R1A_BCHK4
ID R1A_BCHK4 Reviewed; 4434 AA.
AC P0C6T4; A3EX93;
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 HKU4 (BtCoV) (BtCoV/HKU4/2004).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=694007;
OH NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat) (Vespertilio pachypus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU4-1;
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).
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=P0C6T4-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6W3-1; 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; EF065505; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PDB; 2YNA; X-ray; 1.50 A; A/B=3292-3597.
DR PDB; 2YNB; X-ray; 1.96 A; A/B=3292-3597.
DR PDBsum; 2YNA; -.
DR PDBsum; 2YNB; -.
DR SMR; P0C6T4; -.
DR PRIDE; P0C6T4; -.
DR SABIO-RK; P0C6T4; -.
DR Proteomes; UP000006574; 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 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus;
KW 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..4434
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338086"
FT CHAIN 1..195
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338087"
FT CHAIN 196..847
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338088"
FT CHAIN 848..2784
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338089"
FT CHAIN 2785..3291
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338090"
FT CHAIN 3292..3597
FT /note="3C-like proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338091"
FT CHAIN 3598..3889
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338092"
FT CHAIN 3890..3972
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338093"
FT CHAIN 3973..4171
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338094"
FT CHAIN 4172..4281
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338095"
FT CHAIN 4281..4434
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338097"
FT CHAIN 4282..4420
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338096"
FT TRANSMEM 2145..2165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2222..2242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2326..2346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2350..2370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2375..2395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2800..2820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3072..3092
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3105..3125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3149..3169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3603..3623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3637..3657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3662..3682
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3707..3727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3735..3755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3784..3804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3808..3828
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 1152..1321
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1322..1446
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1446..1519
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1524..1579
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1593..1864
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1878..1995
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2012..2133
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2679..2782
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3195..3291
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3292..3597
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3890..3972
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3973..4171
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4172..4281
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4282..4420
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1714..1751
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4355..4371
FT /evidence="ECO:0000250"
FT ZN_FING 4397..4410
FT /evidence="ECO:0000250"
FT REGION 339..360
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 2112..2395
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2800..3169
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3603..3828
FT /note="HD3"
FT /evidence="ECO:0000250"
FT ACT_SITE 1634
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1800
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3332
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3439
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 4355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4364
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 4397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4410
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 2784..2785
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3291..3292
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3597..3598
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3889..3890
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3972..3973
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4171..4172
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4281..4282
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4420..4421
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT HELIX 3302..3305
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3308..3313
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3316..3323
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3326..3330
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3331..3334
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3337..3339
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3345..3350
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3354..3356
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3358..3360
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3363..3365
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3367..3369
FT /evidence="ECO:0007829|PDB:2YNB"
FT STRAND 3371..3377
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3380..3387
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3394..3397
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3405..3412
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3415..3423
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3442..3447
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3450..3462
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3465..3469
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3476..3478
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3481..3484
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3495..3507
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3521..3530
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3540..3549
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3553..3565
FT /evidence="ECO:0007829|PDB:2YNA"
FT STRAND 3575..3577
FT /evidence="ECO:0007829|PDB:2YNA"
FT HELIX 3584..3591
FT /evidence="ECO:0007829|PDB:2YNA"
SQ SEQUENCE 4434 AA; 491823 MW; 942E92FE623EFBCD CRC64;
MLSKASVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTDD MACKLTPWFE DGETAFNQVS
SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS KHFLVNQLAY KDQVGAAMMR
TTLNAKPLGM FFPYDSSLET GEYTFLLRKN GLGGQLFRER PWDRKETPYV EILDDLEADP
TGKYSQNLLK KLIGGDCIPI DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS
DRFIVLNKKL YRVVWNVTRR NVPYPKQTAF TIVSVVQCDD KDSVPEHTFT IGSQILMVSP
LKATNNKNFN LKQRLLYTFY GKDAVQQPGY IYHSAYVDCN ACGRGTWCTG NAIQGFACDC
GANYSANDVD LQSSGLVPRN ALFLANCPCA NNGACSHSAA QVYNILDGKA CVEVGGKSFT
LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR IGDAIFTGCT GTWDKVVETA NLFLEKAQRS
LNFCQQFALT EVVLAILSGT TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI
NIGANGVCNA TINAPFIAFT GLGESFKKVS AIPWKICSNL KSALDYYSSN IMFRVFPYDI
PCDVSNFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SSACQTALSS FLNACVAASR
ATAGFINDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ QVLDIMSKAM KLLHTNVSWA
GTKLSAIIYE GREALLFNSG TYFCLSTKAK TLQGQMNLVL PGDYNKKTLG ILDPVPNADT
IDVNANSTVV DVVHGQLEPT NEHGPSMIVG NYVLVSDKLF VRTEDEEFYP LCTNGKVVST
LFRLKGGMPS KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN MTFSINPVED
VEEVEEFIED DYLSDELPIA DDEEAWARAV EEVMPLDDIL VAEIELEEDP PLETALESVE
AEVVETAEAQ EPSVESIDST PSTSTVVGEN DLSVKPMSRV AETDDVLELE TAVVGGPVSD
VTAIVTNDIV SVEQAQQCGV SSLPIQDEAS ENQVHQVSDL QGNELLCSET KVEIVQPRQD
LKPRRSRKSK VDLSKYKHTV INNSVTLVLG DAIQIASLLP KCILVNAANR HLKHGGGIAG
VINKASGGDV QEESDEYISN NGPLHVGDSV LLKGHGLADA ILHVVGPDAR NNEDAALLKR
CYKAFNKHTI VVTPLISAGI FSVDPKVSFE YLLANVTTTT YVVVNNEDIY NTLATPSKPD
GLVYSFEGWR GTVRTAKNYG FTCFICTEYS ANVKFLRTKG VDTTKKIQTV DGVSYYLYSA
RDALTDVIAA ANGCSGICAM PFGYVTHGLD LAQSGNYVRQ VKVPYVCLLA SKEQIPIMNS
DVAIQTPETA FINNVTSNGG YHSWHLVSGD LIVKDVCYKK LLHWSGQTIC YADNKFYVVK
NDVALPFSDL EACRAYLTSR AAQQVNIEVL VTIDGVNFRT VILNDTTTFR KQLGATFYKG
VDISDAFPTV KMGGESLFVA DNLSESEKVV LKEYYGTSDV TFLQRYYSLQ PLVQQWKFVV
HDGVKSLKLS NYNCYINATI MMIDMLHDIK FVVPALQNAY LRYKGGDPYD FLALIMAYGD
CTFDNPDDEA KLLHTLLAKA ELTVSAKMVW REWCTVCGIR DIEYTGMRAC VYAGVNSMEE
LQSVFNETCV CGSVKHRQLV EHSAPWLLVS GLNEVKVSTS TDPIYRAFNV FQGVETSVGH
YVHIRVKDGL FYKYDSGSLT KTSDMKCKMT SVWYPTVRYT ADCNVVVYDL DGVTKVEVNP
DLSNYYMKDG KYYTSKPTIK YSPATILPGS VYSNSCLVGV DGTPGSDTIS KFFNDLLGFD
ETKPISKKLT YSLLPNEDGD VLLSEFSNYN PVYKKGVMLK GKPILWVNNG VCDSALNKPN
RASLRQLYDV APIVLDNKYT VLQDNTSQLV EHNVPVVDDV PITTRKLIEV KCKGLNKPFV
KGNFSFVNDP NGVTVVDTLG LTELRALYVD INTRYIVLRD NNWSSLFKLH TVESGDLQIV
AAGGSVTRRA RVLLGASSLF ASFAKITVTA TTAACKTAGR GFCKFVVNYG VLQNMFVFLK
MLFFLPFNYL WPKKQPTVDI GVSGLRTAGI VTTNIVKQCG TAAYYMLLGK FKRVDWKATL
RLFLLLCTTI LLLSSIYHLV LFNQVLSSDV MLEDATGILA IYKEVRSYLG IRTLCDGLVV
EYRNTSFDVM EFCSNRSVLC QWCLIGQDSL TRYSALQMLQ THITSYVLNI DWIWFALEFF
LAYVLYTSSF NVLLLVVTAQ YFFAYTSAFV NWRAYNYIVS GLFFLVTHIP LHGLVRVYNF
LACLWFLRKF YSHVINGCKD TACLLCYKRN RLTRVEASTI VCGTKRTFYI AANGGTSYCC
KHNWNCVECD TAGVGNTFIC TEVANDLTTT LRRLIKPTDQ SHYYVDSVVV KDAVVELHYN
RDGSSCYERY PLCYFTNLEK LKFKEVCKTP TGIPEHNFLI YDTNDRGQEN LARSACVYYS
QVLCKPMLLV DVNLVTTVGD SREIAIKMLD SFINSFISLF SVSRDKLEKL INTARDCVRR
GDDFQNVLKT FTDAARGHAG VESDVETTMV VDALQYAHKN DIQLTTECYN NYVPGYIKPD
SINTLDLGCL IDLKAASVNQ TSMRNANGAC VWNSGDYMKL SDSFKRQIRI ACRKCNIPFR
LTTSKLRAAD NILSVKFSAT KIVGGAPSWL LRVRDLTVKG YCILTLFVFT VAVLSWFCLP
SYSIATVNFN DDRILTYKVI ENGIVRDIAP NDVCFANKYG HFSKWFNENH GGVYRNSMDC
PITIAVIAGV AGARVANVPA NLAWVGKQIV LFVSRVFANT NVCFTPINEI PYDTFSDSGC
VLSSECTLFR DAEGNLNPFC YDPTVLPGAS SYADMKPHVR YDMYDSDMYI KFPEVIVEST
LRITKTLATQ YCRFGSCEES AAGVCISTNG SWALYNQNYS TRPGIYCGDD YFDIVRRLAI
SLFQPVTYFQ LSTSLAMGLV LCVFLTAAFY YINKVKRALA DYTQCAVVAV VAALLNSLCL
CFIVANPLLV APYTAMYYYA TFYLTGEPAF IMHISWYVMF GAVVPIWMLA SYTVGVMLRH
LFWVLAYFSK KHVDVFTDGK LNCSFQDAAS NIFVIGKDTY VALRNAITQD SFVRYLSLFN
KYKYYSGAMD TASYREACAA HLCKALQTYS ETGSDILYQP PNCSVTSSVL QSGLVKMSAP
SGAVENCIVQ VTCGSMTLNG LWLDNTVWCP RHIMCPADQL TDPNYDALLI SKTNHSFIVQ
KHIGAQANLR VVAHSMVGVL LKLTVDVANP STPAYTFSTV KPGASFSVLA CYNGKPTGVF
TVNLRHNSTI KGSFLCGSCG SVGYTENGGV INFVYMHQME LSNGTHTGSS FDGVMYGAFE
DKQTHQLQLT DKYCTINVVA WLYAAVLNGC KWFVKPTRVG IVTYNEWALS NQFTEFVGTQ
SIDMLAHRTG VSVEQMLAAI QSLHAGFQGK TILGQSTLED EFTPDDVNMQ VMGVVMQSGV
KRISYGFIHW LISTFVLAYV SVMQLTKFTM WTYLFETIPT QMTPLLLGFM ACVMFTVKHK
HTFMSLFLLP VALCLTYANI VYEPQTLISS TLIAVANWLT PTSVYMRTTH FDFGLYISLS
FVLAIIVRRL YRPSMSNLAL ALCSGVMWFY TYVIGDHSSP ITYLMFITTL TSDYTITVFA
TVNLAKFISG LVFFYAPHLG FILPEVKLVL LIYLGLGYMC TMYFGVFSLL NLKLRVPLGV
YDYSVSTQEF RFLTGNGLHA PRNSWEALIL NFKLLGIGGT PCIKVATVQS KLTDLKCTSV
VLLTVLQQLH LESNSKAWSY CVKLHNEILA AVDPTEAFER FVCLFATLMS FSANVDLDAL
ANDLFENSSV LQATLTEFSH LATYAELETA QSSYQKALNS GDASPQVLKA LQKAVNVAKN
AYEKDKAVAR KLERMAEQAM TSMYKQARAE DKKAKIVSAM QTMLFGMIKK LDNDVLNGVI
ANARNGCVPL SIVPLCASNK LRVVIPDISV WNKVVNWPSV SYAGSLWDIT VINNVDNEVV
KPTDVVETNE SLTWPLVIEC SRSSSSAVKL QNNEIHPKGL KTMVITAGVD QVNCNSSAVA
YYEPVQGHRM VMGLLSENAH LKWAKVEGKD GFINIELQPP CKFLIAGPKG PEIRYLYFVK
NLNNLHRGQL LGHIAATVRL QAGANTEFAS NSTVLTLVAF AVDPAKAYLD YVGSGGTPLS
NYVKMLAPKT GTGVAISVKP EATADQETYG GASVCLYCRA HIEHPDVSGV CKYKTRFVQI
PAHVRDPVGF LLKNVPCNVC QYWVGYGCNC DALRNNTVPQ SKDTNFLNES GVLV
