R1A_CVBLU
ID R1A_CVBLU Reviewed; 4383 AA.
AC P0C6T9; Q8V439;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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 Bovine coronavirus (strain 98TXSF-110-LUN) (BCoV-LUN) (BCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=233264;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11714968; DOI=10.1099/0022-1317-82-12-2927;
RA Chouljenko V.N., Lin X.Q., Storz J., Kousoulas K.G., Gorbalenya A.E.;
RT "Comparison of genomic and predicted amino acid sequences of respiratory
RT and enteric bovine coronaviruses isolated from the same animal with fatal
RT shipping pneumonia.";
RL J. Gen. Virol. 82:2927-2933(2001).
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=P0C6T9-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6W8-1; 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; AF391542; AAL57315.1; -; Genomic_RNA.
DR SMR; P0C6T9; -.
DR Proteomes; UP000008571; 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; cd21557; Macro_X_Nsp3-like; 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; IPR044371; Macro_X_NSP3-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 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 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; Repeat;
KW Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion; Zinc;
KW Zinc-finger.
FT CHAIN 1..4383
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338146"
FT CHAIN 1..246
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338147"
FT CHAIN 247..851
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338148"
FT CHAIN 852..2750
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338149"
FT CHAIN 2751..3246
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338150"
FT CHAIN 3247..3549
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338151"
FT CHAIN 3550..3836
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338152"
FT CHAIN 3837..3925
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338153"
FT CHAIN 3926..4122
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338154"
FT CHAIN 4123..4232
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338155"
FT CHAIN 4233..4369
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338156"
FT CHAIN 4370..4383
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338157"
FT TRANSMEM 2138..2158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2199..2219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2227..2247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2313..2333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2343..2363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2365..2385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2752..2772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2824..2844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3009..3029
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3031..3051
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3063..3083
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3090..3110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3115..3135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3558..3578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3588..3608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3614..3634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3657..3677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3684..3704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3711..3731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3755..3775
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 216..246
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 250..519
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 524..713
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 733..851
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 853..966
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1036..1274
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1275..1435
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1491..1563
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1562..1617
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1631..1892
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1906..2007
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2020..2169
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2647..2750
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3149..3246
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3247..3549
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3837..3925
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3926..4122
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4123..4232
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4233..4370
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1151..1179
FT /note="C4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 1749..1785
FT /note="C4-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4306..4322
FT /evidence="ECO:0000250"
FT ZN_FING 4348..4361
FT /evidence="ECO:0000250"
FT REGION 392..416
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 2138..2385
FT /note="HD1"
FT REGION 2752..3135
FT /note="HD2"
FT REGION 3558..3775
FT /note="HD3"
FT ACT_SITE 1074
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1225
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1671
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1828
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3287
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3391
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4322
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT SITE 246..247
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 851..852
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 2750..2751
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 3246..3247
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3549..3550
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3836..3837
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3925..3926
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4122..4123
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4232..4233
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4369..4370
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
SQ SEQUENCE 4383 AA; 490742 MW; 013D5227DBD36707 CRC64;
MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDIVC STTAQKLETG GICPENHVMV
DCRRLLKQEC CVQSSLIREI VMNTRPYDLE VLLQDALQSR EAVLVTPPLG MSLEACYVRG
CNPNGWTMGL FRRRSVCNTG RCAVNKHVAY QLYMIDPAGV CFGAGQFVGW VIPLAFMPVQ
SRKFIVPWVM YLRKCGEKGA YNKDHKRGGF EHVYNFKVED AYDLVHDEPK GKFSKKAYAL
IRGYRGVKPL LYVDQYGCDY TGGLADGLEA YADKTLQEMK ALFPIWSQEL PFDVTVAWHV
VRDPRYVMRL QSASTIRSVA YVANPTEDLC DGSVVIKEPV HVYADDSIIL RQHNLVDIMS
CFYMEADAVV NAFYGVDLKD CGFVMQFGYI DCEQDLCDFK GWVPGNMIDG FACTTCGHVY
ETGDLLAQSS GVLPVNPVLH TKSAAGYGGF GCKDSFTLYG QTVVYFGGCV YWSPARNIWI
PILKSSVKSY DGLVYTGVVG CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH
KQLLLNRGVY KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA
FCDYADKICH AVVSKSKELL DVSLDSLSAA IHYLNSKIVD LAQHFSDFGT SFVSKIVHFF
KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA SAVAQAFRSV AKVVLDSLRV
TFIDGLSCFK IGRRRICLSG SKIYEVERGL LHSSQLPLDV YDLTMPSQVQ KAKQKPIYLK
GSGSDFSLAD SVVEVVTTSL TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDGHVG
LLDQAWRVPC AGRRVTFKEQ PTVNEIASTP KTIKVFYELD KDFNTILNTA CGVFEVDDTV
DMEEFYAVVV DAIEEKLSPC KELEGVGAKV SAFLQKLEDN SLFLFDEAGE EVLASKLYCA
FTAPEDDDFL EESGVEEDDV EGEETDLTVT SAGEPCVASE QEESSEILED TLDDGPCVET
SDSQVEEDVE MSDFADLESV IQDYENVCFE FYTTEPEFVK VLDLYVPKAT RNNCWLRSVL
AVMQKLPCQF KDKNLQDLWV LYKQQYSQLF VDTLVNKIPA NIVVPQGGYV ADFAYWFLTL
CDWQCVAYWK CIKCDLALKL KGLDAMFFYG DVVSHVCKCG ESMVLIDVDV PFTAHFALKD
KLFCAFITKR SVYKAACVVD VNDSHSMAVV DGKQIDDHRV TSITSDKFDF IIGHGMSFSM
TTFEIAQLYG SCITPNVCFV KGDIIKVSKR VKAEVVVNPA NGHMAHGGGV AKAIAVAAGQ
QFVKETTDMV KSKGVCATGD CYVSTGGKLC KTVLNVVGPD ARTQGKQSYA LLERVYKHLN
KYDCVVTTLI SAGIFSVPSD VSLTYLLGTA EKQVVLVSNN QEDFDLISKC QITAVEGTKK
LAERLSFNVG RSIVYETDAN KLILSNDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN
VDVVPEGWRV VNKFYQINGV RTVKYFECPG GIDICSQDKV FGYVQQGSFN KATVAQIKAL
FLDKVDILLT VDGVNFTNRF VPVGENFGKS LGNVFCDGVN VTKHKCDINY KGKVFFQFDN
LSSEDLKAVR SSFNFDQKEL LAYYNMLVNC SKWQVVFNGK YFTFKQANNN CFVNVSCLML
QSLNLKFKIV QWQEAWLEFR SGRPARFVSL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG
AICDFEIACK CGVKQEQRTG VDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL
ICSNTPASVK LPKGVGSANI FKGDKVGHYV HVKCEQSYQL YDASNVKKVT DVTGNLSDCL
YLKNLKQTFK SVLTTYYLDD VKKIEYKPDL SQYYCDGGKY YTQRIIKAQF KTFEKVDGVY
TNFKLIGHTI CDILNAKLGF DSSKEFVEYK VTEWPTATGD VVLATDDLYV KRYERGCITF
GKPVIWLSHE QASLNSLTYF NRPLLVDENK FDVLKVDDVD DGGDISESDA KESKEINIIK
LSGVKKPFKV EDSVIVNDDT SEIKYVKSLS IVDVYDMWLT GCRYVVRTAN DLSMAVNVPT
IRKFIKFGMT LVSIPIDLLN LREIKPVFNV VKAVRNKISA CFNFIKWLFV LLFGWIKISA
DNKVIYTTEV ASKLTCKLVA LAFKNAFLTF KWSVVARGAC IIATIFLLWF NFIYANVIFS
DFYLPKIGFL PTFVGKIAQW IKSTFSLVTI CDLYSIQDVG FKNQYCNGSI ACQFCLAGFD
MLDNYKAIDV VQYEADRRAF VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL
PELFMLSTLH WSVRLLVSLA NMLPAHVFMR FYIIIASFIK LFSLFRHVAY GCSKPGCLFC
YKRNRSLRVK CSTIVGGMIR YYDVMANGGT GFCSKHQWNC IDCDSYKPGN TFITVEAALD
LSKELKRPIQ PTDVAYHTVT DVKQVGCYMR LFYERDGQRT YDDVNASLFV DYSNLLHSKV
KGVPNMHVVV VENDADKANF LNAAVFYAQS LFRPILMVDK NLITTANTGT SVTETMFDVY
VDTFLSMFDV DKKSLNALIA TAHSSIKQGT QICKVLDTFL SCARKSCSID SDVDTKCLAD
SVMSAVSAGL ELTDESCNNL VPTYLKGDNI VAADLGVLIQ NSAKHVQGNV AKIAGVSCIW
SVDAFNQLSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG AVFSYFVYVC
FLLSLVCFIG LWCLMPTYTV HKSDFQLPVY TSYKVLDNGV IRDVSVEDVC FANKFEQFDQ
WYESTFGLSY YSNSMACPIV VAVVDQDLGS TVFNVPTKVL RYGYHVLHFI THALSADGVQ
CYTPHSQISY SNFYASGCVL SSACTMFAMA DGSPQPYCYT EGLMQNASLY SSLVPHVRYN
LANAKGFIRF PEVLREGLVR IVRTRSMSYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL
PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL IKLKRAFGDY
TSIVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYATL YFPSEISVIM HLQWLVMYGT
IMPLWFCLLY ISVVVSNHAF WVFAYCRRLG TSVRSDGTFE EMALTTFMIT KDSYCKLKNS
LSDVAFNRYL SLYNKYRYYS GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV
STSFLQSGIV KMVNPTSKVE PCIVSVTYGN MTLNGLWLDD KVYCPRHVIC SASDMTNPDY
TNLLCRVTSS DFTVLFDRLS LTVMSYQMQG CMLVLTVTLQ NSRTPKYTFG VVKPGETFTV
LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVGYVLMG DCVKFVYMHQ LELSTGCHTG
TDFNGDFYGP YKDAQVVQLP VQDYIQSVNF VAWLYAAILN NCNWFVQSDK CSVEDFNVWA
LSNGFSQVKS DLVIDALASM TGVSLETLLA AIKRLKNGFQ GRQIMGSCSF EDELTPSDVY
QQLAGIKLQS KRTRLVKGIV CWIMASTFLF SCIITAFVKW TMFMYVTTNM LSITFCALCV
ISLAMLLVKH KHLYLTMYII PVLFTLLYNN YLVVYKQTFR GYVYAWLSYY VPSVEYTYTD
EVIYGMLLLI GMVFVTLRSI NHDLFSFIMF VGRVISVVSL WYMGSNLEEE ILLMLASLFG
TYTWTTALSM AAAKVIAKWV AVNVLYFTDI PQIKIVLVCY LFIGYIISCY WGLFSLMNSL
FRMPLGVYNY KISVQELRYM NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT
DVKCANVVLL NCLQHLHVAS NSKLWQYCST LHNEILATSD LGVAFEKLAQ LLIVLFANPA
AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA RSSGSANQQQ
LKQLEKACNI AKSAYERDRA VARKLERMAD LALTNMYKEA RINDKKSKVV SALQTMLFSM
VRKLDNQALN SILDNAVKGC VPLNAIPSLA ANTLTIIVPD KSVYDQVVDN VYVTYAGNVW
QIQTIQDSDG TNKQLNEISD DCNWPLVIIA NRHNEVSATV LQNNELMPAK LKTQVVNSGP
DQTCNTPTQC YYNNSNNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDVK
GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA FSVDPKKTYL
DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTNQDSY GGASVCIYCR ARVEHPDVDG
LCKLRGKFVQ VPVGIKDPVS YVLTHDVCQV CGFWRDGSCS CVSTDTTVQS KDTNFLNGFG
VRV
