R1A_BC133
ID R1A_BC133 Reviewed; 4441 AA.
AC P0C6F7; Q0Q4F3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 133/2005 (BtCoV) (BtCoV/133/2005).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=389230;
OH NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat) (Vespertilio pachypus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16840328; DOI=10.1128/jvi.00697-06;
RA Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
RA Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
RA Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
RT "Prevalence and genetic diversity of coronaviruses in bats from China.";
RL J. Virol. 80:7481-7490(2006).
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. {ECO:0000269|PubMed:19264783}.
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=P0C6F7-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6W1-1; 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; DQ648794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0C6F7; -.
DR Proteomes; UP000007449; 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; 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; cd21523; SUD_C_MERS-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; 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; IPR044382; NSP3_SUD_C_MERS-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; PF16251; bCoV_NAR; 1.
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..4441
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338062"
FT CHAIN 1..195
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338063"
FT CHAIN 196..847
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338064"
FT CHAIN 848..2791
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338065"
FT CHAIN 2792..3298
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338066"
FT CHAIN 3299..3604
FT /note="3C-like proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338067"
FT CHAIN 3605..3896
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338068"
FT CHAIN 3897..3979
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338069"
FT CHAIN 3980..4178
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338070"
FT CHAIN 4179..4288
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338071"
FT CHAIN 4288..4441
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338073"
FT CHAIN 4289..4427
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338072"
FT TRANSMEM 2152..2172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2229..2249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2333..2353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2357..2377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2382..2402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2807..2827
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3079..3099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3112..3132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3156..3176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3610..3630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3644..3664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3669..3689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3714..3734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3742..3762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3791..3811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3815..3835
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 25..151
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 167..195
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 197..472
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 478..712
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 714..847
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 851..960
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1159..1328
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1329..1453
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1453..1526
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1531..1586
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1600..1871
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1885..2002
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2019..2140
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2686..2789
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3202..3298
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3299..3604
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3897..3979
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3980..4178
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4179..4288
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4289..4427
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1721..1758
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4362..4378
FT /evidence="ECO:0000250"
FT ZN_FING 4404..4417
FT /evidence="ECO:0000250"
FT REGION 339..360
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 1039..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2119..2402
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2807..3176
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3610..3835
FT /note="HD3"
FT /evidence="ECO:0000250"
FT COMPBIAS 1040..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1641
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1807
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3339
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3446
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT SITE 195..196
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 847..848
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 2791..2792
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3298..3299
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3604..3605
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3896..3897
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3979..3980
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4178..4179
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4288..4289
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4427..4428
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
SQ SEQUENCE 4441 AA; 492464 MW; A6E0DB4CDDA40AC7 CRC64;
MLSKAGVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTED MASKLTPWFE DGETAFNQVS
SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS KHFLVNQLAY KDHVGAAMMR
TTLNVKPLGM FFPYDSSLET GEHTFLLRKN GLGGQLFRER PWDRKETPYV EILDDLEADP
TGKYSQNLLK KLIGGDCIPV DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS
DRFIVLNKKL YRVVWNVTRR NVPYSKQTAF TVVSVIQCDD KESVPEHTFT IGSQILMVSP
LKATNNKNFN LKQRLLHTFY GKEAVQQPGY IYHSAYVDCN ACGRGTWCTG NAIQGFACDC
GANYSANDVD LQSSGLVPKN ALFLANCPCA NNGACSHNAA QVYSILDGKA CVEVGGKSFT
LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR IGDAIFTGCT GTWDKVVETA NLFLEKAQHS
LNFCQQFALT EVVLAILSGT TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI
NIGANGVCNA TINAPFIAFT GLGESFKKVA AIPWKICSNL KSALDYYCSN IMFRVFPYDI
PCDVNDFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SNACQTALSS FLNACVAASR
ATAGFISDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ QVLDIMSKAM KLLHTNVSWA
GTKLSAIIYE GREALLFNSG TYFCLSTKAK TLQDQMNLVL PGDYNKKTLG ILDPVPNADT
IDVTANSTVV DVVHGQLEPT NEHGPSMIVG NYVLVSDKLF VRTDDEEFYP LCINGKVVST
LFRLKGGMPS KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN MTFSINPVED
VEEVEEFIED DYLSDELPIA DDEEAWTRAV EEVMPLDDIL VAEIELEEDL PLETALESVE
AEVGESISDE LCVVETAKAQ EPSVESTDST PSTSTVVSEN DLSVKPMSRV AETGDVLEVE
TAVVGGPVSD VTASVVTNDI VSVEQAQQCG VSSLPIQDEA SENQVHQVPD LQCTSETKVE
IVQPRQDLRP RRLRKSKVDL SKYKHTVINN SVTLVLGDAI QIASLLPKCV LVNAANRHLK
HGGGIAGAIN KASGGDVQEE SDEYISNSGP LHVGDSVLLK GYGLADAILR VVGPDARNNE
DAALLKRCYK TFNKHTIVVT PLISSGIFSV DPKVSFEYLL ANVTTTTYVV VNNEDIYNTL
ATPSKPDGLV YSFEGWRGTV RTAKNYGFTC FICTEYSANV KFLRTKGVDT TKKIQTVDGV
SYYLYSARDA LTDVIAAANG CPGICAMPFG YVTHGLDLAQ SGNYVRQVKV PYVCLLASKE
QIPIMNSDVA IQTPETAFIN NVTSNGGYHS WHLVSGDLIV KDVCYKKLLH WSGQTICYAD
NKFYVVKNDV ALPFSDLEAC RAYLTSRAAQ QVNIEVLVTI DGVNFRTVIL NDATTFRKQL
GATFYKGVDI SDALPTVKMG GESLFVADNL SESEEVVLKE YYGTSDVTFL QRYYSLQPLV
QQWKFVVHDG VKSLKLSNYN CYINATIMMI DMLHDIKFVV PALQNAYLRY KGGDPYDFLA
LIMAYGDCTF DNPDDEAKLL HTLLAKAELT VSAKMVWREW CTVCGIRDIE YTGMRACVYA
GVNSMEELQS VFNETCVCGS VKHRQLVEHS TPWLLVSGLN EVKVSTSTDP VYRAFNVFQG
VETSVGHYVH VRVKDGLFYK YDSGSLTKTS DMKCKMTSVW YPKVRYTADC NVVVYDLDGV
TKVEVNPDLS NYYMKDGKYY TSKPTIKYSP ATILPGSVYS NSCLVGVDGT PGSDTISKFF
NDLLGFDETK PISKKLTYSL LPNEDGDVLL SEFNNYNPVY KKGVMLKGKP ILWVNNGVCD
SALNKPNRAS LRQLYDVAPI VLDNKYTVLQ DNTSQLIEPN VPVVEDVSIT TRKLIEVKCK
GLNKPFVKGN FSFVNDPNGV TVVDTLGLTE LRALYVDINT RYIVLRDNNW SSLFKLHTVE
SGDLQIVANG GSVTRRARVL LGASSLFASF AKITVTATTA ACKTAGRSFC KFVVNYGVLQ
NMFLFLKMLF FLPFNYLWPK KQPTVDVGVS GLRTAGVVTT NIVKQCGTAA YYMLLGKFKR
VDWKATLRLF LLLCTTILLL SSIYHLVIFN QVLSSDVMLE DATGILAMYK EVRSYLGIRT
LCDGLAVEYR NTSFDVVDFC SNRSVLCQWC LIGQDSLTRY SALQMLQTHI TSYVLNIDWI
WFALEFFLAY VLYTSSFNVL LLVVTAQYFF AYTSAFVNWR AYNYIVSGLF FLVTHIPLHG
LVRVYNFLAC LWFLRKFYSH VINGCKDTAC LLCYKRNRLT RVEASTIVCG TKRTFYIAAN
GGTSYCCKHN WNCVECDTAG VGNTFICTEV ANDLTTTLRR LIKPTDQSHY YVDSVVVKDA
VVELHYNRDG SSCYERYPLC YFTNLEKLKF KEVCKTPTGI PEHNFLIYDT NDRGQENLAR
SACVYYSQVL CKPMLLVDVN LVTTVGDSRE IAIKMLDSFI NSFISLFSVS RDKLEKLINT
ARDCVRRGDD FQTVLKTFTD AARGHAGVES DVETTMVVDA LQYAHKNDIQ LTTECYNNYV
PGYIKPDSIN TLDLGCLIDL KAASVNQTSM RNANGACVWN SGDYMKLSDS FKRQIRIACR
KCNIPFRLTT SKLRAADNIL SVKFSATKIV GGAPSWLLRV RDLTVKGYCI LTLFVFTVAV
LSWFCLPSYS IATVNFNDDR ILTYKVIENG IVRDIAPNDA CFANKYGHFS KWFNENHGGV
YRNSVDCPIT IAVIAGVAGA RVANVPATLA WVGRQIVLFV SRVFANTNVC FTPTNEIPYD
TFSDSGCVLS SECTLFRDAE GNLNPFCYDP TVLPGASSYA DMKPHVRYDM YDSDMYIKFP
EVIFESTLRI TKTLATQYCR FGSCEESAAG VCISTNGSWA LYNQNYSTRP GIYCGDDYFD
IVRRLAVSLF QPVTYFQLST SLAMGLVLCV FLTAAFYYIN KVKRALADYT QCAVVAVVAA
LLNSLCLCFI VANPLLVAPY TAMYYYATFY LTGEPAFIMH ISWYVMFGTV VPIWMLASYT
VGVMLRHLFW VLAYFSKKHV DVFTDGKLNC SFQDAASNIF VIGKDTYVAL RNAITQDSFV
RYLSLFNKYK YYSGAMDTAS YREACAAHLC KALQTYSETG SDILYQPPNC SVTSSVLQSG
LVKMSAPSGA VENCIVQVTC GSMTLNGLWL DNTVWCPRHI MCPADQLTDP NYDALLISKT
NHSFIVQKHI GAQANLRVVA HSMVGVLLKL TVDVANPSTP AYTFSTVKPG ASFSVLACYN
GKPTGVFTVN LRHNSTIKGS FLCGSCGSVG YTENGGVLNF VYMHQMELSN GTHTGSSFDG
VMYGAFEDKQ THQLQLTDKY CTINVVAWLY AAVLNGCKWF VKPTRVGIVT YNEWALSNQF
TEFVGTQSID MLAHRTGVSV EQMLAAIQSL HAGFQGKTIL GQSTLEDEFT PDDVNMQVMG
VVMQSGVKRI SYGFMHWLMS TLVLAYVSVM QLTKFTMWTY LFETIPTQMT PLLFGFMACV
MFTVKHKHTF LSLFLLPVAL CLTYANIVYE PQTLVSSTLI AVANWLTPTS VYMRTTHLDF
GLYISLSFVL AIIVRRLYRP SMSNLALALC SGVMWFYTYV IGDHSSPITY LMFITTLTSD
YTITVFATVN LAKFISGLVF LYAPHLGFIL PEVKLVLLIY LCLGYMCTMY FGVFSLLNLK
LRVPLGVYDY SVSTQEFRFL TGNGLHAPRN SWEALILNFK LLGIGGTPCI KVATVQSKLT
DLKCTSVVLL TVLQQLHLES NSKAWSYCVK LHNEILAAVD PTEAFERFVC LFATLMSFSA
NVDLDALAND LFENSSVLQA TLTEFSHLAT YAELETAQSS YQKALNSGDA SPQVLKALQK
AVNVAKNAYE KDKAVARKLE RMAEQAMTSM YKQARAEDKK AKIVSAMQTM LFGMIKKLDN
DVLNGVIANA RNGCVPLSIV PLCASNKLRV VIPDISVWNK VVNWPSVSYA GSLWDVTVIN
NVDNEVVKPT DVVETNESLT WPLVIECSRA SSSAVKLQNN EIHPKGLKTM VVTAGIDQVN
CSSSAVAYYE PVQGHRMVMG LLSENAHLKW AKVEGKDGFI NIELQPPCKF LIAGPKGPEI
RYLYFVKNLN NLHRGQLLGH IAATVRLQAG ANTEFASNST VLTLVAFAVD PAKAYLDYVG
SGGTPLSNYV KMLAPKTGTG VAISVKPEAT ADQETYGGAS VCLYCRAHIE HPDVSGVCKY
KTRFVQIPAH VRDPVGFLLK NVPCNVCQYW VGYGCNCDAL RNNTVPQSKD TNFLNESGVL
V
