R1A_BCHK5
ID R1A_BCHK5 Reviewed; 4481 AA.
AC P0C6T5; A3EXC9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 HKU5 (BtCoV) (BtCoV/HKU5/2004).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=694008;
OH NCBI_TaxID=105295; Pipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU5-1;
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 -!- 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=P0C6T5-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6W4-1; 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; EF065509; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0C6T5; -.
DR IntAct; P0C6T5; 1.
DR PRIDE; P0C6T5; -.
DR SABIO-RK; P0C6T5; -.
DR Proteomes; UP000007451; 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: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: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; cd21517; cv_beta_Nsp2_MERS-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; 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; IPR044388; NSP2_MERS-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; 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; Host cytoplasm; Host membrane;
KW 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..4481
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338098"
FT CHAIN 1..195
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338099"
FT CHAIN 196..851
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338100"
FT CHAIN 852..2830
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338101"
FT CHAIN 2831..3338
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338102"
FT CHAIN 3339..3644
FT /note="3C-like proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338103"
FT CHAIN 3645..3936
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338104"
FT CHAIN 3937..4019
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338105"
FT CHAIN 4020..4218
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338106"
FT CHAIN 4219..4328
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338107"
FT CHAIN 4328..4481
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338109"
FT CHAIN 4329..4467
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338108"
FT TRANSMEM 2196..2216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2268..2288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2372..2392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2396..2416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2421..2441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2848..2868
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3119..3139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3152..3172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3203..3223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3650..3670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3684..3704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3709..3729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3760..3777
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3782..3802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3823..3843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3855..3875
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 159..195
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 197..473
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 479..713
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 715..851
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 855..964
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1186..1345
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1354..1480
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1480..1553
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1558..1613
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1628..1902
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1916..2033
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2059..2179
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2725..2828
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3242..3338
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3339..3644
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3937..4019
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 4020..4218
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4219..4328
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4329..4467
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1748..1785
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4402..4418
FT /evidence="ECO:0000250"
FT ZN_FING 4444..4457
FT /evidence="ECO:0000250"
FT REGION 340..361
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 2158..2441
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2848..3223
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3650..3875
FT /note="HD3"
FT /evidence="ECO:0000250"
FT ACT_SITE 1668
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1838
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3379
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3486
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4457
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 851..852
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 2830..2831
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3338..3339
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3644..3645
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3936..3937
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4019..4020
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4218..4219
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4328..4329
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4467..4468
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
SQ SEQUENCE 4481 AA; 494801 MW; 6EA797D2808AF75F CRC64;
MSFVAGVAPQ GARGKYRAEL NTEKRTDHVS LKASLCDAGD LVLKISPWFM DGESAYKHVS
EQLSKGSKLL FVPQTLKGFI RHLPGPRVYL VERLTGGTYS DPFMVNQLAY QNAAGEGVIG
TTLQGKRVGM FFPFDADLVT GEFQFLLRKK GFGGNRFRDA PWDYNWTPYS DLMDALEADP
CGKYSQSLLK KLVGGDFTPI DQYMCGKNGK PIAEFAALMA SEGITKLADV EAEVKSRTDS
DRYIVFKNKL YRIVWNVQRK DVAYSKQSAF TMNSIVQLDT MEDVPRHSFT IGSEIQVIAP
STAVQANGHL NLKQRLLYAF YGKQAVSEPN YIYHSAYVDC TSCGKGSWLT GNAVQGFACD
CGAHYCANDV DLQSSGLVRK NAVLLTTCPC NKDGECKHTL PQLVSMMTDK CDVEVVGKTF
ILTYGGVIYA YMGCSGGTMH FIPRAKSCVS KIGDAIFTGC TGTWSKVCET ANLFLERAQH
AINFVNEFVL TETVVALLSG TTSSIEELRD LCRNATFEKV RDYLTPRGWI VTMGSYIEGV
INVGAAGVCN AALNAPFIVL SGLGESFKKV AATPWKLCSS LRETLDHYAD SITYRVFPYD
IPCDVTDYTA LLLDCAVLTG ASAYFVARYV DEKVEQLTNL VFSSCQSAVA AFVQACMSTY
KATAKFISDM FTLIKVVSER LYVYTSVGFV VVGDYSSQLL KQFMHILSKA MQLLHTTVSW
AGSKLPSVVY NGRDSLVFPS GTYYCVSTQG RSLQDQFDLV IPGDLSKKQI GILEPTPNST
TVDKKINTNV VEVVVGQLEP TKEHSPELVV GDYVIISNKI FVRSVEDSET VFYPLCTDGK
IVPTLFRLKG GAPPKGVKFG GEQTKEITAV RSVSVDYDVH PVLDALLAGS ELATFTVEKD
LPVKDFVDVV KDEVIELLSK LLRGYNVDGF DLEDFADTPC YVYNAEGDLA WSSTMTFSVN
PVEEVEEECD DDYVEDEYLS EEMLVEEDEN SWAAAVEAVI PMEDVQLDTL VAEIDVSEPA
DDVAEQASTE EVEVPSACVL EASQVANAAE VESCEAEVSS SIPLHEDANA AKANDCAEGM
PALDSTETVS KLSVDTPVGD VTQDDATSSN ATVISEDVHT ATHSKGLVAV PEVVPEKALG
TSVERMRSTS EWTVVETSLK QETAVIVKND SSAKPQRVKK PKAENPLKNF KHIVLNNDVT
LVFGDAIAVA RATEDCILVN AANTHLKHGG GIAAAIDRAS GGLVQAESDD YVNFYGPLNV
GDSTLLKGHG LATGILHVVG PDARANQDIQ LLKRCYKAFN KYPLVVSPLI SAGIFCVEPR
VSLEYLLSVV HTKTYVVVNS EKVYNDLAAP KPPTGLTYSH EGWRGIIRNA KSFGFTCFIC
TDQSANAKLL KGRGVDLTKK TQTVDGVKYY LYSSKDPLTD IITAANACKG ICAMPIGYVT
HGLDLAQAGQ QVKKITVPYV CLLASKDQVP ILNSDVAVQT PEQSFINTVI ANGGYHCWHL
VTGELIVKGV SYRKLLNWSD QTICYADNKF YVVKGQIALP FDSLEKCRTY LTSRAAQQKN
VDVLVTIDGV NFRTVVLNNT TTYRVQLGSV FYKGSDISDT IPTEKMSGEA VYLADNLSEA
EKAVLSEVYG TADTAFLHRY YSLLALVKKW KYTVHDGVKS LKLNSNNCYV NVTMLMLDML
KEIKFIVPAL QAAYLKHKGG DSTEFIALIM AYGDCTYGEP DDASRLLHTI LSKAELTTQA
KMVWRQWCNV CGVQDTTTTG LKACIYVGMN SLDELHATHE ECCQCGDVRK RQLVEHNAPW
LLLSGLNEAK VMTPTSQSAG PDYTAFNVFQ GVETSVGHYL HVRVKDNLLY KYDSGSLSKT
SDMKCKMTDV YYPKQRYSAD CNVVVYSLDG NTWADVDPDL SAFYMKDGKY FTKKPVIEYS
PATILSGSVY TNSCLVGHDG TIGSDAISSS FNNLLGFDNS KPVSKKLTYS FFPDFEGDVI
LTEYSTYDPI YKNGAMLHGK PILWVNNSKF DSALNKFNRA TLRQVYDIAP VTLENKYTVL
QDNQIQQVEV EAPKEDAKPQ SPVQVAEDID NKLPIIKCKG LKKPFVKDGY SFVNDPQGVN
VIDTLGIDDL RALYVDRNLR LIVLKENNWS ALFNIHTVEK GDLSVIAASG SITRRVKILL
GASSLFAQFA SVTVNVTTAM GKALGRMTRN VITNTGIIGQ GFALLKMLLI LPFTFWKSKN
QSTVKVEVGA LRTAGIVTTN VVKQCASAAY DVLVVKFKRI DWKSTLRLLF LICTTGLLLS
SLYYLFLFHQ VLTSDVMLDG AEGMLATYRE LRSYLGIHSL CDGMVEAYRN VSYDVNDFCS
NRSALCNWCL IGQDSLTRYS AFQMIQTHVT SYVINIDWVW FVMEFALAYV LYTSTFNVLL
LVVSSQYFFS YTGAFVNWRS YNYLVSGYFF CVTHIPLLGL VRIYNFLACL WFLRRFYNHV
INGCKDTACL LCYKRNRLTR VEASTVVCGS KRTFYIVANG GTSFCCRHNW NCVDCDTAGI
GNTFICEEVA NDLTTSLRRL VKPTDKSHYY VESVTVKDSV VQLHYSREGA SCYERYPLCY
FTNLDKLKFK EVCKTPTGIP EHNFLIYDSS DRGQENLARS ACVYYSQVLS KPMLLVDSNM
VTTVGDSREI ASKMLDSYVN SFISLFGVNR DKLDKLVATA RDCVKRGDDF QTVIKTFTDA
ARGPAGVESD VETSSIVDAL QYAYKHDLQL TTEGFNNYVP SYIKPDSVAT ADLGCLIDLN
AASVNQTSIR NANGACIWNS SDYMKLSDSL KRQIRIACRK CNIPFRLTTS RLRSADNILS
VKFSATKLSG GAPKWLLKLR DFTWKSYCVV TLVVFAMAVL SYLCLPAFNM SQVSFHEDRI
LTYKVVENGI IRDITPSDTC FANKYQSFSK WFNEHYGGLF NNDISCPVTV AVIAGVAGAR
VPNLPANVAW VGRQIVLFVS RVFASSNNVC YTPTAEIPYE RFSDSGCVLA SECTLFRDAE
GKINPYCYDP TVLPGASAYD QMKPHVRYDM YDSDMYIKFP EVVFESTLRI TKTLATRYCR
FGSCEDANEG VCITTNGSWA IYNDHYANKP GVYCGDNYFD IVRRLGLSLF QPVTYFQLST
SLALGVMLCI FLTIAFYYVN KVKRALADYT QCAVVAVAAA LLNSLCLCFV VSNPLLVLPY
TALYYYATFY LTGEPAFVMH VSWFVMFGTV VPIWMVFAYI VGVCLRHLLW VMAYFSKKHV
EVFTDGKLNC SFQDAAANIF VINKDTYVAL RNSITQDSYN RYLSMFNKYK YYSGAMDTAS
YREASAAHLC KALQVYSETG SDVLFQPPNC SVTSSVLQSG LVKMAAPSGV VENCMVQVTC
GSMTLNGLWL DNYVWCPRHV MCPADQLSDP NYDALLVSKT NLSFIVQKNV GAPANLRVVG
HTMVGTLLKL TVESANPQTP AYTFTTVKPG ASFSVLACYN GRPTGVFMVN MRQNSTIKGS
FLCGSCGSVG YTQEGNVINF CYMHQMELSN GTHTGCAFDG VMYGAFEDRQ VHQVQLSDKY
CTINIVAWLY AAILNGCNWF VKPNKTGIAT FNEWAMSNQF TEFIGTQSVD MLAHKTGVSV
EQLLYAIQTL HKGFQGKTIL GNSMLEDEFT PDDVNMQVMG VVMQSGVKRI SYGLVHWLFT
TLLLAYVATL QLTKFTIWNY LFEVIPLQLT PLVLCVMACV MLTVKHKHTF LTLFLLPTAI
CLTYANIVYE PQTPVSSALI AVANWLNPAS VYMRTTHTDL GVYLSLCFAL AVVVRRLYRP
NASNLALALG SAMVWFYTYT TGDCSSPLTY LMFLTTLTSD YTVTVFLAVN VAKFFARVVF
LYAPHAGFIF PEVKLVLLMY LAVGYFCTVY FGVFSLLNLK LRVPLGVYDY TVSTQEFRYL
TGNGLHAPRN SWEALRLNMK LIGIGGTPCI KIASVQSKLT DLKCTSVVLL SVLQQLHLEA
NSKAWAHCVK LHNDILAATD PTEAFDNFVC LFATLMSFSA NVDLEALASD LLDHPSVLQA
TLSEFSHLAS YAELEAAQSS YQKALNSGDA SPQVLKALQK AVNIAKNAYE KDKAVARKLE
RMAEQAMTSM YKQARAEDKK AKIVSAMQTM LFGMIKKLDN DVLNGVISNA RNGCVPLSVV
PLCASNKLRV VIPDITIWNK VVTWPSLSYA GALWDISLIN NVDGEVVKSS DVTETNESLT
WPLVLECTRA ASSAVTLQNN EIRPSGLKTM VVSAGIDHAN CNTSSLAYYE PVEGRKMLMG
ILSENAHLKW AKVEGRDGFV NIELQPPCKF LIAGPKGPEV RYLYFVKNLN NLHRGQLLGH
IAATVRLQAG SNTEFAINSS VLSAVTFSVD PGKAYLDFVN AGGAPLTNCV KMLTPKTGTG
IAVSVKPEAN ADQDTYGGAS VCLYCRAHIE HPDVTGVCKF KGKFVQVPLH IRDPVGFCLQ
NTPCNVCQFW IGHGCNCDAL RGTTIPQSKD SNFLNESGVL L
