ID   R1A_BC512               Reviewed;        4128 AA.
AC   P0C6F6; Q0Q467;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 86.
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=p9;
DE   Contains:
DE     RecName: Full=Non-structural protein 2;
DE              Short=nsp2;
DE     AltName: Full=p87;
DE   Contains:
DE     RecName: Full=Non-structural protein 3;
DE              Short=nsp3;
DE              EC=3.4.19.12;
DE              EC=3.4.22.-;
DE     AltName: Full=PL1-PRO/PL2-PRO;
DE     AltName: Full=PLP1/PLP2;
DE     AltName: Full=Papain-like proteinases 1/2;
DE     AltName: Full=p195;
DE   Contains:
DE     RecName: Full=Non-structural protein 4;
DE              Short=nsp4;
DE     AltName: Full=Peptide HD2;
DE   Contains:
DE     RecName: Full=3C-like proteinase;
DE              Short=3CL-PRO;
DE              Short=3CLp;
DE              EC=3.4.22.-;
DE     AltName: Full=M-PRO;
DE     AltName: Full=nsp5;
DE     AltName: Full=p34;
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     AltName: Full=p5;
DE   Contains:
DE     RecName: Full=Non-structural protein 8;
DE              Short=nsp8;
DE     AltName: Full=p23;
DE   Contains:
DE     RecName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE     AltName: Full=p12;
DE   Contains:
DE     RecName: Full=Non-structural protein 10;
DE              Short=nsp10;
DE     AltName: Full=Growth factor-like peptide;
DE              Short=GFL;
DE     AltName: Full=p14;
DE   Contains:
DE     RecName: Full=Non-structural protein 11;
DE              Short=nsp11;
GN   ORFNames=1a;
OS   Bat coronavirus 512/2005 (BtCoV) (BtCoV/512/2005).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Pedacovirus.
OX   NCBI_TaxID=693999;
OH   NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
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).
CC   -!- FUNCTION: The papain-like proteinase 1 (PLP1) and papain-like
CC       proteinase 2 (PLP2) are responsible for the cleavages located at the N-
CC       terminus of the replicase polyprotein. In addition, PLP2 possesses a
CC       deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC       'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2
CC       also antagonizes innate immune induction of type I interferon by
CC       blocking the nuclear translocation of host IRF-3 (By similarity).
CC       {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=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=P0C6F6-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6W0-1; Sequence=External;
CC   -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC       association of the replication complex and thereby alter the
CC       architecture of the host cell membrane. {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC       mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC       processed (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Bat coronavirus 512/2005 is highly similar to porcine
CC       epidemic diarrhea virus (PEDV).
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; DQ648858; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0C6F6; -.
DR   Proteomes; UP000113079; 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:0016020; C: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:0008242; F:omega peptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; 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; cd21901; alpha_betaCoV_Nsp10; 1.
DR   CDD; cd21558; alphaCoV-Nsp6; 1.
DR   CDD; cd21514; alphaCoV_Nsp2_HCoV-229E-like; 1.
DR   CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR   CDD; cd21826; alphaCoV_Nsp7; 1.
DR   CDD; cd21830; alphaCoV_Nsp8; 1.
DR   CDD; cd21897; alphaCoV_Nsp9; 1.
DR   CDD; cd21731; alphaCoV_PLPro; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21875; PEDV-like_alphaCoV_Nsp1; 1.
DR   CDD; cd21712; TM_Y_alphaCoV_Nsp3_C; 1.
DR   Gene3D; 1.10.8.1190; -; 2.
DR   Gene3D; 3.10.20.540; -; 1.
DR   Gene3D; 6.10.140.2090; -; 1.
DR   Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR   Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR   Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR   Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR046443; a/bCoV_NSP1_glob.
DR   InterPro; IPR043613; CoV_NSP2_C.
DR   InterPro; IPR047573; CoV_NSP2_M.
DR   InterPro; IPR043611; CoV_NSP3_C.
DR   InterPro; IPR047566; CoV_NSP3_Y3.
DR   InterPro; IPR032505; CoV_NSP4_C.
DR   InterPro; IPR043612; CoV_NSP4_N.
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; IPR044385; NSP2_HCoV-229E-like.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR   InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR   InterPro; IPR038123; NSP4_C_sf_CoV.
DR   InterPro; IPR044309; NSP5_Mpro_alphaCoV.
DR   InterPro; IPR044369; NSP6_alphaCoV.
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; IPR043178; PLpro_thumb_sf_CoV.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   Pfam; PF09401; CoV_NSP10; 1.
DR   Pfam; PF19212; CoV_NSP2_C; 2.
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; 2.
DR   Pfam; PF01661; Macro; 1.
DR   Pfam; PF05409; Peptidase_C30; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF144246; Coronavirus NSP10-like; 1.
DR   SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR   SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF101816; Replicase NSP9; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51993; COV_3ECTO; 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_Y; 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; 2.
PE   3: Inferred from homology;
KW   Activation of host autophagy by virus; Disulfide bond; Host cytoplasm;
KW   Host membrane; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW   Membrane; Metal-binding;
KW   Modulation of host ubiquitin pathway by viral deubiquitinase;
KW   Modulation of host ubiquitin pathway by virus; Protease; Repeat;
KW   Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..4128
FT                   /note="Replicase polyprotein 1a"
FT                   /id="PRO_0000338050"
FT   CHAIN           1..110
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338051"
FT   CHAIN           111..897
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338052"
FT   CHAIN           898..2530
FT                   /note="Non-structural protein 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338053"
FT   CHAIN           2531..3012
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338054"
FT   CHAIN           3013..3314
FT                   /note="3C-like proteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338055"
FT   CHAIN           3315..3590
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338056"
FT   CHAIN           3591..3673
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338057"
FT   CHAIN           3674..3868
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338058"
FT   CHAIN           3869..3976
FT                   /note="Non-structural protein 9"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338059"
FT   CHAIN           3977..4111
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000338060"
FT   CHAIN           4112..4128
FT                   /note="Non-structural protein 11"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338061"
FT   TRANSMEM        1973..1993
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2036..2056
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2119..2139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2141..2161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2164..2184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2543..2563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2634..2654
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2669..2689
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2769..2789
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2802..2822
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2829..2849
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2878..2898
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3351..3371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3376..3396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3414..3434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3443..3463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3466..3486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3488..3507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3511..3531
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2..109
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          112..368
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          396..785
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          776..897
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          898..993
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1069..1302
FT                   /note="Peptidase C16 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1303..1467
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1638..1693
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1699..1965
FT                   /note="Peptidase C16 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          2052..2116
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2190..2530
FT                   /note="CoV Nsp3 Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          2917..3012
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          3013..3314
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3591..3673
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3674..3868
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          3869..3976
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          3977..4115
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   ZN_FING         1174..1205
FT                   /note="C4-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         1816..1849
FT                   /note="C4-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         4050..4066
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4092..4105
FT                   /evidence="ECO:0000250"
FT   REGION          1973..2184
FT                   /note="HD1"
FT                   /evidence="ECO:0000250"
FT   REGION          2190..2280
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2194..2207
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2240..2250
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2281..2530
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2281..2370
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2371..2428
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2429..2530
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2543..2898
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3351..3531
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1103
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1252
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1265
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1737
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1902
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1915
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        3053
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        3156
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   BINDING         2194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4050
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4053
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4059
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4066
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4092
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4095
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   SITE            110..111
FT                   /note="Cleavage; by PL1-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            897..898
FT                   /note="Cleavage; by PL1-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            2530..2531
FT                   /note="Cleavage; by PL2-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3012..3013
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3314..3315
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3590..3591
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3673..3674
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3868..3869
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3976..3977
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4111..4112
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   DISULFID        2068..2094
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2086..2091
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
SQ   SEQUENCE   4128 AA;  456581 MW;  550324DCD9D1820F CRC64;
     MASNHISLAF ANDEEISAIG FGSVEEAVSY YSDAAVNGFD QCRFVSLGLQ DAVVGVEDDD
     VVMLITGVTQ LRAYLGTFGD RPLNLRGWLL FSNCNYFLEE LDLVFGRCGG TTIPVDQFMC
     GADGAPVIQE GDWTFMDYFQ DSNQFTLNGI TYVKAWDVDR KPNDYAKQNV TCIRRITYIT
     DHRHVLADGT TMKTARHPKV NKSVVLDSPF DQIYKEVGSP FMGNGSTFVE MLKDPAFFHA
     LITCECGRSE WTVGDWKGYN SLCCNIKCKP ITIVTPKAVP GAVVITKAGI GAGLKCYNNV
     FLKHIIDLVV PGTNLGWGVW RIAKVQSKDD VATSGNVLVD DPEDRLDPCY FGNDGPFATK
     FKFQLLANSF DDEVKGAIVQ GVVHVNTAIC DVVKDILGLP WFVKKLGSLV TVMWDQFVAG
     VQSMKICTLK VVQLAKALSC ATMSVVKGVI TLVAEVPEIF KRLFYTLTSA LKSLCTSSCD
     ALVVAGKSFA KIGDYVLLPS ALVRLVSSKV KGKAQSGIKQ LQFATVVLGD THKVESDRVE
     FSSVNLKMVD EEFPLNPVGH TVAVGNQAFF CSDGLYRFMA DRDLVITSPI FKPELELEPI
     FECDAIPGFP KVAASNVAEL CVKVDTLLFN YDKIYKKYST IIKGDRCYIQ CTHTFKAPSY
     YFDDDEFVEL CTKYYKLPDF DAFYNAVHAA TDMDQFCALC TSGFEVFIPR VPDCPPILND
     IDGGSIWTSF ILSVRSATDF IKTLKIDLGL NGVVVFVTKK FRKAGALLQK LYNAFLDTVT
     SFIKVAGVAF KYCATCVPKI VINGCYHTVT RLFAKDLQIP TEDGVADFNT FNHCVFPVNP
     TRIETDSLEL EEVDFVEPGV DGKLVILDDY SFYSDGTNYY PSDGKGVVAS CFKKKGGGVV
     TISDEVQVRT IDPVYKVRLE YEFEDETLVK VCEKAIGTKL KVTGDWSNLL ETLEKAMDVV
     RQHLDVPDYF VYDEEGGTDL NLTIMVSQWP LSSDSEDDFK AVDDEPNANT DETVDTFAED
     VAETQNVQQD VTQDEVEAVC DLVVKATEEG PIEHEELSED QKEVQQALAF IEDKPVVVKP
     DVFAFSYASY GGLKVLNQSS NNCWVSSALV QLQLTGLLDS DEMQLFNAGR VSPMVKRCYE
     SQRAIFGSLG DVSACLESLL KDRDGMSITC TIDCGCGPGV RVYENAIFRF TPLKTAFPMG
     RCLICSKTLM HTITQMKGTG IFCRDATALD VDTLVVKPLC AAVYVGAQDG GHYLTNMYDA
     NMAVDGHGRH PIKFNTINTL CYKDVDWEVS NGSCDVKPFL TYKNIEFYQG ELSALLSVNH
     DFVVNAANEQ LSHGGGIAKA LDDLTKGELQ VLSNQYVSRN GSIKVGSGVL IKCKEHSILN
     VVGPRKGKHA AELLTKAYTF VFKQKGVPLM PLLSVGIFKV PITESLAAFL ACVGDRVCKC
     FCYTDKERLA IQNFVTSFQT EQPVEPLPVI QEVKGVQLEK PVPDVKVENP CEPFRIEGDA
     KFYDLTPSMV QSLQVTRLVS FTNSDLCLGS FVRDCDGYVQ GSLGGAIANY KKSNPVLPAG
     NCVTLKCDGF ISFTFVILPK EGDTNYEKNF NRAIAKFLKL KGSLLVVVED SSVFNKISHA
     SVAGYVAKPA LVDTLFEAKP VQVVVTQDQR SFHTVELSTS QTYGQQLGDC VVEDKKVTNL
     KPVSKDKVVS VVPNVDWDKH YGFVDAGIFH TLDHTMFVFD NNVVNGKRVL RTSDNNCWIN
     AVCLQLQFAN AKFKPKGLQQ LWESYCTGDV AMFVHWLYWI TGVEKGEPSD AENTLNIISR
     FLKPQGSVEM LRATSTTCDG TCSTKRVVST PVVNASVLKV GLDDGNCVHG LPLVDRVVSV
     NGTVIITNVG DTPGKPVVAT ENLLLDGVSY TVFQDSTTGV GHYTVFDKEA KLMFDGDVLK
     PCDLNVSPVT SVVVCNNKKI VVQDPVKRVE LDASKFLDTM NVASEKFFTF GDFVSRNIIV
     LIVYLFSLLA ICFRALKKRD MKVMAGVPER TGIILKRSVK YNYKALKFFF RLKFQYIKVF
     LKFSLVLYTL YALMFMFIRF TPVGTPICKR YTDGYANSTF DKNDYCGNVL CKICLYGYEE
     LSDFTHTRVI WQHLKDPLIG NILPLFYLVF LIIFGGFFVR IGITYFIMQY INAAGVALGY
     QDNVWLLHLL PFNSMGNIIV VAFIVTRILL FLKHVLFGCD KPSCIACSKS AKLTRVPLQT
     ILQGVTKSFY VNANGGKKFC KKHNFFCVDC DSYGYGCTFI NDVIAPELSN VTKLNVIPTG
     PATIIIDKVE FSNGFYYLYS GSTFWKYNFD ITEAKYACKD VLKNCNILTD FVVFNNSGSN
     VTQVKNACVY FSQLLCKPIK LVDSALLASL NVDFSANLHK AFVEVLSNSF GKDLSNCSNM
     NECRESLGLS DVPEEEFSAA VSEAHRYDVL ISDVSFNNLI VSYAKPEEKL AVHDIANCMR
     VGAKVVNHNV LTKDNVPVVW LAKDFIALSE EARKYIVRTT KTKGINFMLT FNDRRMHLTI
     PTISVANKKG AGLPSLFTRL YSFFWHLCVL IVVLFVATSL LDFSAQVTSD TQYDFKYIEN
     GVLKVFEKPL DCVHNAFVNF NEWHNAKFGS IPTNSRRCPI VVGTSDEVRY IPGVPAGVFL
     YGKSLIFAMS TIFGTSGLCF DDRGLTDPDS CIFNSACTTL SGIGGRNVYC YREGVVDNAK
     LYSSLLPHSY YRLMDGNHIV LPEIITRGFG IRTIKTQAMT YCRTGECIDS QAGVCVGLDR
     FFVYSKTPGS DYVCGTGFFS LLFNVIGMFS NSIPVTVMSG QILLNCVVAF TAVMACFAFT
     KFKRLFGDMS FGVLSVGLCT VVNNLSYVVT QNSIGMLAYA TLYFLCTKGV RYSWVWHVGF
     AISYCFLAPW WVVLAYLICA LLEFLPNLFK LKVSTQLFEG DKFVGSFESA ASGTFVLDMH
     SYQKLANSIS TEKLKQYCAS YNRYKYYSGS ASEADYRLAC FAHLAKAMSD FANDHMDKLY
     TPPTVSYNST LQAGLRKMAQ PSGIVEGCIV RVSYGNLTLN GLWLGDTVIC PRHVIASNTT
     NVIDYDHAMS LVRLHNFSIS SGNMFLGVIS ASMRGTLLHI KVNQSNVNTP NYTYKVLKPG
     DSFNILACYD GSAAGVYGVN MRTNYTIRGS FISGACGSPG YNINNGVVEF CYMHHLELGS
     GCHVGSDMDG TMYGKYEDQP TLQIEGASNL VTENVCSWLY GALINGDRWW LSSVSVGVDT
     YNEWALRNGM TALKNVDCFS LLVAKTGVDV GRLLASIQKL HGNFGGKSIL GCTSLCDEFT
     LSEVVKQMYG VTLQSGKVSR AFRNASIVCC LLFLFLSEML NHSKLFWINP GYITPVFLAI
     IVASSALMLL VKHKLLFLQL YLLPSLCIVS GYNIFKDYHF YTYMLEEFDY KVPFGGFNVT
     GVLNISLCCF VMGLHTFRFL QTPNKIFSYV VAVLTVLYTY YYSTDVLGLI LTSMSGFTNY
     WFIGTATYKL ATYVLPHTSL LDSFDAIKAV VFLYLLLGYC NCVYYGSLYW INRFCKLTLG
     CYEFKVSAAE FKYMVANGLR APTGVFDALI LSLKLIGVGG RKTIKISSVQ SKLTDLKCTN
     VVLLGCLSNM NIAANSREWA YCVDLHNKIN LCNDAEAAQE MLLALLAFFL SKNSAFGVDE
     LLDSYFNDSS VLQSVAATYV NLPSYLAYET ARQSYEDALA NGSPPQLVKQ LRHAMNVAKS
     EFDREASTQR KLDRMAEQAA SQMYKEARAV NRKSKVVSAM HSLLFGMLRR LDMSSVDTIL
     SLAKDGVVPL SIIPAVSATK LNIVVSDIES YSKIQREGCV HYAGVIWSVV DIKDNDGKPV
     HAKEVVTSNV ESLAWPLFLN CERIIKLQNN EIIPSKIKQR PIKAEGEGVV ADGNALYSNE
     GGRTFMYAFI SDKPDLKVVK WEFDGGSNAI ELEPPCKFLV EAPSGPVVKY LYFVRNLNNL
     RRGAVLGFIG ATVRLQAGKQ TEQATNSSLL TLCAFAVDPP KTYLDAVKSG HRPVGNCVKM
     LANGSGNGQA ITNGVEASTN QDSYGGASVC LYCRAHVEHP DMDGFCKLRG KYVQVPLGTL
     DPIRFVLENT VCKVCGCWQA NGCTCDRAVI QSVDSGYLNE CGALVQLD
//