ID R1AB_CVHN2 Reviewed; 7152 AA.
AC P0C6X3; Q14EB2;
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=p28;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p65;
DE Contains:
DE RecName: Full=Papain-like proteinase nsp3;
DE Short=PL-PRO;
DE EC=3.4.19.12;
DE EC=3.4.22.-;
DE AltName: Full=Non-structural protein 3;
DE Short=nsp3;
DE AltName: Full=p210;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE AltName: Full=Peptide HD2;
DE AltName: Full=p44;
DE Contains:
DE RecName: Full=3C-like proteinase nsp5;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.-;
DE AltName: Full=M-PRO;
DE AltName: Full=nsp5;
DE AltName: Full=p27;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE AltName: Full=p10;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE AltName: Full=p22;
DE Contains:
DE RecName: Full=Viral protein genome-linked nsp9;
DE AltName: Full=Non-structural protein 9;
DE Short=nsp9;
DE AltName: Full=RNA-capping enzyme subunit nsp9;
DE AltName: Full=p12;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE AltName: Full=p15;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase nsp12;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE EC=2.7.7.50;
DE AltName: Full=nsp12;
DE AltName: Full=p100;
DE Contains:
DE RecName: Full=Helicase nsp13;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=nsp13;
DE AltName: Full=p67;
DE Contains:
DE RecName: Full=Guanine-N7 methyltransferase nsp14;
DE Short=ExoN;
DE EC=2.1.1.56;
DE EC=3.1.13.-;
DE AltName: Full=nsp14;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease nsp15;
DE EC=4.6.1.-;
DE AltName: Full=NendoU;
DE AltName: Full=nsp15;
DE AltName: Full=p35;
DE Contains:
DE RecName: Full=2'-O-methyltransferase nsp16;
DE EC=2.1.1.57;
DE AltName: Full=nsp16;
GN Name=rep; ORFNames=1a-1b;
OS Human coronavirus HKU1 (isolate N2) (HCoV-HKU1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus; Human coronavirus HKU1.
OX NCBI_TaxID=443240;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16809319; DOI=10.1128/jvi.00509-06;
RA Woo P.C.Y., Lau S.K.P., Yip C.C.Y., Huang Y., Tsoi H.-W., Chan K.-H.,
RA Yuen K.-Y.;
RT "Comparative analysis of 22 coronavirus HKU1 genomes reveals a novel
RT genotype and evidence of natural recombination in coronavirus HKU1.";
RL J. Virol. 80:7136-7145(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;
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: [Viral protein genome-linked nsp9]:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000250|UniProtKB:P0DTD1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000250|UniProtKB:P0DTD1};
CC -!- CATALYTIC ACTIVITY: [Guanine-N7 methyltransferase nsp14]:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67009;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- COFACTOR: [Uridylate-specific endoribonuclease nsp15]:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC Note=Likely affects Nsp15 binding to RNA.
CC {ECO:0000250|UniProtKB:P0C6X7};
CC -!- COFACTOR: [RNA-directed RNA polymerase nsp12]:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0DTD1};
CC -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 4]: Interacts with papain-like
CC protease nsp3 and non-structural protein 6.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [3C-like proteinase nsp5]: Monomer. Homodimer. Only the
CC homodimer shows catalytic activity. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 7]: Interacts with nsp8 and nsp12 to
CC form the replication-transcription complex (RTC): nsp12, nsp7, two
CC subunits of nsp8, and up to two subunits of nsp13.
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBUNIT: [Non-structural protein 8]: Interacts with nsp7, nsp13 and
CC nsp12 to form the replication-transcription complex (RTC): nsp12, nsp7,
CC two subunits of nsp8, and up to two subunits of nsp13.
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBUNIT: [Viral protein genome-linked nsp9]: Interacts with nsp12.
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBUNIT: [Non-structural protein 10]: Interacts with proofreading
CC exoribonuclease nsp14 and 2'-O-methyltransferase nsp16; these
CC interactions enhance nsp14 and nsp16 enzymatic activities.
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase nsp12]: Interacts with nsp7 and
CC nsp8 to form the replication-transcription complex (RTC): nsp12, nsp7,
CC two subunits of nsp8, and up to two subunits of nsp13. Interacts with
CC nsp9. {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBUNIT: [Helicase nsp13]: Interacts with nsp8 to form the replication-
CC transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC to two subunits of nsp13. {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBCELLULAR LOCATION: [Papain-like proteinase nsp3]: Host membrane;
CC Multi-pass membrane protein. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-
CC pass membrane protein. Host cytoplasm. Note=Localizes in virally-
CC induced cytoplasmic double-membrane vesicles.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Viral protein genome-linked nsp9]: Host
CC cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9
CC and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
CC in infection, they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Helicase nsp13]: Host endoplasmic reticulum-
CC Golgi intermediate compartment {ECO:0000305}. Note=The helicase
CC interacts with the N protein in membranous complexes and colocalizes
CC with sites of synthesis of new viral RNA.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease nsp15]: Host
CC cytoplasm, host perinuclear region {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6X3-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6U4-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Isolate N2 belongs to genotype B.
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; AY884001; AAX76519.1; -; Genomic_RNA.
DR SMR; P0C6X3; -.
DR IntAct; P0C6X3; 1.
DR Proteomes; UP000006551; Genome.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd21901; alpha_betaCoV_Nsp10; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21722; betaCoV_Nsp13-helicase; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21519; betaCoV_Nsp2_MHV-like; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd21827; betaCoV_Nsp7; 1.
DR CDD; cd21831; betaCoV_Nsp8; 1.
DR CDD; cd21898; betaCoV_Nsp9; 1.
DR CDD; cd21732; betaCoV_PLPro; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21593; HCoV_HKU1-like_RdRp; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21879; MHV-like_Nsp1; 1.
DR CDD; cd21812; MHV-like_Nsp3_betaSM; 1.
DR CDD; cd21824; MHV-like_Nsp3_NAB; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1.
DR CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR CDD; cd21714; TM_Y_MHV-like_Nsp3_C; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.8.1190; -; 2.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 6.10.140.2090; -; 1.
DR Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR Gene3D; 3.40.50.11020; Replicase polyprotein, nucleic acid-binding domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR046443; a/bCoV_NSP1_glob.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR022570; B-CoV_A_NSP1.
DR InterPro; IPR046442; bCoV_NSP1_C.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR047573; CoV_NSP2_M.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR047566; CoV_NSP3_Y3.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR046435; N7_MTase_CoV.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR046438; NIV_2_O_MTASE.
DR InterPro; IPR046436; NIV_EXON.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR047570; NSP12_IF_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR048673; NSP13_stalk_CoV.
DR InterPro; IPR048672; NSP13_ZBD_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044315; NSP14_betaCoV.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR044330; NSP15_alpha_betaCoV_N.
DR InterPro; IPR044322; NSP15_M_alpha_beta_CoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR044384; NSP2_MHV-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR047567; NSP3_G2M_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044367; NSP6_betaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002705; Pept_C30/C16_B_coronavir.
DR InterPro; IPR013016; Peptidase_C16_CoV.
DR InterPro; IPR008740; Peptidase_C30_CoV.
DR InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043177; PLpro_N_sf_CoV.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR046441; RdRp_CoV.
DR InterPro; IPR044347; RdRp_HCoV_HKU1-like.
DR InterPro; IPR009469; RdRp_N_CoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF13604; AAA_30; 1.
DR Pfam; PF11963; B-CoV_A_NSP1; 1.
DR Pfam; PF16251; bCoV_NAB; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF20631; CoV_NSP13_1B; 1.
DR Pfam; PF20633; CoV_NSP13_stalk; 1.
DR Pfam; PF20632; CoV_NSP13_ZBD; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF19216; CoV_NSP15_M; 1.
DR Pfam; PF19219; CoV_NSP15_N; 1.
DR Pfam; PF19212; CoV_NSP2_C; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF01831; Peptidase_C16; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF144246; Coronavirus NSP10-like; 1.
DR SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF142877; EndoU-like; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF159936; NSP3A-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF101816; Replicase NSP9; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51963; BCOV_NSP1_C; 1.
DR PROSITE; PS51942; BCOV_NSP3C_C; 1.
DR PROSITE; PS51994; BCOV_NSP3E_G2M; 1.
DR PROSITE; PS51945; BCOV_NSP3E_NAB; 1.
DR PROSITE; PS51993; COV_3ECTO; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51962; COV_NSP1; 1.
DR PROSITE; PS52000; COV_NSP12_IF; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51991; COV_NSP2_C; 1.
DR PROSITE; PS51990; COV_NSP2_M; 1.
DR PROSITE; PS51989; COV_NSP2_N; 1.
DR PROSITE; PS51992; COV_NSP3_Y; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 2.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus; ATP-binding;
KW Decay of host mRNAs by virus; Disulfide bond; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
KW Host cytoplasm; Host gene expression shutoff by virus; Host membrane;
KW Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 by virus; Inhibition of host NF-kappa-B by virus;
KW Interferon antiviral system evasion; Lyase; Manganese; Membrane;
KW Metal-binding; Methyltransferase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; 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..222
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297773"
FT CHAIN 223..809
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297774"
FT CHAIN 810..2808
FT /note="Papain-like proteinase nsp3"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297775"
FT CHAIN 2809..3304
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297776"
FT CHAIN 3305..3607
FT /note="3C-like proteinase nsp5"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297777"
FT CHAIN 3608..3894
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297778"
FT CHAIN 3895..3986
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297779"
FT CHAIN 3987..4180
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297780"
FT CHAIN 4181..4290
FT /note="Viral protein genome-linked nsp9"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297781"
FT CHAIN 4291..4427
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297782"
FT CHAIN 4428..5355
FT /note="RNA-directed RNA polymerase nsp12"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297783"
FT CHAIN 5356..5958
FT /note="Helicase nsp13"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297784"
FT CHAIN 5959..6479
FT /note="Guanine-N7 methyltransferase nsp14"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297785"
FT CHAIN 6480..6853
FT /note="Uridylate-specific endoribonuclease nsp15"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297786"
FT CHAIN 6854..7152
FT /note="2'-O-methyltransferase nsp16"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000297787"
FT TRANSMEM 2196..2216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2257..2277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2288..2308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2371..2391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2413..2433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2814..2834
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3089..3109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3121..3141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3148..3168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3173..3193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3621..3641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3646..3666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3671..3691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3714..3734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3742..3762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3770..3790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3813..3833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 54..174
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 192..222
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 226..488
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 493..681
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 697..809
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 811..923
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REPEAT 945..954
FT /note="1"
FT REPEAT 955..964
FT /note="2"
FT REPEAT 965..974
FT /note="3"
FT REPEAT 975..984
FT /note="4"
FT REPEAT 985..994
FT /note="5"
FT REPEAT 995..1004
FT /note="6"
FT REPEAT 1005..1014
FT /note="7"
FT REPEAT 1015..1024
FT /note="8"
FT REPEAT 1025..1034
FT /note="9"
FT REPEAT 1035..1044
FT /note="10"
FT REPEAT 1045..1054
FT /note="11"
FT DOMAIN 1093..1343
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1321..1492
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1548..1619
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1619..1674
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1688..1948
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1962..2063
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2078..2227
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2293..2354
FT /note="3Ecto"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT DOMAIN 2441..2808
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3207..3304
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3305..3607
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3895..3983
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3984..4180
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4181..4290
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4291..4428
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4433..4688
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4689..4787
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT DOMAIN 4788..5355
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 5035..5197
FT /note="RdRp catalytic"
FT DOMAIN 5356..5468
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5611..5792
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5793..5962
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 6029..6244
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6253..6479
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6480..6540
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6541..6661
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6711..6850
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6855..7149
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1208..1236
FT /note="C4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 1805..1841
FT /note="C4-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4364..4380
FT /evidence="ECO:0000250"
FT ZN_FING 4406..4419
FT /evidence="ECO:0000250"
FT REGION 365..389
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 945..1054
FT /note="11 X 10 AA tandem repeat of N-[DN]-D-E-D-V-V-T-G-D"
FT REGION 947..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2196..2433
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2441..2531
FT /note="Y1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2445..2458
FT /note="ZF1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2491..2501
FT /note="ZF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2532..2808
FT /note="CoV-Y"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2532..2624
FT /note="Y2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2625..2707
FT /note="Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2708..2808
FT /note="Y4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT REGION 2814..3193
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3621..3833
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 4790..5004
FT /note="RdRp Fingers N-ter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT REGION 5005..5043
FT /note="RdRp Palm N-ter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT REGION 5044..5102
FT /note="RdRp Fingers C-ter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT REGION 5103..5238
FT /note="RdRp Palm C-ter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT REGION 5239..5355
FT /note="RdRp Thumb"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT REGION 6366..6380
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1131
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1282
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1293
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1727
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1884
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1898
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3345
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3449
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 5182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 6047
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6049
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6756
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6796
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6983
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 7023
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 7056
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 1208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1805
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1807
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1839
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 1841
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT BINDING 2445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2494
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 2501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT BINDING 4364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4636
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT BINDING 4645
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DTD1"
FT BINDING 4718
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT BINDING 4724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT BINDING 4729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT BINDING 4733
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT BINDING 4910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT BINDING 5065
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT BINDING 5068
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT BINDING 5069
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT BINDING 5360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5636..5643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 6164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6288..6294
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 222..223
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 809..810
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 2808..2809
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 3304..3305
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3607..3608
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3894..3895
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3986..3987
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4180..4181
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4290..4291
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4427..4428
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5355..5356
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6479..6480
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6853..6854
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT DISULFID 2309..2333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT DISULFID 2324..2330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
SQ SEQUENCE 7152 AA; 807495 MW; 1B6E93484EF69631 CRC64;
MIKTSKYGLG FKWAPEFRWL LPDAAEELAS PMKSDEGGLC PSTGQAMESV GFVYDNHVKI
DCRCILGQEW HVQSNLIRDI FVHEDLHVVE VLTKTAVKSG TAILIKSPLH SLGGFPKGYV
MGLFRSYKTK RYVVHHLSMT TSTTNFGEDF LGWIVPFGFM PSYVHKWFQF CRLYIEESDL
IISNFKFDDY DFSVEDAYAE VHAEPKGKYS QKAYALLRQY RGIKPVLFVD QYGCDYSGKL
ADCLQAYGHY SLQDMRQKQS VWLANCDFDI VVAWHVVRDS RFVMRLQTIA TICGIKYVAQ
PTEDVVDGAV VIREPVHLLS ADAIVLKLPS LMKVMTHMDD FSIKSIYNVD LCDCGFVMQY
GYVDCFNDNC DFYGWVSGNM MDGFSCPLCC TVYDSSEVKA QSSGVIPENP VLFTNSTDTV
NPDSFNLYGY SVTPFGSCIY WSPRPGLWIP IIKSSVKSYD DLVYSGVVGC KSIVKETALI
THALYLDYVQ CKCGNLEQNH ILGVNNSWCR QLLLNRGDYN MLLKNIDLFV KRRADFACKF
AVCGDGFVPF LLDGLIPRSY YLIQSGIFFT SLMSQFSQEV SDMCLKMCIL FMDRVSVATF
YIEHYVNRLV TQFKLLGTTL VNKMVNWFNT MLDASAPATG WLLYQLLNGL FVVSQANFNF
VALIPDYAKI LVNKFYTFFK LLLECVTVDV LKDMPVLKTI NGLVCIVGNK FYNVSTGLIP
GFVLPCNAQE QQIYFFEGVA ESVIVEDDVI ENVKSSLSSY EYCQPPKSVE KICIIDNMYM
GKCGDKFFPI VMNDKNICLL DQAWRFPCAG RKVNFNEKPV VMEIPSLMTV KVMFDLDSTF
DDILGKVCSE FEVEKGVTVD DFVAVVCDAI ENALNSCKDH PVVGYQVRAF LNKLNENVVY
LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEEI VTGDNDDQIV VTGDDVDDIE
SVYDFDTYKA LLVFNDVYND ALFVSYGSSV ETETYFKVNG LWSPTITHTN CWLRSVLLVM
QKLPFKFKDL AIENMWLSYK VGYNQSFVDY LLTTIPKAIV LPQGGYVADF AYWFLNQFDI
NAYANWCCLK CGFSFDLNGL DAVFFYGDIV SHVCKCGHNM TLIAADLPCT LHFSLFDDNF
CAFCTPKKIF IAACAVDVNV CHSVAVIGDE QIDGKFVTKF SGDKFDFIVG YGMSFSMSSF
ELAQLYGLCI TPNVCFVKGD IINVARLVKA DVIVNPANGH MLHGGGVAKA IAVAAGKKFS
KETAAMVKSK GVCQVGDCYV STGGKLCKTI LNIVGPDARQ DGRQSYVLLA RAYKHLNNYD
CCLSTLISAG IFSVPADVSL TYLLGVVDKQ VILVSNNKED FDIIQKCQIT SVVGTKALAV
RLTANVGRVI KFETDAYKLF LSGDDCFVSN SSVIQEVLLL RHDIQLNNDV RDYLLSKMTS
LPKDWRLINK FDVINGVKTV KYFECPNSIY ICSQGKDFGY VCDGSFYKAT VNQVCVLLAK
KIDVLLTVDG VNFKSISLTV GEVFGKILGN VFCDGIDVTK LKCSDFYADK ILYQYENLSL
ADISAVQSSF GFDQQQLLAY YNFLTVCKWS VVVNGPFFSF EQSHNNCYVN VACLMLQHIN
LKFNKWQWQE AWYEFRAGRP HRLVALVLAK GHFKFDEPSD ATDFIRVVLK QADLSGAICE
LELICDCGIK QESRVGVDAV MHFGTLAKTD LFNGYKIGCN CAGRIVHCTK LNVPFLICSN
TPLSKDLPDD VVAANMFMGV GVGHYTHLKC GSPYQHYDAC SVKKYTGVSG CLTDCLYLKN
LTQTFTSMLT NYFLDDVEMV AYNPDLSQYY CDNGKYYTKP IIKAQFKPFA KVDGVYTNFK
LVGHDICAQL NDKLGFNVDL PFVEYKVTVW PVATGDVVLA SDDLYVKRYF KGCETFGKPV
IWLCHDEASL NSLTYFNKPS FKSENRYSVL SVDSVSEESQ GNVVTSVMES QISTKEVKLK
GVRKTVKIED AIIVNDENSS IKVVKSLSLV DVWDMYLTGC DYVVWVANEL SRLVKSPTVR
EYIRYGIKPI TIPIDLLCLR DDNQTLLVPK IFKARAIEFY GFLKWLFIYV FSLLHFTNDK
TIFYTTEIAS KFTFNLFCLA LKNAFQTFRW SIFIKGFLVV ATVFLFWFNF LYINVIFSDF
YLPNISVFPI FVGRIVMWIK ATFGLVTICD FYSKLGVGFT SHFCNGSFIC ELCYSGFDML
DTYAAIDFVQ YEVDRRVLFD YVSLVKLIVE LVIGYSLYTV WFYPLFCLIG LQLFTTWLPD
LFMLETMHWL IRFIVFVANM LPAFVLLRFY IVVTAMYKVV GFIRHIVYGC NKAGCLFCYK
RNCSVRVKCS TIVGGVIRYY DITANGGTGF CVKHQWNCFN CHSFKPGNTF ITVEAAIELS
KELKRPVNPT DASHYVVTDI KQVGCMMRLF YDRDGQRVYD DVDASLFVDI NNLLHSKVKV
VPNLYVVVVE SDADRANFLN AVVFYAQSLY RPILLVDKKL ITTACNGISV TQTMFDVYVD
TFMSHFDVDR KSFNNFVNIA HASLREGVQL EKVLDTFVGC VRKCCSIDSD VETRFITKSM
ISAVAAGLEF TDENYNNLVP TYLKSDNIVA ADLGVLIQNG AKHVQGNVAK AANISCIWFI
DTFNQLTADL QHKLKKACVK TGLKLKLTFN KQEASVPILT TPFSLKGGVV LSNLLYILFF
ISLICFILLW ALLPTYSVYK SDIHLPAYAS FKVIDNGVVR DISVNDLCFA NKFFQFDQWY
ESTFGSFYYH NSMDCPIVVA VMDEDIGSTM FNVPTKVLRH GFHVLHFLTY AFASDSVQCY
TPHIQISYND FYASGCVLSS LCTMFKRGDG TPHPYCYSDG VMKNASLYTS LVPHTRYSLA
NSNGFIRFPD VISEGIVRIV RTRSMTYCRV GACEYAEEGI CFNFNSSWVL NNDYYRSMPG
TFCGRDLFDL FYQFFSSLIR PIDFFSLTAS SIFGAILAIV VVLVFYYLIK LKRAFGDYTS
VVVINVIVWC INFLMLFVFQ VYPICACVYA CFYFYVTLYF PSEISVIMHL QWIVMYGAIM
PFWFCVTYVA MVIANHVLWL FSYCRKIGVN VCNDSTFEET SLTTFMITKD SYCRLKNSVS
DVAYNRYLSL YNKYRYYSGK MDTAAYREAA CSQLAKAMET FNHNNGNDVL YQPPTASVST
SFLQSGIVKM VSPTSKIEPC IVSVTYGSMT LNGLWLDDKV YCPRHVICLS SNMNEPDYSA
LLCRVTLGDF TIMSGRMSLT VVSYQMQGCQ LVLTVSLQNP YTPKYTFGVV KPGETFTVLA
AYNGRPQGAF HVTMRSSYTI KGSFLCGSCG SVGYVLTGDS VKFVYMHQLE LSTGCHTGTD
FTGNFYGPYR DAQVVQLPVK DYVQTVNVIA WLYAAILNNC AWFVQNDVCS IEDFNVWAMT
NGFSQVKADL VLDALASMTG VSIETLLAAI KRLYMGFQGR QILGSCTFED ELAPSDVYQQ
LAGVKLQSKT KRFIKETIYW ILISTFLFSC IISAFVKWTI FMYINTHMIG VTLCVLCFVS
FMMLLVKHKH FYLTMYIIPV LCTLFYVNYL VVYKEGFRGL TYVWLSYFVP AVNFTYVYEV
FYGCILCVFA IFITMHSINH DIFSLMFLVG RIVTLISMWY FGSNLEEDVL LFITAFLGTY
TWTTILSLAI AKIVANWLSV NIFYFTDVPY IKLILLSYLF IGYILSCYWG FFSLLNSVFR
MPMGVYNYKI SVQELRYMNA NGLRPPRNSF EAILLNLKLL GIGGVPVIEV SQIQSKLTDV
KCANVVLLNC LQHLHVASNS RLWQYCSILH NEILSTSDLS VAFDKLAQLL IVLFANPAAV
DTKCLASIDE VSDDYVQDST VLQALQSEFV NMASFVEYEV AKKNLADAKN SGSVNQQQIK
QLEKACNIAK SVYERDKAVA RKLERMADLA LTNMYKEARI NDKKSKVVSA LQTMLFSMVR
KLDNQALNSI LDNAVKGCVP LNAIPALAAN TLTIIIPDKQ VFDKVVDNVY VAYAGSVWHI
QTVQDADGIN KQLTDISVDS NWPLVIIANR YNEVANAVMQ NNELMPHKLK IQVVNSGSDM
NCNIPTQCYY NNGSSGRIVY AVLSDVDGLK YTKIIKDDGN CVVLELDPPC KFSIQDVKGL
KIKYLYFIKG CNTLARGWVV GTLSSTIRLQ AGVATEYAAN SSILSLCAFS VDPKKTYLDY
IQQGGVPIIN CVKMLCDHAG TGMAITIKPE ATINQDSYGG ASVCIYCRAR VEHPDVDGLC
KLRGKFVQVP LGIKDPILYV LTHDVCQVCG FWRDGSCSCV GSGVAVQSKD LNFLNRVRGT
SVNARLVPCA SGLSTDVQLR AFDICNTNRA GIGLYYKVNC CRFQRIDDDG NKLDKFFVVK
RTNLEVYNKE KTYYELTKSC GVVAEHDFFT FDIDGSRVPH IVRKNLSKYT MLDLCYALRH
FDCNDCSVLC EILCEYADCK ESYFSKKDWY DFVENPDIIN IYKKLGPIFN RALLNTVSFA
DTLVKVGLVG VLTLDNQDLY GQWYDFGDFI QTAPGFGVAV ADSYYSYMMP MLTMCHVLDC
ELFVNDSYRQ FDLVQYDFTD YKLELFNKYF KYWGMKYHPN TVDCDNDRCI IHCANFNILF
SMVLPNTCFG PLVRQIFVDG VPFVVSIGYH YKELGVVMNL DVDTHRYRLS LKDLLLYAAD
PAMHVASASA LLDLRTCCFS VAAITSGIKF QTVKPGNFNQ DFYEFVKSKG LFKEGSTVDL
KHFFFTQDGN AAITDYNYYK YNLPTMVDIK QLLFVLEVVY KYFEIYDGGC IPASQVIVNN
YDKSAGYPFN KFGKARLYYE ALSFEEQNEI YAYTKRNVLP TLTQMNLKYA ISAKNRARTV
AGVSILSTMT GRMFHQKCLK SIAATRGVPV VIGTTKFYGG WDDMLRHLIK DVDNPVLMGW
DYPKCDRAMP NILRIVSSLV LARKHEFCCS HGDRFYRLAN ECAQVLSEIV MCGGCYYVKP
GGTSSGDATT AFANSVFNIC QAVTANVCSL MACNGHKIED LSIRNLQKRL YSNVYRTDYV
DYTFVNEYYE FLCKHFSMMI LSDDGVVCYN SDYASKGYIA NISVFQQVLY YQNNVFMSES
KCWVENDITN GPHEFCSQHT MLVKIDGDYV YLPYPDPSRI LGAGCFVDDL LKTDSVLLIE
RFVSLAIDAY PLVHHENEEY QKVFRVYLEY IKKLYNDLGN QILDSYSVIL STCDGLKFTD
ESFYKNMYLK SAVMQSVGAC VVCSSQTSLR CGSCIRKPLL CCKCCYDHVM ATNHKYVLSV
SPYVCNAPNC DVSDVTKLYL GGMSYYCENH KPHYSFKLVM NGMVFGLYKQ SCTGSPYIDD
FNKIASCKWT EVDDYVLANE CIERLKLFAA ETQKATEEAF KQSYASATIQ EIVSDREIIL
CWETGKVKPP LNKNYVFTGY HFTSTGKTVL GEYVFDKSEL TNGVYYRATT TYKLSIGDVF
VLTSHSVANL SAPTLVPQEN YASIRFSSVY SVPLLFQTNV ANYQHIGMKR YCTVQGPPGT
GKSHLAIGLA VYYYTARVVY TAASHAAVDA LCEKAYKFLN INDCTRIIPA KVRVDCYDKF
KINDTTCKYV FTTINALPEL VTDIVVVDEV SMLTNYELSV INARVKAKHY VYIGDPAQLP
APRVLLSKGS LEPRHFNSIT KIMCCLGPDI FLGNCYRCPK EIVETVSALV YDNKLKAKND
NSSLCFKVYF KGQTTHESSS AVNIQQIYLI SKFLKANPVW NSAVFISPYN SQNYVAKRIL
GVQTQTVDSA QGSEYDYVIY SQTAETAHSI NVNRFNVAIT RAKKGIFCVM SNMQLFESLN
FITLPLDKIQ NQTLSRLHCT TNLFKDCSKN FLGYHPAHAP SFLSVDDKYK VNEDLAVCLN
ICEPVLTYSR LISLMGFKLD LTLDGYSKFF ITKDEAIKRV RGWVGFDVEG AHATRDNIGT
NFPLQIGFST GVDFVVEATG LFAERDCYIF KRTVAKAPPG DNFKHLIPLM SKGQKWDVVR
IRIVQMLSDY LLDLSDSVVF ITWSASFELT CLRYFAKLGR ELNCDVCPNR ATCYNSRTGY
YGCWRHSYTC DYVYNPLIVD IQQWGYTGSL TSNHDIICNV HKGAHVASSD AIMTRCLAIY
DCFCKSVNWN LEYPIISNEV SINTSCRLLQ RVMLKAAMLC NRYNLCYDIG NPKGIACVKD
YEFKFYDASP VVKSVKQLFY VYDVHKDNFK DGLCMFWNCN VDKYPSNSIV CRFDTRVLNK
LNLPGCNGGS LYVNKHAFHT NPFTRTVFEN LKPMPFFYYS DTPCVYVDGL ESKQVDYVPL
RSATCITRCN LGGAVCSKHA EDYCKYLESY NVATTAGFTF WVYKTFDFYN LWNTFTMLQS
LENVIYNLVN AGHYDGRIGE LPCAIMNDKV VVKINNVDTV IFKNNTSLPT NIAVELFTKR
SIRHHPELKI LRNLNIDICW KHVLWDYVKD SLFCSSTYGV CKYTDLNFIE NLNVLFDGRD
NGALEAFRKA RNGVFISTGK LSSLSMIKGP QRADLNGVIV DKVGELNVEF WFAMRKDGDD
VIFSRADSLS PSHYWSPQGN LGGNCAGNAS GNDALARFTI FTQSRVLSTF EPRSDLERDF
IDMEDSLFIA KYGLEDYAFD HIVYGSFNYK VIGGLHLLIG LFRRLKKSNL VIQEFLQYDS
SIHSYFITDQ ECGSSKSVCT VIDLLLDDFV VIVKSLNLNC VSKVVNINVD FKDFQFMLWC
NDNKIMTFYP KMQATSDWKP GYSMPVLYKY LNVPLERVSL WNYGKAINLP TGCMMNVAKY
TQLCQYLNTT TLAVPVNMRV LHLGAGSDKE VAPGSAVLRQ WLPSGSILVD NDLNPFVSDS
LVTYFGDCMT LPFDCHWDLI ISDMYDPLTK NIGDYNVSKD GFFTYICYLI RDKLSLGGSV
AIKITEFSWN ADLYKLMSYF AFWTVFCTNV NASSSEGFLI GINYLGKSCF EIDGNVMHAN
YLFWRNSTTW NGGAYSLFDM SKFSLKLAGT AVVNLRPDQL NDLVYSLIER GKLLVRDTRK
EIFVGDSLVN TC
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