255"
FT   DISULFID        2121..2138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   HELIX           1346..1355
FT                   /evidence="ECO:0007829|PDB:5UTV"
FT   STRAND          1360..1364
FT                   /evidence="ECO:0007829|PDB:5UTV"
FT   STRAND          1368..1371
FT                   /evidence="ECO:0007829|PDB:5UTV"
FT   STRAND          1374..1382
FT                   /evidence="ECO:0007829|PDB:5UTV"
FT   STRAND          1385..1389
FT                   /evidence="ECO:0007829|PDB:5UTV"
FT   STRAND          1394..1398
FT                   /evidence="ECO:0007829|PDB:5UTV"
FT   STRAND          1401..1404
FT                   /evidence="ECO:0007829|PDB:5UTV"
FT   STRAND          1406..1408
FT                   /evidence="ECO:0007829|PDB:5UTV"
FT   HELIX           1409..1415
FT                   /evidence="ECO:0007829|PDB:5UTV"
SQ   SEQUENCE   6930 AA;  769729 MW;  9ED06D0888C7EC7B CRC64;
     MEGVPDPPKL KSMVVTTLKW CDPFANPNVT GWDIPIEEAL EYAKQQLRTP EPQLVFVPYY
     LSHAPGISGD RVVITDSIWY ATNFGWQPIR ELAMDKDGVR YGRGGTHGVL LPMQDPSFIM
     GDIDIQIRKY GIGANSPPDV LPLWDGFSDP GPDVGPYLDF PDNCCPTKPK AKRGGDVYLS
     DQYGFDNNGI LVEPVMKLLG VIKSDFTLEQ LLAALGKYRT EDGYDLPDGY VKVAIKVGRK
     AVPVLKQSIF TVVGVTEQLV PGYYYPFSTS SVVEHTKPTR GGPVGKTVEA VMLSLYGTNN
     YNPATPVARL KCSYCDYYGW TPLKDIGTVN CLCGAEFQLT SSCVDAESAG VIKPGCVMLL
     DKSPGMRLIP GNRTYVSFGG AIWSPIGKVN GVTVWVPRAY SIVAGEHSGA VGSGDTVAIN
     KELVEYLIEG IRVDADTLDN PTCATFIANL DCDTKAPVVH TVESLQGLCL ANKIMLGDKP
     LPTDEFHPFI VGLAYHVQRA CWYGALASRT FEAFRDFVRT EEERFAQFFG KVCAPINGCV
     YLAYTTGRVT LFSAYQVLNT AIAKSKDAFG GVAAIVVDML KPILEWVLKK MSIAKGAWLP
     YAEGLLALFK AQFTVVKGKF QFLRASLNSK CHSLCDLLTT IMSKLLTSVK WAGCKVDALY
     TGTYYYFSRK GVLTEVQLCA KRLGLLLTPK QQKMEVEVLD GDFDAPVTLT DLELEECTGV
     LEEVFGASDV KLVKGTLVSL ASKLFVRTED GFLYRYVKSG GVLGKAFRLR GGGVSKVTFG
     DEEVHTIPNT VTVNFSYDVC EGLDAILDKV MAPFQVEEGT KLEDLACVVQ KAVYERLSDL
     FSDCPAELRP INLEDFLTSE CFVYSKDYEK ILMPEMYFSL EDAVPVDDEM VDDIEDTVEQ
     ASDSDDQWLG DEGAEDCDNT IQDVDVATSM TTPCGYTKIA EHVYIKCADI VQEARNYSYA
     VLVNAANVNL HHGGGVAGAL NRATNNAMQK ESSEYIKANG SLQPGGHVLL SSHGLASHGI
     LHVVGPDKRL GQDLALLDAV YAAYTGFDSV LTPLVSAGIF GFTVEESLCS LVKNVACTTY
     VVVYDRQLYE RALATSFDVP GPQSSVQHVP AIDWAEAVEV QESIVDQVET PSLGAVDTVD
     SNADSGLNET ARSPENVVGS VPDDVVADVE SCVRDLVRQV VKKVKRDKRP PPIVPQQTVE
     QQPQEISSPG DCNTVLVDVV SMSFSAMVNF GKEKGLLIPV VIDYPAFLKV LKRFSPKEGL
     FSSNGYEFYG YSRDKPLHEV SKDLNSLGRP LIMIPFGFIV NGQTLAVSAV SMRGLTVPHT
     VVVPSESSVP LYRAYFNGVF SGDTTAVQDF VVDILLNGAR DWDVLQTTCT VDRKVYKTIC
     KRGNTYLCFD DTNLYAITGD VVLKFATVSK ARAYLETKLC APEPLIKVLT TVDGINYSTV
     LVSTAQSYRA QIGTVFCDGH DWSNKNPMPT DEGTHLYKQD NFSSAEVTAI REYYGVDDSN
     IIARAMSIRK TVQTWPYTVV DGRVLLAQRD SNCYLNVAIS LLQDIDVSFS TPWVCRAYDA
     LKGGNPLPMA EVLIALGKAT PGVSDDAHMV LSAVLNHGTV TARRVMQTVC EHCGVSQMVF
     TGTDACTFYG SVVLDDLYAP VSVVCQCGRP AIRYVSEQKS PWLLMSCTPT QVPLDTSGIW
     KTAIVFRGPV TAGHYMYAVN GTLISVYDAN TRRRTSDLKL PATDILYGPT SFTSDSKVET
     YYLDGVKRTT IDPDFSKYVK RGDYYFTTAP IEVVAAPKLV TSYDGFYLSS CQNPQLAESF
     NKAINATKTG PMKLLTMYPN VAGDVVAISD DNVVAHPYGS LHMGKPVLFV TRPNTWKKLV
     PLLSTVVVNT PNTYDVLAVD PLPVNNETSE EPISVKAPIP LYGLKATMVL NGTTYVPGNK
     GHLLCLKEFT LTDLQTFYVE GVQPFVLLKA SHLSKVLGLR VSDSSLHVNH LSKGVVYAYA
     ATRLTTRVTT SLLGGLVTRS VRKTADFVRS TNPGSKCVGL LCLFYQLFMR FWLLVKKPPI
     VKVSGIIAYN TGCGVTTCVL NYLRSRCGNI SWSRLLKLLR YMLYIWFVWT CLTICGVWLS
     EPYAPSLVTR FKYFLGIVMP CDYVLVNETG TGWLHHLCMA GMDSLDYPAL RMQQHRYGSP
     YNYTYILMLL EAFFAYLLYT PALPIVGILA VLHLIVLYLP IPLGNSWLVV FLYYIIRLVP
     FTSMLRMYIV IAFLWLCYKG FLHVRYGCNN VACLMCYKKN VAKRIECSTV VNGVKRMFYV
     NANGGTHFCT KHNWNCVSCD TYTVDSTFIC RQVALDLSAQ FKRPIIHTDE AYYEVTSVEV
     RNGYVYCYFE SDGQRSYERF PMDAFTNVSK LHYSELKGAA PAFNVLVFDA TNRIEENAVK
     TAAIYYAQLA CKPILLVDKR MVGVVGDDAT IARAMFEAYA QNYLLKYSIA MDKVKHLYST
     ALQQISSGMT VESVLKVFVG STRAEAKDLE SDVDTNDLVS CIRLCHQEGW EWTTDSWNNL
     VPTYIKQDTL STLEVGQFMT ANAKYVNANI AKGAAVNLIW RYADFIKLSE SMRRQLKVAA
     RKTGLNLLVT TSSLKADVPC MVTPFKIIGG HRRIVSWRRV LIHVFMLLVV LNPQWFTPWY
     IMRPIEYNVV DFKVIDNAVI RDITSADQCF ANKFSAFENW YSNRYGSYVN SRGCPMVVGV
     VSDIVGSLVP GLPARFLRVG TTLLPLVNYG LGAVGSVCYT PHYAINYDVF DTSACVLAAT
     CTLFSSASGE RMPYCADAAL IQNASRYDML KPHVMYPFYE HSGYIRFPEV ISAGVHIVRT
     MAMEYCKVGR CDVSEAGLCM SLQPRWVVNN AYFRQQSGVY CGTSAFDLFM NMLLPIFTPV
     GAVDITTSIL MGALLAVVVS MSLYYLLRFR RAFGDYSGVI FTNILAFVLN VIVLCLEGPY
     PMLPSIYAMV FLYATCYFGS DIACMMHVSF LIMFAGVVPL WVTVLYIVVV LSRHILWFAS
     LCTKRTVQVG DLAFHSFQDA ALQTFMLDKE VFLRLKREIS SDAYFKYLAM YNKYKYYSGP
     MDTAAYREAA CSHLVMALEK YSNGGGDTIY QPPRCSVASA ALQAGLTRMA HPSGLVEPCL
     VKVNYGSMTL NGIWLDNFVI CPRHVMCSRD ELANPDYPRL SMRAANYDFH VSQNGHNIRV
     IGHTMEGSLL KLTVDVNNPK TPAYSFIRVS TGQAMSLLAC YDGLPTGVYT CTLRSNGTMR
     ASFLCGSCGS PGFVMNGKEV QFCYLHQLEL PNGTHTGTDF SGVFYGPFED KQVPQLAAPD
     CTITVNVLAW LYAAVLSGEN WFLTKSSISP AEFNNCAVKY MCQSVTSESL QVLQPLAAKT
     GISVERMLSA LKVLLSAGFC GRTIMGSCSL EDEHTPYDIG RQMLGVKLQG KFQSMFRWTL
     QWFAIIFVLT ILILLQLAQW TFVGALPFTL LLPLIGFVAV CVGFVSLLIK HKHTYLTVYL
     LPVAMVTAYY NFQYTPEGVQ GYLLSLYNYV NPGRIDVIGT DLLTMLIISV ACTLLSVRMV
     RTDAYSRIWY VCTAVGWLYN CWTGSADTVA ISYLTFMVSV FTNYTGVACA SLYAAQFMVW
     VLKFLDPTIL LLYGRFRCVL VCYLLVGYLC TCYFGVFNLI NRLFRCTLGN YEYVVSSQEL
     RYMNSHGLLP PTNSWQALML NIKLAGIGGI PIYRVSTIQS NMTDLKCTSV VLLSVLQQLR
     VESSSKLWAL CVKLHNEILA SNSPTEAFEA FVSLLSVLLS LPGAINLDEL CSSILENNSV
     LQAVASEFSN LSSYVDYENA QKAYDTAVAT GAPASTVNAL KKAMNVAKSV LDKDVATTRK
     LERMSELAMT AMYKQARAED RRSKVTAAMQ TMLFNMIRRL DSDALSNILN NARNGVVPLG
     VIPRTAANKL LLVVPDFSVY TATITMPTLT YAGSAWDVMQ VADADGKTVN ATDITRENSV
     NLAWPLVVTA QRQQATSPVK LQNNELMPQT VKRMNVVAGV SQTACVTDAV AYYNATKEGR
     HVMAILADTD GLAFAKVEKS TGDGFVILEL EPPCKFMVDT PKGPALKYLY FTKGLKNLCR
     GTVLGTLACT VRLHAGSATE VASNSSILSL CSFSVDPEAT YKDYLDNGGS PIGNCVKMLT
     PHTGTGLAIT AKPDANIDQE SFGGASCCLY CRCHIEHPGA SGVCKYKGKF VQIPLVGVND
     PIGFCIRNVV CAVCNMWQGY GCPCSSLREI NLQARDECFL NRVRGTSGVA RLVPLGSGVQ
     PDIVLRAFDI CNTKVAGFGL HLKNNCCRYQ ELDADGTQLD SYFVVKRHTE SNYLLEQRCY
     EKLKDCGVVA RHDFFKFNIE GVMTPHVSRE RLTKYTMADL VYSLRHFDNN NCDTLKEILV
     LRGCCTADYF DRKDWYDPVE NPDIIRVYHN LGETVRKAVL SAVKMADSMV EQGLIGVLTL
     DNQDLNGQWY DFGDFIEGPA GAGVAVMDTY YSLAMPVYTM TNMLAAECHV DGDFSKPKRV
     WDICKYDYTQ FKYSLFSKYF KYWDMQYHPN CVACADDRCI LHCANFNILF SMVLPNTSFG
     PLVQKIYVDG VPFVVSTGYH YRELGVVMNQ DIRQHAQRLS LRELLVYAAD PAMHVAASNA
     LADKRTVCMS VAAMTTGVTF QTVKPGQFNE DFYNFAVKCG FFKEGSTISF KHFFYAQDGN
     AAISDYDYYR YNLPTMCDIK QLLFSLEVVD KYFDCYDGGC LQASQVVVAN YDKSAGFPFN
     KFGKARLYYE SLSYADQDEL FAYTKRNVLP TITQMNLKYA ISAKNRARTV AGVSIASTMT
     NRQFHQKMLK SIAAARGASV VIGTTKFYGG WNRMLRTLCE GVENPHLMGW DYPKCDRAMP
     NLLRIFASLI LARKHATCCN ASERFYRLAN ECAQVLSEMV LCGGGFYVKP GGTSSGDSTT
     AYANSVFNIC QAVSANLNTF LSIDGNKIYT TYVQELQRRL YLGIYRSNTV DNELVLDYYN
     YLRKHFSMMI LSDDGVVCYN ADYAQKGYVA DIQGFKELLY FQNNVFMSES KCWVEPDITK
     GPHEFCSQHT MLVDMKGEQV YLPYPDPSRI LGAGCFVDDL LKTDGTLMME RYVSLAIDAY
     PLTKHPDPEY QNVFWCYLQY IKKLHEELTG HLLDTYSVML ASDNASKYWE VEFYENMYME
     SATLQSVGTC VVCNSQTSLR CGGCIRRPFL CCKCCYDHVV STTHKLVLSV TPYVCNNPSC
     DVADVTQLYL GGMSYYCRDH RPPISFPLCA NGQVFGLYKN ICTGSPDVAD FNSLATCDWS
     NSKDYVLANT ATERLKLFAA ETLRATEENA KQAYASAVVK EVLSDRELVL SWETGKTRPP
     LNRNYVFTGF HITKNSKVQL GEYIFEKGDY GDVVNYRSST TYKLQVGDYF VLTSHSVQPL
     SSPTLLPQER YTKLVGLYPA MNVPESFASN VVHYQRVGMS RYTTVQGPPG TGKSHLSIGL
     ALYYPSAKIV YTACSHAAVD ALCEKAHKNL PINRCSRIVP AKARVECFSK FKVNDVGAQY
     VFSTINALPE TTADILVVDE VSMCTNYDLS MINARVRAKH IVYVGDPAQL PAPRTLLTKG
     TLAPEHFNSV CRLMVAVGPD IFLATCYRCP KEIVDTVSAL VYDKKLKANK VTTGECYKCY
     YKGSVTHDSS SAINKPQLGL VKEFLIKNPK WQSAVFISPY NSQNSVARRM LGLQTQTVDS
     SQGSEFDYVI YCQTSDTAHA LNVNRFNVAI TRAKKGILCV MSDSTLYESL EFTPLDVNDY
     VKPKMQSEVT VGLFKDCAKA EPLGPAYAPT FVSVNDKFKL NESLCVHFDT TELQMPYNRL
     ISKMGFKFDL NIPGYSKLFI TREQAIREVR GWVGFDVEGA HACGPNIGTN LPLQIGFSTG
     VNFVVTPSGY IDTESGSRLA NVVSKAPPGD QFKHLIPLMR KGEPWSVVRK RIVEMLCDTL
     DGVSDTVTFV TWAHGFELTT LHYFAKVGPE RKCFMCPRRA TLFSSVYGAY SCWSHHRHIG
     GADFVYNPFL VDVQQWGYVG NLQVNHDNVC DVHKGAHVAS CDAIMTRCLA IHDCFCGEVN
     WDVEYPIIAN ELAINRACRS VQRVVLKAAV KALHIETIYD IGNPKAIKVY GVNVNNWNFY
     DTNPVVEGVK QLHYVYDVHR DQFKDGLAMF WNCNVDCYPH NALVCRFDTR VLSKLNLAGC
     NGGSLYVNQH AFHTDAFNKN AFVNLKPLPF FYYSDTACEN ATGVSTNYVS EVDYVPLKSN
     VCITRCNLGG AVCKKHADEY RNFLESYNTM VSAGFTLWVD KTFDVFNLWS TFVKLQSLEN
     VAYNVLKSGH FTAVAGELPV AILNDRLYIK EDGADKLLFT NNTCLPTNVA FELWAKRSVN
     VVPEVKLLRN LGVTCTYNLV IWDYESNAPL VPNTVGICTY TDLTKLDDQV VLVDGRQLDA
     YSKFCQLKNA IYFSPSKPKC VCTRGPTHAS INGVVVEAPD RGTAFWYAMR KDGAFVQPTD
     GYFTQSRTVD DFQPRTQLEI DFLDLEQSCF LDKYDLHDLG LEHIVYGQFD GTIGGLHLLI
     GAVRRKRTAH LVMETVLGTD TVTSYAVIDQ PTASSKQVCS VVDIILDDFI ALIKAQDRSV
     VSKVVQCCLD FKVFRFMLWC KGGKISTFYP QLQAKQDWKP GYSMPALYKV QNAVLEPCLL
     HNYGQAARLP SGTLMNVAKY TQLCQYLNTC SLAVPAKMRV MHFGAGSDKG VCPGTAVLKQ
     WLPADAYLVD NDLCYCASDA DSTYVGSCET FFSVNKWDFI FSDMYDARTK NTSGDNTSKE
     GFFTYLTGFI RSKLALGGSI AIKITEHSWS ADLYAIMGHF NWWTCFCTSV NSSSSEAFLI
     GVNYIGVGAL LDGWQMHANY VFWRNSTVMQ LSSYSLYDLQ RFPLRLKGTP VMSLKEDQLN
     ELVLNLIRAG RLIVRDAVDI GVRGVACSGV
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