R1A_CVM2
ID R1A_CVM2 Reviewed; 4416 AA.
AC P0C6U9; Q9PYA3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Replicase polyprotein 1a;
DE Short=pp1a;
DE AltName: Full=ORF1a polyprotein;
DE Contains:
DE RecName: Full=Non-structural protein 1;
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=Non-structural protein 3;
DE Short=nsp3;
DE EC=3.4.19.12;
DE EC=3.4.22.69;
DE AltName: Full=PL1-PRO/PL2-PRO;
DE AltName: Full=PL1/PL2;
DE AltName: Full=Papain-like proteinases 1/2;
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;
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=Non-structural protein 9;
DE Short=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=Non-structural protein 11;
DE Short=nsp11;
GN ORFNames=1a;
OS Murine coronavirus (strain 2) (MHV-2) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=76344;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Das Sarma J., Hingley S.T., Lai M.M.C., Weiss S.R., Lavi E.;
RT "Pathogenesis and sequence analysis of mouse hepatitis virus type 2: an
RT experimental model system of acute meningitis and hepatitis in mice.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The papain-like proteinase 1 (PL1-PRO) and papain-like
CC proteinase 2 (PL2-PRO) are responsible for the cleavages located at the
CC N-terminus of the replicase polyprotein. In addition, PLP2 possesses a
CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains from cellular substrates.
CC Antagonizes innate immune induction of type I interferon by blocking
CC the phosphorylation, dimerization and subsequent nuclear translocation
CC of host IRF-3 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [3C-like proteinase]: Responsible for the majority of
CC cleavages as it cleaves the C-terminus of replicase polyprotein at 11
CC sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-
CC [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function
CC (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}.
CC -!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity to the
CC polymerase, maybe by binding to dsRNA or by producing primers utilized
CC by the latter. {ECO:0000250}.
CC -!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
CC -!- FUNCTION: [Non-structural protein 1]: Binds to the 40S ribosomal
CC subunit and inhibits host translation. The nsp1-40S ribosome complex
CC further induces an endonucleolytic cleavage near the 5'UTR of host
CC mRNAs, targeting them for degradation. By suppressing host gene
CC expression, nsp1 facilitates efficient viral gene expression in
CC infected cells and evasion from host immune response (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides
CC corresponding to the two self-cleavage sites of the SARS 3C-like
CC proteinase are the two most reactive peptide substrates. The enzyme
CC exhibits a strong preference for substrates containing Gln at P1
CC position and Leu at P2 position.; EC=3.4.22.69;
CC -!- CATALYTIC ACTIVITY:
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 -!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of nsp7
CC and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is
CC a dimer. Nsp10 forms a dodecamer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: 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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6U9-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6X8-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
CC conventional translation.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
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DR EMBL; AF201929; AAF19383.1; -; Genomic_RNA.
DR SMR; P0C6U9; -.
DR MEROPS; C16.001; -.
DR PRIDE; P0C6U9; -.
DR Proteomes; UP000139707; Genome.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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 virus 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:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; 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; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd21519; cv_beta_Nsp2_MHV-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21524; DPUP_MHV_Nsp3; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
DR Gene3D; 1.10.150.420; -; 1.
DR Gene3D; 1.10.1840.10; -; 1.
DR Gene3D; 1.10.8.1190; -; 2.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.11020; -; 1.
DR InterPro; IPR022570; B-CoV_A_NSP1.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044384; NSP2_MHV-like.
DR InterPro; IPR044381; NSP3_DPUP_MHV.
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; 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; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF16251; bCoV_NAR; 1.
DR Pfam; PF09401; CoV_NSP10; 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; PF11963; DUF3477; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF01831; Peptidase_C16; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; SSF159936; SSF159936; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF53335; SSF53335; 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; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51962; COV_NSP1; 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_Y3; 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; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 2.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus; Decay of host mRNAs by virus;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW 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 IRF3 by virus; Inhibition of host ISG15 by virus;
KW Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Protease;
KW Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
KW Thiol protease; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..4416
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338266"
FT CHAIN 1..247
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338267"
FT CHAIN 248..832
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338268"
FT CHAIN 833..2783
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338269"
FT CHAIN 2784..3279
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338270"
FT CHAIN 3280..3582
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338271"
FT CHAIN 3583..3869
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338272"
FT CHAIN 3870..3961
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338273"
FT CHAIN 3962..4155
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338274"
FT CHAIN 4156..4265
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338275"
FT CHAIN 4266..4402
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338276"
FT CHAIN 4403..4416
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338277"
FT TRANSMEM 2232..2252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2260..2280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2346..2366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2388..2408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2789..2809
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2869..2889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3042..3062
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3064..3084
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3096..3116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3123..3143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3148..3168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3591..3611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3621..3641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3647..3667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3690..3710
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3717..3737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3744..3764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3788..3808
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 54..196
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 217..247
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 251..511
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 518..706
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 726..832
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 834..946
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1031..1268
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1269..1429
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1484..1556
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1555..1610
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1625..1884
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1898..1999
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2053..2202
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2680..2783
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3182..3279
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3280..3582
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3870..3958
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3959..4155
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4156..4265
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4266..4403
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1145..1173
FT /note="C4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 1741..1777
FT /note="C4-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4339..4355
FT /evidence="ECO:0000250"
FT ZN_FING 4381..4394
FT /evidence="ECO:0000250"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..414
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 2232..2408
FT /note="HD1"
FT REGION 2789..3168
FT /note="HD2"
FT REGION 3525..3808
FT /note="HD3"
FT ACT_SITE 1068
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1219
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1663
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1820
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3320
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3424
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT SITE 247..248
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 832..833
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 2783..2784
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 3279..3280
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3582..3583
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3869..3870
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3961..3962
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4155..4156
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4265..4266
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4402..4403
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
SQ SEQUENCE 4416 AA; 491187 MW; 4FD965F1EEC15362 CRC64;
MAKMGKYGLG FKWAPEFPWM LPNASEKLGS PERSEEDGFC PSAAQEPKTK GKTLINHVRV
DCSRLPALEC CVQSAIIRDI FVDEDPLNVE ASTMMALQFG SAVLVKPSKR LSIQAWAKLG
VLPKTPAMGL FKRFCLCNTR ECVCDAHVAF QLFTVQPDGV CLGNGRFIGW FVPVTAIPAY
AKQWLQPWSI LLRKGGNKGS VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSRKAYA
LLKGYRGVKS ILFLDQYGCD YTGRLAKGLE DYGDCTLEEM KELFPVWCDS LDNEVVVAWH
VDRDPRAVMR LQTLATIRSI GYVGQPTEDL VDGDVVVREP AHLLAANAIV KRLPRLVETM
LYTDSSVTEF CYKTKLCDCG FITQFGYVDC CGDACDFRGW VPGNMMDGFL CPGCSKSYMP
WELEAQSSGV IPKGGVLFTQ STDTVNRESF KLYGHAVVPF GSAVYWSPYP GMWLPVIWSS
VKSYADLTYT GVVGCKAIVQ ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN
RGDYSLLLEN VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN
FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT EWFDLAVDTA
ASAAGWLCYQ LVNGLFAVAN GGITFLSDVP ELVKNFVDKF KVFFKVLIDS MSVSVLSGLT
VVKTASNRVC LAGCKVYEVV QKRLSAYVMP VGCNEATCLV GEIEPAVVED DVVDVVKAPL
TYQGCCKPPT SFEKICVVDK LYMAKCGDQF YPVVVDNDTI GVLDQCWRFP CAGKKVEFND
KPKVKEIPST RKIKINFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
KEHDVIGTKV CALLNRLAED YVYLFDEGGE EVIAPKMYCS FSAPDDEDCV AADVVDADEN
QGDDADDSAA LVTDTQEEDG VAKGQVGVAE SDARLDQVEA FDIEKVEDPI LNELSAELNA
PADKTYEDVL AFDAIYSEAL SAFYAVPGDE THFKVCGFYS PAIERTNCWL RSTLIVMQSL
PLEFKDLEMQ KLWLSYKSSY NKEFVDKLVK SVPKSIILPQ GGYVADFAYF FLSQCSFKAY
ANWRCLKCDM DLKLQGLDAM FFYGDVVSHV CKCGTGMTLL SADIPYTLHF GLRDDKFCAF
YTPRKVFRAA CVVDVNDCHS MAVVDGKQID GKVVTKFNGD KYDFMVGHGM AFSMSAFEIA
QLYGSCITPN VCFVKGDVIK VLRRVGAEVI VNPANGRMAH GAGVAGAIAK AAGKSFIKET
ADMVKNQGVC QVGECYESTG GNLCKTVLNI VGPDARGHGK QCYSFLERAY QHINKCDDVV
TTLISAGIFS VPTDVSLTYL IGVVTKNVIL VSNNKDDFDV IEKCQVTSIA GTKALSLQLA
KNLCRDVKFE TNACDSLFSD SCFVSSYDVL QEVELLRHDI QLDDDARVFV QAHMDNLPAD
WRLVNKFDSV DGVRTVKYFE CPGEIFVSSQ GKKFGYVQNG SFKVASVSQI RALLANKVDV
LCTVDGVNFR SCCVAEGEVF GKTLGSVFCD GINVTKVRCS AIHKGKVFFQ YSGLSAADLV
AVTDAFGFDE PQLLKYYNML GMCKWPVVVC GNYFAFKQSN NNCYINVACL MLQHLSLKFH
KWQWQEAWNE FRSGKPLRFV SLVLAKGSFK FNEPSDSTDF MRVVLREADL SGATCDFEFV
CKCGVKQEQR KGVDAVMHFG TLDKGDLAKG YTIACTCGNK LVHCTQLNVP FLICSNKPEG
KKLPDDVVAA NIFTGGSLGH YTHVKCKPKY QLYDACNVSK VSEAKGNFTD CLYLKNLKQT
FSSKLTTFYL DDVKCVEYNP DLSQYYCESG KYYTKPIIKA QFRTFEKVEG VYTNFKLVGH
SIAEKFNAKL GFDCNSPFTE YKITEWPTAT GDVVLASDDL YVSRYSGGCV TFGKPVIWLG
HEEASLKSLT YFNRPSVVCE NKFNVLPVDV SEPTDKGPVP AAVLVTGALS GAATAPGTAK
EQKVCASDSV VDQVVSGFLS DLSGATVDVK EVKLNGVKKP IKVEDSVVVN DPTSETKVVK
SLSIVDVYDM FLTGCRYVVW MANELSRLVN SPTVREYVKW GMTKIVIPAK LVLLRDEKQE
FVAPKVVKAK VIACYSAVKW FFLYCFSWIK FNTDNKVIYT TEVASKLTFN LCCLAFKNAL
QTFNWNVVSR GFFLVATVFL LWFNFLYANV ILSDFYLPNI GFFPTFVGQI VAWVKTTFGI
FTLCDLYQVS DVGYRSSFCN GSMVCELCFS GFDMLDNYDA INVVQHVVDR RVSFDYISLF
KLVVELVIGY SLYTVCFYPL FGLIGMQLLT TWLPEFFMLE TMHWSARFFV FVANMLPAFT
LLRFYIVVTA MYKIFCLCRH VMYGCSRPGC LFCYKRNRSV RVKCSTVVGG TLRYYDVMAN
GGTGFCAKHQ WNCLNCSAFG PGNTFITHEA AADLSKELKR PVNPTDSAYY LVTEVKQVGC
SMRLFYERDG QRVYDDVSAS LFVDMNGLLH SKVKGVPETH VVVVENEADK AGFLNAAVFY
AQSLYRPMLL VEKKLITTAN TGLSVSQTMF DLYVDSLLGV LDVDRKSLTS FVNAAHNSLK
EGVQLEQVMD TFIGCARRKC AIDSDVETKS ITKSIMSAVN AGVDFTDESC NNLVPTYVKS
DTIVAADLGV LIQNNAKHVQ ANVAKAANVA CIWSVDAFNQ LSADLQHRLR KACSKTGLKI
KLTYNKQEAN VPILTTPFSL KGGAVFSKVL QWLFVVNLIC FIVLWALMPT YAVHKSDMQL
PLYASFKVID NGVLRDVTVT DACFANKFIQ FDQWYESTFG LVYYRNSRAC PVVVAVIDQD
IGYTLFNVPT KVLRYGFHVL HFITHAFATD SVQCYTPHMQ IPYDNFYASG CVLSSLCTML
AHADGTPHPY CYTEGIMHNA SLYDSLAPHV RYNLANSNGY IRFPEVVSEG IVRIVRTRSM
TYCRVGLCED AEEGVCFNFN SSWVLNNPYY RAMPGTFCGR NAFDLIHQVL GGLVRPIDFF
ALTASSVAGA ILAIIVVLAF YYLIKLKRAF GDYTSVVVIN VIVWCINFLM LFVFQVYPTL
SCLYACFYFY TTLYFPSEIS VVMHLQWLVM YGAIMPLWFC IIYVAVVVSN HALWLFSYCR
KLGTEVRSDG TFEEMSLTTF MITKESYCKL KNSVSDVAFN RYLSLYNKYR YFSGKMDTAA
YREAACSQLA KAMETFNHNN GNDVLYQPPT ASVTTSFLQS GIVKMVFPTS KVEPCVVSVT
YGNMTLNGLW LDDKVYCPRH VICSSADMTD PDYSNLLCRV ISSDFCVMSG RMSLTVMSYQ
MQGSLLVLTV TLQNPNTPKY SFGVVKPGET FTVLAAYNGK SQGAFHVTMR SSYTIKGSFL
CGSCGSVGYV LTGDSVRFVY MHQLELSTGC HTGTDFSGNF YGPYRDAQVV QLPVQDYTQT
VNVVAWLYAA ILNRCNWFVQ SDSCSLEEFN VWAMTNGFSS IKADLVLDAL ASMTGVTVEQ
ILAAIKRLYS GFQGKQILGS CVLEDELTPS DVYQQLAGVK LQSKRTRVVK GTCCWILAST
LLFCSIISAF VKWTMFMYVT THMLGVTLCA LCFVSFAMLL VKHKHLYLTM FIMPVLCTLF
YTNYLVVYKQ SFRGLAYAWL SHFVPAVDYT YMDEVLYGVV LLVAMVFVTM RSINHDVFSV
MFLVGRLVSL VSMWYFGANL EEEVLLFLTS LFGTYTWTTM LSLATAKVIA KWLAVNVLYF
TDVPQVKLVL LSYLCIGYVC CCYWGVLSLL NSIFRMPLGV YNYKISVQEL RYMNANGLRP
PRNSFEALVL NFKLLGIGGV PVIEVSQIQS RLTDVKCVNV VLLNCLQHLH IASSSKLWQY
CSTLHNEILA TSDLSVAFDK LAQLLVVLFA NPAAVDSKCL ASIEEVSDDY VRDSTVLQAL
QSEFVNMASF VEYELAKKNL DEAKASGSAN QQQIKQLEKA CNIAKSAYER DRAVARKLER
MADLALTNMY KEARINDKKS KVVSALQTML FSMIRKLDNQ ALNSILDNAV KGCVPLNAIP
SLTSNTLTII VPDKQVFDQV VDNVYVTYAG NVWHIQSIQD ADGAVKQLNE IDVNITWPLV
IAANRHNEVS SVVLQNNELM PQKLRTQVVN SGSDMNCNTP TQCYYNTTGM GKIVYAILSD
CDGLKYTKIV KEDGNCVVLE LDPPCKFSVQ DVKGLKIKYL YFVKGCNTLA RGWVVGTLSS
TVRLQAGTAT EYASNSAIRS LCAFSVDPKK TYLDYIQQGG APVTNCVKML CDHAGTGMAI
TIKPEATTNQ DSYGGASVCI YCRSRVEHPD VDGLCKLRGK FVQVPLGIKD PVSYVLTHDV
CQVCGFWRDG SCSCVGTGSQ FQSKDTNFLN GFGVQV
