R1A_BCHK9
ID R1A_BCHK9 Reviewed; 4248 AA.
AC P0C6T6; A3EXG5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 HKU9 (BtCoV) (BtCoV/HKU9).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Nobecovirus.
OX NCBI_TaxID=694006;
OH NCBI_TaxID=9408; Rousettus leschenaultii (Leschenault's rousette).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU9-1;
RX PubMed=17121802; DOI=10.1128/jvi.02182-06;
RA Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA Zheng B.-J., Yuen K.-Y.;
RT "Comparative analysis of twelve genomes of three novel group 2c and group
RT 2d coronaviruses reveals unique group and subgroup features.";
RL J. Virol. 81:1574-1585(2007).
RN [2]
RP FUNCTION OF NSP1.
RX PubMed=19264783; DOI=10.1128/jvi.02485-08;
RA Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K., Makino S.;
RT "Suppression of host gene expression by nsp1 proteins of group 2 bat
RT coronaviruses.";
RL J. Virol. 83:5282-5288(2009).
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.
CC {ECO:0000269|PubMed:19264783}.
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=P0C6T6-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6W5-1; 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: [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; EF065513; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0C6T6; -.
DR Proteomes; UP000006576; 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; cd21518; cv_beta_Nsp2_HKU9-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21537; SUD_C_HKU9_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; 3.40.50.11020; -; 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; IPR044386; NSP2_HKU9-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044352; Nsp3_SUD_C_HKU9_CoV.
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; PF11501; bCoV_NSP1; 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; 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.
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..4248
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338110"
FT CHAIN 1..175
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338111"
FT CHAIN 176..772
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338112"
FT CHAIN 773..2609
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338113"
FT CHAIN 2610..3103
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338114"
FT CHAIN 3104..3409
FT /note="3C-like proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338115"
FT CHAIN 3410..3699
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338116"
FT CHAIN 3700..3782
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338117"
FT CHAIN 3783..3982
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338118"
FT CHAIN 3983..4094
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338119"
FT CHAIN 4094..4248
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338121"
FT CHAIN 4095..4233
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338120"
FT TRANSMEM 2040..2060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2081..2101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2162..2182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2183..2203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2218..2238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2621..2641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2719..2739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2865..2885
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2887..2907
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2916..2936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2946..2966
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2970..2990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3423..3443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3449..3469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3474..3494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3517..3537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3569..3589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3592..3612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3620..3640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 10..131
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 149..175
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 177..431
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 432..644
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 646..772
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 775..885
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 930..1097
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1216..1340
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1345..1417
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1423..1478
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1492..1757
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1770..1870
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 1883..2012
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2507..2609
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3007..3103
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3104..3409
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3700..3782
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3783..3982
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3983..4094
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4095..4233
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1610..1647
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4168..4184
FT /evidence="ECO:0000250"
FT ZN_FING 4211..4224
FT /evidence="ECO:0000250"
FT REGION 312..333
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 1188..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2015..2238
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2621..2990
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3423..3640
FT /note="HD3"
FT /evidence="ECO:0000250"
FT ACT_SITE 1533
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1694
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3144
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3248
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT SITE 175..176
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 772..773
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 2609..2610
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3103..3104
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3409..3410
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3699..3700
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3782..3783
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3982..3983
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4094..4095
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4233..4234
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
SQ SEQUENCE 4248 AA; 468590 MW; C0D0584A862070A7 CRC64;
MEGVPDPPKL KSMVVTTLKW CDPFANPNVT GWDIPIEEAL EYAKQQLRTP EPQLVFVPYY
LSHAPGISGD RVVITDSIWY ATNFGWQPIR ELAMDKDGVR YGRGGTHGVL LPMQDPSFIM
GDIDIQIRKY GIGANSPPDV LPLWDGFSDP GPDVGPYLDF PDNCCPTKPK AKRGGDVYLS
DQYGFDNNGI LVEPVMKLLG VIKSDFTLEQ LLAALGKYRT EDGYDLPDGY VKVAIKVGRK
AVPVLKQSIF TVVGVTEQLV PGYYYPFSTS SVVEHTKPTR GGPVGKTVEA VMLSLYGTNN
YNPATPVARL KCSYCDYYGW TPLKDIGTVN CLCGAEFQLT SSCVDAESAG VIKPGCVMLL
DKSPGMRLIP GNRTYVSFGG AIWSPIGKVN GVTVWVPRAY SIVAGEHSGA VGSGDTVAIN
KELVEYLIEG IRVDADTLDN PTCATFIANL DCDTKAPVVH TVESLQGLCL ANKIMLGDKP
LPTDEFHPFI VGLAYHVQRA CWYGALASRT FEAFRDFVRT EEERFAQFFG KVCAPINGCV
YLAYTTGRVT LFSAYQVLNT AIAKSKDAFG GVAAIVVDML KPILEWVLKK MSIAKGAWLP
YAEGLLALFK AQFTVVKGKF QFLRASLNSK CHSLCDLLTT IMSKLLTSVK WAGCKVDALY
TGTYYYFSRK GVLTEVQLCA KRLGLLLTPK QQKMEVEVLD GDFDAPVTLT DLELEECTGV
LEEVFGASDV KLVKGTLVSL ASKLFVRTED GFLYRYVKSG GVLGKAFRLR GGGVSKVTFG
DEEVHTIPNT VTVNFSYDVC EGLDAILDKV MAPFQVEEGT KLEDLACVVQ KAVYERLSDL
FSDCPAELRP INLEDFLTSE CFVYSKDYEK ILMPEMYFSL EDAVPVDDEM VDDIEDTVEQ
ASDSDDQWLG DEGAEDCDNT IQDVDVATSM TTPCGYTKIA EHVYIKCADI VQEARNYSYA
VLVNAANVNL HHGGGVAGAL NRATNNAMQK ESSEYIKANG SLQPGGHVLL SSHGLASHGI
LHVVGPDKRL GQDLALLDAV YAAYTGFDSV LTPLVSAGIF GFTVEESLCS LVKNVACTTY
VVVYDRQLYE RALATSFDVP GPQSSVQHVP AIDWAEAVEV QESIVDQVET PSLGAVDTVD
SNADSGLNET ARSPENVVGS VPDDVVADVE SCVRDLVRQV VKKVKRDKRP PPIVPQQTVE
QQPQEISSPG DCNTVLVDVV SMSFSAMVNF GKEKGLLIPV VIDYPAFLKV LKRFSPKEGL
FSSNGYEFYG YSRDKPLHEV SKDLNSLGRP LIMIPFGFIV NGQTLAVSAV SMRGLTVPHT
VVVPSESSVP LYRAYFNGVF SGDTTAVQDF VVDILLNGAR DWDVLQTTCT VDRKVYKTIC
KRGNTYLCFD DTNLYAITGD VVLKFATVSK ARAYLETKLC APEPLIKVLT TVDGINYSTV
LVSTAQSYRA QIGTVFCDGH DWSNKNPMPT DEGTHLYKQD NFSSAEVTAI REYYGVDDSN
IIARAMSIRK TVQTWPYTVV DGRVLLAQRD SNCYLNVAIS LLQDIDVSFS TPWVCRAYDA
LKGGNPLPMA EVLIALGKAT PGVSDDAHMV LSAVLNHGTV TARRVMQTVC EHCGVSQMVF
TGTDACTFYG SVVLDDLYAP VSVVCQCGRP AIRYVSEQKS PWLLMSCTPT QVPLDTSGIW
KTAIVFRGPV TAGHYMYAVN GTLISVYDAN TRRRTSDLKL PATDILYGPT SFTSDSKVET
YYLDGVKRTT IDPDFSKYVK RGDYYFTTAP IEVVAAPKLV TSYDGFYLSS CQNPQLAESF
NKAINATKTG PMKLLTMYPN VAGDVVAISD DNVVAHPYGS LHMGKPVLFV TRPNTWKKLV
PLLSTVVVNT PNTYDVLAVD PLPVNNETSE EPISVKAPIP LYGLKATMVL NGTTYVPGNK
GHLLCLKEFT LTDLQTFYVE GVQPFVLLKA SHLSKVLGLR VSDSSLHVNH LSKGVVYAYA
ATRLTTRVTT SLLGGLVTRS VRKTADFVRS TNPGSKCVGL LCLFYQLFMR FWLLVKKPPI
VKVSGIIAYN TGCGVTTCVL NYLRSRCGNI SWSRLLKLLR YMLYIWFVWT CLTICGVWLS
EPYAPSLVTR FKYFLGIVMP CDYVLVNETG TGWLHHLCMA GMDSLDYPAL RMQQHRYGSP
YNYTYILMLL EAFFAYLLYT PALPIVGILA VLHLIVLYLP IPLGNSWLVV FLYYIIRLVP
FTSMLRMYIV IAFLWLCYKG FLHVRYGCNN VACLMCYKKN VAKRIECSTV VNGVKRMFYV
NANGGTHFCT KHNWNCVSCD TYTVDSTFIC RQVALDLSAQ FKRPIIHTDE AYYEVTSVEV
RNGYVYCYFE SDGQRSYERF PMDAFTNVSK LHYSELKGAA PAFNVLVFDA TNRIEENAVK
TAAIYYAQLA CKPILLVDKR MVGVVGDDAT IARAMFEAYA QNYLLKYSIA MDKVKHLYST
ALQQISSGMT VESVLKVFVG STRAEAKDLE SDVDTNDLVS CIRLCHQEGW EWTTDSWNNL
VPTYIKQDTL STLEVGQFMT ANAKYVNANI AKGAAVNLIW RYADFIKLSE SMRRQLKVAA
RKTGLNLLVT TSSLKADVPC MVTPFKIIGG HRRIVSWRRV LIHVFMLLVV LNPQWFTPWY
IMRPIEYNVV DFKVIDNAVI RDITSADQCF ANKFSAFENW YSNRYGSYVN SRGCPMVVGV
VSDIVGSLVP GLPARFLRVG TTLLPLVNYG LGAVGSVCYT PHYAINYDVF DTSACVLAAT
CTLFSSASGE RMPYCADAAL IQNASRYDML KPHVMYPFYE HSGYIRFPEV ISAGVHIVRT
MAMEYCKVGR CDVSEAGLCM SLQPRWVVNN AYFRQQSGVY CGTSAFDLFM NMLLPIFTPV
GAVDITTSIL MGALLAVVVS MSLYYLLRFR RAFGDYSGVI FTNILAFVLN VIVLCLEGPY
PMLPSIYAMV FLYATCYFGS DIACMMHVSF LIMFAGVVPL WVTVLYIVVV LSRHILWFAS
LCTKRTVQVG DLAFHSFQDA ALQTFMLDKE VFLRLKREIS SDAYFKYLAM YNKYKYYSGP
MDTAAYREAA CSHLVMALEK YSNGGGDTIY QPPRCSVASA ALQAGLTRMA HPSGLVEPCL
VKVNYGSMTL NGIWLDNFVI CPRHVMCSRD ELANPDYPRL SMRAANYDFH VSQNGHNIRV
IGHTMEGSLL KLTVDVNNPK TPAYSFIRVS TGQAMSLLAC YDGLPTGVYT CTLRSNGTMR
ASFLCGSCGS PGFVMNGKEV QFCYLHQLEL PNGTHTGTDF SGVFYGPFED KQVPQLAAPD
CTITVNVLAW LYAAVLSGEN WFLTKSSISP AEFNNCAVKY MCQSVTSESL QVLQPLAAKT
GISVERMLSA LKVLLSAGFC GRTIMGSCSL EDEHTPYDIG RQMLGVKLQG KFQSMFRWTL
QWFAIIFVLT ILILLQLAQW TFVGALPFTL LLPLIGFVAV CVGFVSLLIK HKHTYLTVYL
LPVAMVTAYY NFQYTPEGVQ GYLLSLYNYV NPGRIDVIGT DLLTMLIISV ACTLLSVRMV
RTDAYSRIWY VCTAVGWLYN CWTGSADTVA ISYLTFMVSV FTNYTGVACA SLYAAQFMVW
VLKFLDPTIL LLYGRFRCVL VCYLLVGYLC TCYFGVFNLI NRLFRCTLGN YEYVVSSQEL
RYMNSHGLLP PTNSWQALML NIKLAGIGGI PIYRVSTIQS NMTDLKCTSV VLLSVLQQLR
VESSSKLWAL CVKLHNEILA SNSPTEAFEA FVSLLSVLLS LPGAINLDEL CSSILENNSV
LQAVASEFSN LSSYVDYENA QKAYDTAVAT GAPASTVNAL KKAMNVAKSV LDKDVATTRK
LERMSELAMT AMYKQARAED RRSKVTAAMQ TMLFNMIRRL DSDALSNILN NARNGVVPLG
VIPRTAANKL LLVVPDFSVY TATITMPTLT YAGSAWDVMQ VADADGKTVN ATDITRENSV
NLAWPLVVTA QRQQATSPVK LQNNELMPQT VKRMNVVAGV SQTACVTDAV AYYNATKEGR
HVMAILADTD GLAFAKVEKS TGDGFVILEL EPPCKFMVDT PKGPALKYLY FTKGLKNLCR
GTVLGTLACT VRLHAGSATE VASNSSILSL CSFSVDPEAT YKDYLDNGGS PIGNCVKMLT
PHTGTGLAIT AKPDANIDQE SFGGASCCLY CRCHIEHPGA SGVCKYKGKF VQIPLVGVND
PIGFCIRNVV CAVCNMWQGY GCPCSSLREI NLQARDECFL NESGVLVE
