R1A_BCRP3
ID R1A_BCRP3 Reviewed; 4380 AA.
AC P0C6T7; Q3I5J6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Leader protein;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p65 homolog;
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=PL2-PRO;
DE AltName: Full=Papain-like proteinase;
DE Short=PL-PRO;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE Contains:
DE RecName: Full=3C-like proteinase;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.-;
DE AltName: Full=nsp5;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE Contains:
DE RecName: Full=Non-structural protein 11;
DE Short=nsp11;
GN ORFNames=1a;
OS Bat coronavirus Rp3/2004 (BtCoV/Rp3/2004) (SARS-like coronavirus Rp3).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=349344;
OH NCBI_TaxID=59479; Rhinolophus ferrumequinum (Greater horseshoe bat).
OH NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
OH NCBI_TaxID=188571; Rhinolophus pearsonii.
OH NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16195424; DOI=10.1126/science.1118391;
RA Li W., Shi Z., Yu M., Ren W., Smith C., Epstein J.H., Wang H., Crameri G.,
RA Hu Z., Zhang H., Zhang J., McEachern J., Field H., Daszak P., Eaton B.T.,
RA Zhang S., Wang L.F.;
RT "Bats are natural reservoirs of SARS-like coronaviruses.";
RL Science 310:676-679(2005).
CC -!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for the
CC cleavages located at the N-terminus of replicase polyprotein. In
CC addition, PL-PRO possesses a deubiquitinating/deISGylating activity and
CC processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
CC cellular substrates. Antagonizes innate immune induction of type I
CC interferon by blocking the phosphorylation, dimerization and subsequent
CC nuclear translocation 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=P0C6T7-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6W6-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Bat coronavirus rp3 is highly similar to SARS-CoV (SARS-
CC like).
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; DQ071615; AAZ67050.1; -; Genomic_RNA.
DR BMRB; P0C6T7; -.
DR SMR; P0C6T7; -.
DR PRIDE; P0C6T7; -.
DR Proteomes; UP000006570; 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:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; 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; cd21516; cv_beta_Nsp2_SARS-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21562; Macro_cv_SUD-N_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21525; SUD_C_SARS-CoV_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; -; 1.
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; 3.40.220.20; -; 1.
DR Gene3D; 3.40.220.30; -; 1.
DR Gene3D; 3.40.30.150; -; 1.
DR Gene3D; 3.40.50.11020; -; 1.
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; IPR021590; NSP1_bCoV.
DR InterPro; IPR038030; NSP1_sf_bCoV.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044389; NSP2_SARS-CoV-like.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR024358; NSP3_N_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR038166; NSP3_PL2pro_sf_bCoV.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044864; NSP3_SUD-N_bCoV.
DR InterPro; IPR044374; NSP3_SUD-N_SARS-CoV.
DR InterPro; IPR043478; NSP3_SUD-N_sf_bCoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044367; NSP6_betaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; 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; PF11501; bCoV_NSP1; 1.
DR Pfam; PF12379; bCoV_NSP3_N; 1.
DR Pfam; PF12124; bCoV_SUD_C; 1.
DR Pfam; PF11633; bCoV_SUD_M; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF19212; CoV_NSP2_C; 1.
DR Pfam; PF19211; CoV_NSP2_N; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 1.
DR Pfam; PF01661; Macro; 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; SSF160099; SSF160099; 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; PS51941; BCOV_NSP3C_M; 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; 1.
DR PROSITE; PS51940; SARS_NSP3C_N; 1.
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..4380
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338122"
FT CHAIN 1..179
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338123"
FT CHAIN 180..818
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338124"
FT CHAIN 819..2738
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338125"
FT CHAIN 2739..3238
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338126"
FT CHAIN 3239..3544
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338127"
FT CHAIN 3545..3834
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338128"
FT CHAIN 3835..3917
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338129"
FT CHAIN 3918..4115
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338130"
FT CHAIN 4116..4228
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338131"
FT CHAIN 4229..4367
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338132"
FT CHAIN 4368..4380
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338133"
FT TRANSMEM 2201..2221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2312..2334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2349..2369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2753..2773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3020..3040
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3059..3079
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3081..3101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3103..3123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3140..3160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3562..3582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3584..3604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3610..3630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3657..3676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3683..3702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3726..3746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3754..3774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 12..127
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 148..179
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 183..456
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 458..688
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 690..818
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 822..930
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1001..1167
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1205..1333
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1341..1468
FT /note="Macro 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1470..1536
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1540..1595
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1609..1873
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1886..1996
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2021..2130
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2635..2738
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3140..3238
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3239..3544
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3835..3917
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3918..4115
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4116..4228
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4229..4367
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1727..1764
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4302..4318
FT /evidence="ECO:0000250"
FT ZN_FING 4345..4358
FT /evidence="ECO:0000250"
FT REGION 200..236
FT /note="C2H2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 323..344
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 370..416
FT /note="C2HC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 2201..2369
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2753..3160
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3562..3774
FT /note="HD3"
FT /evidence="ECO:0000250"
FT ACT_SITE 1649
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1810
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3279
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3383
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 4356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT SITE 179..180
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 818..819
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3238..3239
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3544..3545
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3834..3835
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3917..3918
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4115..4116
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4228..4229
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4367..4368
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
SQ SEQUENCE 4380 AA; 486337 MW; 0DDA57CD3DF1535B CRC64;
MESLVLGINE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKSGT CGIVELEKGV
LPQPEQPYVF IKRSDAQGTD HGHRVRELVA ELDGVQYGRS GITLGVLVPH VGETPIAYRN
VLLRKNGNKG AGGHSFGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGVL RELTRELNGG
ALTRYVDNNF CGPDGYPLEC IKDLLARAGK SMCTLSEQLD YIESKRGVYC CRDHGHEIAW
FTERSDKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV SEGPNTCGYL
PTNAVVKMPC PACQDPEIGP EHSAADYHNH SNIETRLRKG GRTRCFGGCV FAYVGCYNKR
AYWVPRASAD IGSGHTGITG DNVETLNEDL LEILSRERVN INIVGDFQLN EEVAIILASF
SASTSAFIDT IKSLDYKSFK TIVESCGNYK VTKGKPIKGA WNIGQHRSVL TPLCGFPSQA
AGVIRSIFSR TLDAANHSIP DLQRAAVTIL DSISEQSLRL VDAMVYTSNL LTNSVIIMAY
VTGGLVQQTS QWLSNLLDTT VEKLRPIFAW IEAKLSAGVE FLKDAWEILK FLITGVFDIV
KGQIQVASDN IKDCVKCFVD VVNKALEMCI DQVTIAGAKL RSLNLGEVFI AQSKGLYRQC
IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV LTSEEVVLKN GELEALETPV DSFTNGAVVG
TPVCINGLML LEIKANEQYC ALSPGLLATN NVFRLKGGAP TKGVTFGEDT VVEVQGYKNV
RITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
WSVATFYLFD DSGEEKLSSR MYCSFYPPDE EEDCEEYEEE EEVSERTCEH EYGTEEDYKG
LPLEFGASTD IIQVEEQEEE DWLDDAVEAE PEPEPLHEEP VNQLTGYLKL TDNVAIKCVD
IVEEAQNANP MVIVNAANIH LKHGGGVAGA LNKATNGAMQ KESDHYIKLN GPLTVGGSCL
LSGHNLAKKC LHVVGPNLNA GEDIQLLKAA YENFNSQDIL LAPLLSAGIF GAKPLQSLQM
CVQTVRTQVY IVVNDKVLYE QVVMDYLDSL KPKVEAPKQE VLPKAEYPKV DEKSVVQKTI
DVKPKIKACI DEVTTTLEET KFLTNKLLLF TDINGKLYQD SKNMLRGEDM SFLEKDAPYM
VGDVITSGDI TCVVIPSKKA GGTTEMLSRA LKKVPINEYI TTYPGQGCAG YTLEEAKTAL
KKCKSAFYVL PSETPNAKEE ILGTVSWNLR EMLAHAEETR KLMPVCMDVR AIMATIQRKY
KGIKIQEGIV DYGVRFFFYT SKEPVASIIT KLNSLNEPLV TMPIGYVTHG FNLEEAARCM
RSLKAPAIVS VSSPDAVTTY NGYLTSSSKT SEDHFVETVS LAGSYRDWSY SGQRTELGVE
FLKRGEKIVY HTLESPVKFH LDGEVLPLDK LKSLLSLREV KTIKVFTTVD NTNLHTQLVD
MSMTYGQQLG PTYLEGADVT KIKPHVNHEG KTFFVLPSDD TLRSEAFEYY HTLDESFLGR
YMSALNHTKK WKFPQVGGLT SIKWADNNCY LSSVLLALQQ IEVKFNAPAL QEAYYRARAG
DAANFCALIL AYSNKTVGEL GDVRETMTHL LQHANLESAK RVLNVVCKHC GQKTTTLTGV
EAVMYMGTLS YDNLKMGVSI PCVCGRDATQ YLVQQESSFV MMSAPPAEYK LQQGTFLCAN
EYTGNYQCGH YTHITAKETL YRIDGAHLTK MSEYKGPVTD VFYKETSYTT TIKPVSYKLD
GVTYTEIEPK LDGYYKKDNA YYTEQPIDLI PTQPLPNASF DNFKLTCSNT KFADDLNQMT
GFTKPASREL SVTFFPDLNG DVVAIDYRHY SASFKKGAKL LHKPIVWHIN QATTKTTFKP
NTWCLRCLWS TKPVDTSNSF EVLAVEDTQG MDNLACESQQ PTPEEVVENP TIQKEVIECD
VKTTEVVGNV ILKPSDEGVK VTQELDHEDL MAAYVENTSI TIKKPNELSL ALGLKTIATH
GIAAINSVPW GKILAYVKPF LGQAAVTTSN CAKRLVQRMF NNYMPYVLTL LFQLCTFTKS
TNSRIRASLP TTIAKNSVRG IVRLCLDAGI NYVKSPKFSK LFTIAMWLLL LSICLGSLIY
VTAALGVLLS NFGAPSYCSG VRESYLNSSN VTTMDFCEGS FPCSVCLSGL DSLDSYPALE
TIQVTISSYK LDLTILGLAA EWFFAYMLFT KFFYLLGLSA IMQVFFGYFA SHFISNSWLM
WFIISIVQMA PVSAMVRMYI FFASFYYIWK SYVHIMDGCT SSTCMMCYKR NRATRVECTT
IVNGMKRSFY VYANGGRGFC KTHNWNCLNC DTFCAGSTFI SDEVARDLSL QFKRPINPTD
QSSYVVDSVA VKNGALHLYF DKAGQKTYER HPLSHFVNLD NLRANNTKGS LPINVIVFDG
KSKCDESAAK SASVYYSQLM CQPILLLDQA LVSDVGDSTE VSVKMFDAYV DTFSATFSVP
MEKLKALVAT AHSELAKGVA LDGVLSTFVS ASRQGVVDTD VDTKDVIECL KLSHHSDLEV
TGDSCNNFML TYNKVENMTP RDLGACIDCN ARHINAQVAR SHNVSLIWNV KDYMSLSEQL
RKQIRSAAKK NNIPFRLTCA TTRQVVNVIT TKISLKGGKI VSTWFKIMLK ATLLCVLAAL
VCYIVMPVHI LSVHGGYTNE IIGYKAIQDG VTRDIVSTDD CFANKHAGFD SWFSQRGGSY
KNDKSCPVVA AIITREIGFI VPGLPGTVLR AINGDFLHFL PRVFSAVGNI CYTPSKLIEY
SDFSTSACVL AAECTIFKDA MGKPVPYCYD TNLLEGSISY SELRPDTRYV LMDGSIIQFP
NAYLEGSVRV VTTFDAEYCR HGTCERSEAG ICLSTSGRWV LNNEHYRALP GVFCGVDAMN
LIANIFTPLV QPVGALDVSA SVVAGGIIAI LVTCAAYYFM KFRRAFGEYN HVVAANAPLF
LMSFTILCLA PAYSFLPGVY SVFYLYLTFY FTNDVSFLAH LQWFAMFSPI VPFWITAIYV
FCISLKHFHW FFNNYLRKRV VFNGVTFSTF EEAALCTFLL NKEMYLKLRS ETLLPLTQYN
RYLALYNKYK YFSGALDTTS YREAACCHLA KALNDFSNSG ADVLYQPPQT SITSAVLQSG
FRKMAFPSGK VEGCMVQVTC GTTTLNGLWL DDTVYCPRHV ICTAEDMLNP NYEDLLIRKS
NHSFLVQAGN VQLRVIGHSM QNCLLRLKVD TSNPKTPKYK FVRIQPGQTF SVLACYNGSP
SGVYQCAMRP NHTIKGSFLN GSCGSVGFNI DYDCVSFCYM HHMELPTEVH AGTDLEGKFY
GPFVDRQTAQ AAGTDTTITL NVLAWLYAAV INGDRWFLNR FTTTLNDFNL VAMKYNYEPL
TQDHVDILGP LSAQTGIAVL DMCAALKELL QNGMNGRTIL GSTILEDEFT PFDVVRQCSG
VTFQGKFKRI VKGTHHWMLL TFLTSLLILV QSTQWSLFFF VYENAFLPFT LGIMAVAACA
MLLVKHKHAF LCLFLLPSLA TVAYFNMVYM PASWVMRIMT WLELADTSLS GYRLKDCVMY
ASALVLLVLM TARTVYDDAA RRVWTLMNVI TLVYKVYYGN ALDQAISMWA LVISVTSNYS
GVVTTIMFLA RAIVFVCVEY YPLLFITGNT LQCIMLVYCF LGYCCCCYFG LFCLLNRYFR
LTLGVYDYLV STQEFRYMNS QGLLPPKSSI DAFKLNIKLL GIGGKPCIKV ATVQSKMSDV
KCTSVVLLSV LQQLRVESSS KLWAQCVQLH NDILLAKDTT EAFEKMVSLL SVLLSMQGAV
DINKLCEEML DNRATLQAIA SEFSSLPSYA AYATAQEAYE QAVANGDSEV VLKKLKKSLN
VAKSEFDRNA AMQRKLEKMA DQAMTQMYKQ ARSEDKRAKV TSAMQTMLFT MLRKLDNDAL
NNIINNARDG CVPLNIIPLT TAAKLMVVVP DYGTYKNTCD GNTFTYASAL WEIQQVVDAD
SKIVQLSEIN MENSSNLAWP LIVTALRANS AVKLQNNELS PVALRQMSCA AGTTQTACTD
DNALAYYNNS KGGRFVLALL SDHQDLKWAR FPKSDGTGTI YTELEPPCRF VTDTPKGPKV
KYLHFIKGLN NLNRGMVLGS LAATVRLQAG NATEVPANST VLSFCAFAVD PAKAYKDYLA
SGGQPITNCV KMLCTHTGTG QAITVTPEAN MDQESFGGAS CCLYCRCHID HPNPKGFCDL
KGKYVQIPTT CANDPVGFTL RNTVCTVCGM WKGYGCSCDQ LREPMMQSAD ASTFLNGFAV
