R1A_BCHK3
ID R1A_BCHK3 Reviewed; 4376 AA.
AC P0C6F8; Q3LZX2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 HKU3 (BtCoV) (SARS-like coronavirus HKU3).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=442736;
OH NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU3-1;
RX PubMed=16169905; DOI=10.1073/pnas.0506735102;
RA Lau S.K.P., Woo P.C.Y., Li K.S.M., Huang Y., Tsoi H.-W., Wong B.H.L.,
RA Wong S.S.Y., Leung S.-Y., Chan K.-H., Yuen K.-Y.;
RT "Severe acute respiratory syndrome coronavirus-like virus in Chinese
RT horseshoe bats.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14040-14045(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=P0C6F8-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6W2-1; 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 HKU3 is highly similar to SARS-CoV
CC (SARS-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; DQ022305; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR BMRB; P0C6F8; -.
DR SMR; P0C6F8; -.
DR Proteomes; UP000007450; 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..4376
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338074"
FT CHAIN 1..179
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338075"
FT CHAIN 180..818
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338076"
FT CHAIN 819..2734
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338077"
FT CHAIN 2735..3234
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338078"
FT CHAIN 3235..3540
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338079"
FT CHAIN 3541..3830
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338080"
FT CHAIN 3831..3913
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338081"
FT CHAIN 3914..4111
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338082"
FT CHAIN 4112..4224
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338083"
FT CHAIN 4225..4363
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338084"
FT CHAIN 4364..4376
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338085"
FT TRANSMEM 2197..2217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2298..2318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2345..2365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2744..2764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2986..3006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3016..3036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3048..3068
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3071..3091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3099..3119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3136..3156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3558..3578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3580..3600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3606..3626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3652..3672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3679..3698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3722..3742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3750..3770
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 998..1164
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1201..1329
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1337..1464
FT /note="Macro 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1466..1532
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1536..1591
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1605..1869
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1882..1992
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2017..2126
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2631..2734
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3136..3234
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3235..3540
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3831..3913
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3914..4111
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4112..4224
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4225..4363
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1723..1760
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4298..4314
FT /evidence="ECO:0000250"
FT ZN_FING 4341..4354
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 2086..2365
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2749..3156
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3558..3770
FT /note="HD3"
FT /evidence="ECO:0000250"
FT ACT_SITE 1645
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1806
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3275
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3379
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 4298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4354
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; by PL-PRO"
FT /evidence="ECO:0000250"
FT SITE 818..819
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3234..3235
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3540..3541
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3830..3831
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3913..3914
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4111..4112
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4224..4225
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4363..4364
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
SQ SEQUENCE 4376 AA; 485585 MW; 338874921B682E15 CRC64;
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT CGLVELEKGV
LPQLEQPYVF IKRSDALSTN HGHKVVELVA ELDGIQFGRS GITLGVLVPH VGETPIAYRN
VLLRKNGNKG AGGHSFGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGAL RELTRELNGG
VVTRYVDNNF CGPDGYPLEC IKDFLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW
FTERSEKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV CEGPTTCGYL
PTNAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG GRTKCFGGCV FSYVGCYNKR
AYWVPRASAN IGANHTGITG ENVETLNEDL LEILNRERVN INIVGDFRFN EEVAIILASF
SASPSAFIET VKGLDYKSFK VIVESCGNYK VTNGKPVTGA WNIGQQRSIL TPLCGFPSQA
AGVIRSIFSR TLDAANHSIL DLQRAAVTTL DGISEQSLRL VDAMVYTSDL LTNSVVVMAY
VTGGLVQQTM QWLSNMLGTA VDKLKPVFTW VEAKLSAGVE FLRDAWEILK FLITGVFDVI
KGQIQVATDN IKECVKIFLG VVNKALEMCL DQVTIAGTKL RALNLGEVFI AQSRGLYRQC
IRGKEQLQLL MPLKAPKEVT FLEGDAHDTV LTSEEVVLKS GELEALETPI DSFTSGAVVG
TPVCINGLML LELENKEQYC ALSPGLLATN NVFRLKGGAP VKGVTFGEDT VLEVQGYKNV
KITFELDVRV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTPMGIDLDE
WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEECEDE EETCEHEYGT EDDYKGLPLE
FGASTETPHV EEEEEEEDWL DDAIEAEPEP EPLPEEPVNQ FVGYLKLTDN VAIKCIDIVK
EAQSAKPTVI VNAANTHLKH GGGVAGALNK ATNGAMQNES DEYIRQNGPL TVGGSCLLSG
HNLAEKCLHV VGPNLNAGED VQLLKRAYEN FNSQDVLLAP LLSAGIFGAK PLQSLKMCVE
IVRTQVYLAV NDKSLYDQIV LDYLDSLKPK VESPNKEEEP KLEEPKAVQP VAEKPVDVKP
KIKACIDEVT TTLEETKFLT NKLLLFADIN GKLYQDSQNM LRGEDMSFLE KDAPYIVGDV
ITSGDITCVI IPAKKSGGTT EMLARALKEV PVAEYITTYP GQGCAGYTLE EAKTALKKCK
SAFYVLPSET PNEKEEVLGT VSWNLREMLA HAEETRKLMP ICLDVRAIMA TIQRKYKGIK
VQEGIVDYGV RFFFYTSKEP VASIITKLNS LNEPLVTMPI GYVTHGLNLE EAARCMRSLK
APAVVSVSSP DAVTAYNGYL TSSSKTPEEY FVETTSLAGS YRDWSYSGQR TELGVEFLKR
GDKIVYHTTG SPIEFHLDGE VLPLDKLKSL LSLREVKTIK VFTTVDNTNL HTHIVDMSMT
YGQQFGPTYL DGADVTKIKP HVNHEGKTFF VLPSDDTLRS EAFEYYHTID ESFLGRYMSA
LNHTKKWKFP QVGGLTSIKW ADNNCYLSSV LLALQQVEVK FNAPALQEAY YRARAGDAAN
FCALILAYSN KTVGELGDVR ETMTHLLQHA NLESAKRVLN VVCKHCGQKT TTLKGVEAVM
YMGTLSYDEL KTGVSIPCVC GRNATQYLVQ QESSFVMMSA PPAEYKLQQG AFLCANEYTG
NYQCGHYTHI TAKETLYRVD GAHLTKMSEY KGPVTDVFYK ETSYTTAIKP VSYKLDGVTY
TEIEPKLDGY YKKGNAYYTE QPIDLVPTQP MPNASFDNFK LTCSNTKFAD DLNQMTGFKK
PASRELTVTF FPDLNGDVVA IDYRHYSTSF KKGAKLVHKP ILWHINQTTN KTTYKPNIWC
LRCLWSTKPV DTSNSFEVLV VEDTQGMDNL ACESQTTTSE EVVENPTVQK EIIECDVKTT
EVVGNVILKP SEEGVKVTQE LGHEDLMAAY VEETSITIKK PNELSLALGL KTLATHGAAA
INSVPWSKIL AYVKPFLGQT AVITSNCIKK CVQRVFSNYM PYVITLLFQL CTFTKSTNSR
IKASLPTTIA KNSVKSVAKL CLDVCINYVK SPKFSKLFTI VMWLLLLSIC LGSLTYVTAV
LGVCLSSLGV PSYCDGVREL YINSSNVTTM DFCQGYFPCS VCLSGLDSLD SYPALETIQV
TISSYKLDLT FLGLAAEWLL AYMLFTKFFY LLGLSAIMQA FFGYFASHFI SNSWLMWFII
SIVQMAPVSA MVRMYIFFAS FYYVWKSYVH IMDGCTSSTC MMCYKRNRAT RVECTTIVNG
VKRSFYVYAN GGRGFCKAHN WNCLNCDTFC AGSTFISDEV ARDLSLQFKR PINPTDQSAY
VVDSVTVKNG ALHLYFDKAG QKTYERHPLS HFVNLDNLRA NNTKGSLPIN VIVFDGKSKC
EESAAKSASV YYSQLMCQPI LLLDQALVSD VGDSTEVSVK MFDAYVDTFS ATFSVPMEKL
KALVATAHSE LAKGVALDGV LSTFVSAARQ GVVDTDVDTK DVIECLKLSH HSDIEVTGDS
CNNFMLTYNK VENMTPRDLG ACIDCNARHI NAQVAKSHNV SLVWNVKDYM SLSEQLRKQI
RSAAKKNNIP FRLTCATTRQ VVNVITTKIS LKGGKVVSTW FKLLLKVTLL CVLAALFCYV
IMPVHSLSVH DGYTNEIIGY KAIQDGVTRD IVSTDDCFAN KHAGFDSWFS QRGGSYRNDK
NCPVVAAIIT REIGFIVPGL PGTVLRALNG DFLHFLPRVF SAVGNICYTP SKLIEYSDFA
TSACVLAAEC TIFKDAMGKP VPYCYDTNLL EGSISYSELR PDTRYVLMDG SIIQFPNTYL
EGSVRVVTTF DAEYCRHGTC ERSEVGVCLS TSGRWVLNNE HYRALPGVFC GVDAMNLIAN
IFTPLVQPVG ALDVSASVVA GGIIAILVTC AAYYFMKFRR AFGEYNHVVA ANALLFLMSF
TILCLAPAYS FLPGVYSIFY LYLTFYFTND VSFLAHLQWF AMFSPIVPFW ITAIYVFCIS
LKHFHWFFSN YLKKRVMFNG VTFSTFEEAA LCTFLLNKEM YLRLRSETLL PLTQYNRYLA
LYNKYKYFSG ALDTTSYREA ACCHLAKALN DFSNSGADVL YQPPQTSITS AVLQSGFRKM
AFPSGKVEGC MVQVTCGTTT LNGLWLDDTV YCPRHVVCTA EDMLNPNYDD LLIRKSNHSF
LVQAGNVQLR VIGHSMQNCL LRLKVDTSNP KTPKYKFVRI QPGQTFSVLA CYNGSPSGVY
QCAMRPNHTI KGSFLNGSCG SVGFNIDYDC VSFCYMHHME LPTGVHAGTD LEGKFYGPFV
DRQTAQAAGT DTTITLNVLA WLYAAVINGD RWFLNRFTTT LNDFNLVAMK YNYEPLTQDH
VDILGPLSAQ TGIAVLDMCA ALKELLQNGM NGRTILGSTI LEDEFTPFDV VRQCSGVTFQ
GKFKKIVKGT HHWMLLTFLT SLLILVQSTQ WSLFFFVYEN AFLPFALGIM AVAACAMLLV
KHKHAFLCLF LLPSLATVAY FNMVYMPASW VMRIMTWLEL ADTSLSGYRL KDCVMYASAL
VLLILMTART VYDDAARRVW TLMNVITLVY KVYYGNSLDQ AISMWALVIS VTSNYSGVVT
TIMFLARAIV FVCVEYYPLL FITGNTLQCI MLVYCFLGYC CCCYFGLFCL LNRYFRLTLG
VYDYLVSTQE FRYMNSQGLL PPKSSIDAFK LNIKLLGIGG KPCIKVATVQ SKMSDVKCTS
VVLLSVLQQL RVESSSKLWA QCVQLHNDIL LAKDTTEAFE KMVSLLSVLL SMQGAVDINK
LCEEMLDNRA TLQAIASEFS SLPSYAAYAT AQEAYEQAVS NGDSEVVLKK LKKSLNVAKS
EFDHDAAMQR KLEKMADQAM TQMYKQARSE DKRAKVTSAM QTMLFTMLRK LDNDALNNII
NNARDGCVPL NIIPLTTAAK LMVVVPDYGT YKNTCDGNTF TYASALWEIQ QVVDADSKIV
QLSEINMDNS PNLAWPLIVT ALRANSAVKL QNNELSPVAL RQMSCAAGTT QTACTDDNAL
AYYNNAKGGR FVLALLSDHQ DLKWARFPKS DGTGTIYTEL EPPCRFVTDT PKGPKVKYLY
FIKGLNNLNR GMVLGSLAAT VRLQAGNATE VPANSTVLSF CAFAVDPAKA YKDYLASGGQ
PITNCVKMLC THTGTGQAIT VTPEANMDQE SFGGASCCLY CRCHIDHPNP KGFCDLKGKY
VQIPTTCAND PVGFTLRNTV CTVCGMWKGY GCSCDQLREP MMQSADASTF LNGFAV
