ID R1AB_BEV Reviewed; 6857 AA.
AC P0C6V7; P18458; Q1WFM5; Q65826; Q65827;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Non-structural protein 1;
DE Short=nsp1;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE Contains:
DE RecName: Full=3C-like serine proteinase;
DE Short=3CLSP;
DE EC=3.4.21.-;
DE AltName: Full=M-PRO;
DE AltName: Full=nsp3;
DE AltName: Full=p27;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE Contains:
DE RecName: Full=Non-structural protein 5;
DE Short=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=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=nsp10;
DE AltName: Full=p100;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=nsp11;
DE AltName: Full=p67;
DE Contains:
DE RecName: Full=Exoribonuclease;
DE Short=ExoN;
DE EC=3.1.13.-;
DE AltName: Full=nsp12;
DE Contains:
DE RecName: Full=Non-structural protein 13;
DE Short=nsp13;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease;
DE EC=3.1.-.-;
DE AltName: Full=NendoU;
DE AltName: Full=nsp14;
DE Contains:
DE RecName: Full=Putative 2'-O-methyl transferase;
DE EC=2.1.1.-;
DE AltName: Full=nsp15;
GN Name=rep; ORFNames=1a-1b;
OS Berne virus (BEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus;
OC Renitovirus; Equine torovirus.
OX NCBI_TaxID=11156;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-4569, CHARACTERIZATION OF 3C-LIKE
RP PROTEINASE M-PRO, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=16571831; DOI=10.1128/jvi.80.8.4157-4167.2006;
RA Smits S.L., Snijder E.J., de Groot R.J.;
RT "Characterization of a torovirus main proteinase.";
RL J. Virol. 80:4157-4167(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-252.
RX PubMed=1856694; DOI=10.1099/0022-1317-72-7-1635;
RA Snijder E.J., den Boon J.A., Horzinek M.C., Spaan J.M.;
RT "Characterization of defective interfering RNAs of Berne virus.";
RL J. Gen. Virol. 72:1635-1643(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4219-6857.
RC STRAIN=Isolate P138/72;
RX PubMed=2388833; DOI=10.1093/nar/18.15.4535;
RA Snijder E.J., den Boon J.A., Bredenbeek P.J., Horzinek M.C., Rijnbrand R.,
RA Spaan W.J.M.;
RT "The carboxyl-terminal part of the putative Berne virus polymerase is
RT expressed by ribosomal frameshifting and contains sequence motifs which
RT indicate that toro- and coronaviruses are evolutionarily related.";
RL Nucleic Acids Res. 18:4535-4542(1990).
CC -!- FUNCTION: The 3C-like serine proteinase is responsible for the majority
CC of cleavages.
CC -!- FUNCTION: The helicase which contains a zinc finger structure displays
CC RNA and DNA duplex-unwinding activities with 5' to 3' polarity.
CC {ECO:0000250}.
CC -!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3' to
CC 5' direction. {ECO:0000250}.
CC -!- FUNCTION: NendoU is a Mn(2+)-dependent, uridylate-specific enzyme,
CC which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 2]: 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6V7-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6F3-1; 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 protease yield
CC mature proteins. 3CL-PRO is autocatalytically processed (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
CC ribosomal frameshifting at the 1a-1b genes boundary.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36600.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA36601.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ310701; ABC26008.1; -; Genomic_RNA.
DR EMBL; X56016; CAA39493.1; -; Genomic_RNA.
DR EMBL; X52374; CAA36600.1; ALT_SEQ; Genomic_RNA.
DR EMBL; X52374; CAA36601.1; ALT_SEQ; Genomic_RNA.
DR PIR; S11237; S11237.
DR PIR; S11238; S11238.
DR Proteomes; UP000006571; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21162; NendoU_tv_PToV-like; 1.
DR CDD; cd23186; Tobaniviridae_RdRp; 1.
DR CDD; cd21413; unc_tv_SF1_Hel-like; 1.
DR CDD; cd21403; ZBD_tv_SF1_Hel-like; 1.
DR Gene3D; 3.90.1140.10; Cyclic phosphodiesterase; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044397; NendoU_PToV-like.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR046438; NIV_2_O_MTASE.
DR InterPro; IPR046436; NIV_EXON.
DR InterPro; IPR039573; NS2A-like.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR044355; SF1_Hel_unc_tv.
DR InterPro; IPR044336; SF1_Hel_ZBD_tv.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF05213; Corona_NS2A; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF142877; EndoU-like; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endonuclease; Exonuclease; Helicase; Host membrane; Hydrolase;
KW Membrane; Metal-binding; Methyltransferase; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; Repeat; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication; Zinc; Zinc-finger.
FT CHAIN 1..6857
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000106126"
FT CHAIN 1..2873
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283842"
FT CHAIN 2874..3251
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283843"
FT CHAIN 3252..3543
FT /note="3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283845"
FT CHAIN 3544..3802
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283846"
FT CHAIN 3803..3979
FT /note="Non-structural protein 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283847"
FT CHAIN 3980..4161
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283848"
FT CHAIN 4162..4246
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283849"
FT CHAIN 4247..4399
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283850"
FT CHAIN 4400..5410
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283851"
FT CHAIN 5411..5968
FT /note="Helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283852"
FT CHAIN 5969..6298
FT /note="Exoribonuclease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283853"
FT CHAIN 6299..6442
FT /note="Non-structural protein 13"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283854"
FT CHAIN 6443..6592
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283855"
FT CHAIN 6593..6857
FT /note="Putative 2'-O-methyl transferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283856"
FT TRANSMEM 2303..2323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2330..2350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2385..2405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2535..2555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2639..2659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2664..2684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2889..2909
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3057..3077
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3106..3126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3142..3162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3556..3575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3580..3602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3611..3631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3640..3660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3663..3683
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3698..3718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3723..3738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1679..1860
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 4566..4797
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 5105..5256
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5413..5528
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5633..5812
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5813..5972
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5970..6183
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6451..6591
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6593..6857
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT REGION 2158..2191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2303..2683
FT /note="HD1"
FT REGION 2889..3162
FT /note="HD2"
FT REGION 3555..3738
FT /note="HD3"
FT ACT_SITE 3304
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255"
FT ACT_SITE 3347
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255"
FT ACT_SITE 3416
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255"
FT ACT_SITE 5984
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6085
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6504
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6737
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 5417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 6149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT SITE 2873..2874
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 3251..3252
FT /note="Cleavage; by 3C-like serine proteinase"
FT SITE 3543..3544
FT /note="Cleavage; by 3C-like serine proteinase"
FT SITE 3802..3803
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 3979..3980
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4161..4162
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4246..4247
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4399..4400
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 5410..5411
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 5968..5969
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 6298..6299
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 6442..6443
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 6592..6593
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT CONFLICT 251..252
FT /note="RR -> KK (in Ref. 2; CAA39493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 6857 AA; 784289 MW; 9B6D3B9DE488C854 CRC64;
MSTSSSILDI PSKMFRILKN NTRETEQHLS SSTLDLISKS QLLAQCFDTQ EIMASLSKTV
RSILESQNLE HKSTLTPYNS SQSLQLLVMN TSCTQFKWTT GSTSSVKALL EKELCRGLVP
LNDITPKSNY VELSLLTPSI LIGNETSTTT TLPEIPLDME QSIISCVENT LLKEVQALSG
QESCQEYFLS ANYQSLIPPQ VLLNLMKMSS VVDLSPLTLP NTRLWLKLSP FHGGTSVSYA
TQIKGYANCA RREEKCLKNR LTKKQKNQEK GSFDARSVIT LGGKMYRYKV VVLRCEDQSD
NLSELQFEPQ VEYTMDMVPH CWKELVKKRL IRAKGTWDLS CVEDLDLDHV EVRGDSLLHR
SSVVHDLTSI VDDTLQEKLF SRTWLRQSLK YSGNILQRLS SLFATEGLKK ITLVNSDITP
VQVGDKWLNF VDFGKSTVFF VKTLNNIHLA MTRQRESCNY IHEKFGRVRW LGAKPEQGAI
VKVFAWCLNK KEFKFRDNQL KQYVCRQGVI KHEPCEYLNV EVLDEFVALN NDLNCVQKIK
TYLAAYFGLK KVKLTQKNFM TPLITKKQEL VFQPCNCPNH QFYVAQFDKH VTLGLGRKDG
ILFAEQVPSY AIILAVGFGT VETQLVTHYY SEMRRVYHPL DFQSNTFVFD HQGVMLEDIS
PADYNDVGEE DYQLEYSGGF DQPFQNYHSD DEDQAFPDFE DERHPDEENW ARPIISSGES
SVVSSRPSSP LVYSSLVPVA SPFGYMNGIR VFDICLADDL DFLQIHGQCP CARCKGLYFY
QPIRPRGFTI FENVVEFFSF VEKCEVFEEI GPFFKMIEYS MLYNEYNIFY GLGKKIYQSD
LVLPVKHLDQ LWKRAQLDID VVSEFENFKN SLQNINNVVY IAPYFNDQGE WNDIFDGYEF
NLNDNQFWFQ AKPVYDLVCY IYQGFFSDSR PLEKLYQKLC LDYHTSAMLH TQTHLKYCYV
ALLHSERAFQ MSINLDSLDN EQLHFLATMG MGDASLVGPT YLSEYHSNFN WYSIMSKACH
YVKLEQLVGL TYQEKRLMIL SRVQEFYEQQ HRGPIQLILS PLKVVNLPPI TCTEGYCYQP
VTRLFDTCVM PDIMKKLSRK RTSVSDVFGI LADYFKRTLS YRCFKVHEFC GIERQQEFSD
MTTLKLVTDW CQDTYYFYNE YATMTDVEPK VQVSSDYYLK IPSEVVEHIR QFLPHNVNVG
LMNYVSSNCD FDQCKFEFCL SGKGYVLGNM FFNRCAIQYV KTNLFIVLFK SRPLLYITQE
SIYLSDFNVL QAQCLTGEFC LDFEPVQGKT LFGVYFTNGQ RYGQQWETLP RFSLKPLNSP
RKRVPTQPFE ELAEVCIFKQ KLKLTQLHND CSVTPRVCSI PQTITATFQP YYCLENFYGV
KAPKVIVSGH LATHYVKLTH KISKCVLVTK LAVARAFYFT PTSMGSHYHL DPMEGISFGK
RATVQFEPVG LIKDVNLLVY QFGSHVSIQF FPEAPCIVAD GHYPSKYSGV WLGYLPSVEE
CKIAQVNHRV YVPTILRTSK SAPFHIIQNG DMGRGPITVT YHYAKNFDNK SLTPMFKMFQ
QVFEKSKDDI FKAFNTMSLE QKKVLSHFCG EFDEAYTLQT MSDEISFESS AYPDVVACSL
AYILGYEMCL TVKVNAKNEK LDIGSQCERV FVDYDVKKNE WTLSPEEGED SDDNLDLPFE
QYYEFKIGQT NVVLVQDDFK SVFEFLKSEQ GVDYVVNPAN SQLKHGGGIA KVISCMCGPK
LQAWSNNYIT KNKTVPVTKA IKSPGFQLGK KVNIIHAVGP RVSDGDVFQK LDQAWRSVFD
LCEDQHTILT SMLSTGIFGC TVNDSFNTFL SNVARLDKSL VVFVVTNMVE QYNQAFAVIK
MYQQYHGLPN FGNTCWFNAL YQLLKSFSEK EQCVNDLLNC FDDFYDCPTS QCVEWVCEQL
GVQFGQQQDA VEMLMKVFDV FKCDVRVGFD CLSRLQQVNC GFCVEVPAQA VLMFSGKDQC
GHWTAARKIV DKWYTFDDNH VVQKDPVWQN VVLVLRDRGI FRSADFERKP ARRRRVSHRV
PRDTLSQDAI TYIEDLRFSS GTCLSRYFVE SVESFVSGDN VSEVSDEQTC VEVAIEESDG
HVEQICQSSV DCVGMPESFQ FTFSMPLQTF VQECDQKCED DFSQEHVECD QQFEPVEQVG
QGGQQDGQVD QQIKESEQVV EPSAPSGQES PQALLQQVVD EVVYQIEQVK CDQKQDQDSV
QCDEIEEINS RGEQTVQQQL QPILGHDLNE NEGPTLSVGA GKLVRCRSLA VTESNLSTSN
TIFVWSEVLT HQYIGFKTDL MGLTYNIKFK LICYVLFLWF GVLCCTSHNT PFYMRLCIYL
VLLWLSLMIW NASQINVKTG WNELYVLKLL TSIKLPNIVK FRCELVQWFV LKCLFVSFYV
YDYVVKVCVS IFQMPQLRPF TWPFIKLGFV DTFLSHHILA FPEKVANQST LPTCGDKRYY
VYVPSWCRAS FTSLVMRARE LTSTGRSKTL DNWHYQCCSK TAKPLSCFNV REFVFDQDCK
HEAYGFLSSL CVYLLFYSGF LTFWLPLFCY YYVLFMCTFK NLPVDITKPI KWTVLQQVVN
DVLSLVTKPL FGRPVCPPLT TYLTSTTADE AVKVSRSLLG RFCTPLGFQQ PVMNVENGVT
VSNFGFFNPL MWPLFVVVLL DNRFIWFFNV LSYVMMPVFV IILFYFYLKK ICGCINFKGL
SKCCTKHFNQ FSKPLVAAGV HGNRTNFTYQ PMQEHWCDRH SWYCPKEEHY MTPDMAVYIK
NYYNLACAPT ADLVWCDYTK SAPTMTWSNF KYSSYKAKET VLCAPSSHAD SMLMAWYALL
HNVRFTVNPN VVDLPPAVNT IYVSSDSEDS VQDKSQPDVK LRPKKPKGNF KKQSVAYFSR
EPVDIWYYTT LVIVMGVLFM FMYSCLMVGQ YVVMPRDKFF GVNPTGYSYV NAPPYLHAAP
PVLQNSDGMI LATQLKVPSI TYSVYRLLSG HLYFTKLIVS DNECTPPFGA ARLSNEFSCN
GFTYVLPAHL RFFNRYVMLI HPDQLHMLPF EVEYGSHTRV CYTTGSNSVE CLPTFEIISP
YVFVFIVVIF TVIFLILIRL YIVMYSYFKV FTYVVFKLLF VNIIMVLFVV CLPPLVPGVV
FVLALWLCDS VMFLLYLAFL SLFILPWFYV LFFLFMVGGF VFWWMMRSAD VVHLTTDGLT
FNGTFEQISK CVFPLNPLIV NRMLLDCQMS HSDLVEKSKL KTTEGKLANE MMKVFMTGET
SYYQPSNFSF QSVFSKATSP FTLHARPPMP MFKLYVHFTG SCVGSTSTGT GFAIDDNTIV
TAKHLFEYDD LKPTHVSVEI VTRSHSARSA SIIWKEPDVK GWTFKGENAY IQVENLKDFY
IEDFKYLPFQ QIEKDFYKRM EPVTIYSVKY GSEFATQAWQ TVNGHFVCYN TEGGDSGAPL
VCNGRIVGVH QGLCDNFKTT LASDFEGKMM TEVKGHHVDP PVYYKPIIIS AAYNKFVAGE
DSSVGDGKNY HKFENEDFAC MCKELESVTF GDQLRRYCYN LPQFLEPLQY FHVPSFWQPF
KKQSVSNNVS WVVEHLHFIF SIYFLICDFV AYWWLDDPFS VVLPLFFIVQ LLSTVFLKNV
LFWTTSYLIT LAVTFYIHSE VAESMFLLGF LSDRVVNRMS LIIVVAIMCL FVVVRVVVNV
KRAIFVFVVS VVLIFVHICL GIVQFNSFVN VVLFDVYAVF TALLTPQPVV AIIMLLLFDT
KMLMSFAFIV IVLSFRVFKD YKFVKVLHNF CNFDFVLSQV SLFRYRHRNQ GNDPTHYEAL
WLFLKELYYG IQDAKYEVFS PQAGSYNVKF LTDMTEQDQL EAVEQVQRRL QRFNIVQDKA
SPRLVLYSKT IEFIKDQIQQ QRAVGANPFI ITTLTSNDIG LDNVEVHNPA NFKPEDLQAH
MWFFSKSPVF IGQVPIPTNV QTAAVLDTTY NCQDLTADEK NNVAATLQIQ NAAITLSLFE
KCTQFLESEL GEVPTLMWQA EDVADIKHLE SQIENLRKVL DGMQFGTTEY KATRKQLNIC
QSQLDQAKAF ERKLAKFLEK VDQQQAITNE TAKQLSAFKN LVKQVYESYM SSLKVKVLEA
NDASCLLTST DLPRKLVLMR PITGVDGIKI VEKANGCEIT AFGTTFNTGH GSNLAGLAYS
TTQPLSAYPF IFNLEGIFKQ QANIGYKTVE CNMSSHNGSV LYKGKVVAVP SDDNPDFVVC
GKGYKLDCGI NVLMIPSIVR YITLNLTDHL QKQSLKPRRR LQYRQQGVRL GGVNLGEHQA
FSNELISTVG YTTWVSSTVC RDNTHKHPWF VQIPVNEKDP EWFMHNTQLK DNQWVVDLKP
THWLVNADTG EQLFALSLTD EQALKAEAIL QKWSPITQDV ECWFKDLKGY YTVSGFQPLW
PVCPVNICNV RLDPVFKPQS IVYADDPTHF LSLPVVNKNF LAAFYDLQEG FPGKKQVAPH
ISLTMLKLSD EDIEKVEDIL DEMVLPNSWV TITNPHMMGK HYVCDVEGLD SLHDEVVSVL
REHGIACDQK RLWKPHLTIG ELNDVSFDKF KDFAISCKLE DCDFVKLGAP KANARYEFIT
TLPLGDFKLL RGAWSACRHL CFQNGAYQSS RSKHYIDLAT EYNAGIVKVN KSNTHSVEYQ
SKRFMIKRVK DQSEFALAKT AFLPSIIPHH MEKQNGEWFL IRGPTSQWSL GDLVYAIWLG
DQDYLSECGF VFNPSRDEFL DDANQRSFLA NLLEPAILNF SHIYWQVKMC KVPYKLTLDN
VDLNGQLYDF GDYPCPNSVD NQSALFVLAE VWSMTRRPFP VAFARLLANE MEIPTDYQMF
FQNILLSGSY LDKALCLNNV RPFLSDPANL TTTPFFSQHN GVWTHFYNPI YGLVECNLDE
FAELPEVLQQ LVTVQGPITN NMTPAISVGE GVYAANVPSA SATKQKIPFY DVGLCQELTD
AGVDCGEAFK YFYYLSNPAG ALADVCYYDY QGTGFYSPKL LAGVYDFMKR VTECYRINER
FTYEQAKPRK SSMGINITGY QQDAVYRALG PENIARLFEY AQKAPLPFCT KIITKFALSA
KARARTVSSC SFIASTIFRF AHKPVTSKMV EVAQNSGGFC LIGVSKYGLK FSKFLKDKYG
AIEGFDVFGS DYTKCDRTFP LSFRALTAAL LYELGEWDEK SWLYLNEVNS YMLDTMLCDG
MLLNKPGGTS SGDATTAHSN TFYNYMVHYV VAFKTILSDL SEGNKVMRIA AHNAYTTGDY
QVFNTLLEDQ FQTNYFLNFL SDDSFIFSKP EALKIFTCEN FSNKLQTILH TKVDQTKSWS
TKGHIEEFCS AHIIKTDGEY HFLPSRGRLL ASLLILDKLS DVDIYYMRFV AILCESAVYS
RYQPEFFNGL FQVFLDKVQQ FRKDYCCDPC PPQLLEREFY ENLVFTSNSE VGIVDCYLEN
FKLQCEFKQQ ANFDKVCFCC PNPAVSVCEE CYVPLPLCAY CYYVHVVISN HSKVEDKFKC
FCGQDNIREL YIVLNNSICM YQCKNCVESD RLRISLLSDV DQIVRLPGFK SNSASIAKNG
VAQLLTSVDN VDVSLDWNYQ ESVQQNVARI VYHSANMTQM SIEVVYVSFT LVRNDGSSAI
LDIPNFKCPD TSYCLFYKPG KSGVLKFTGK GTLTSCYDNK NLTWFKVTCP DFNQPWRLAT
CFVIQQHDVV YPPIKATQYE NVTFVMGPPG TGKTTFVYDT YLSKASSSNR FVYCAPTHRL
VGDMDEKVDG AVVVSAYNDR TYRNPVWNKD DSYGVLLCTH NTLPFIKSAV LIADEVSLIP
PHVMIKILSM GFKKVVLLGD PFQLSPVYKN HKVHFKYDTF YLLQLATQKR YLTACYRCPP
QILSAFSKPY CDVGVDLVSF NNKPGKFDII VSKQLANIQD FSVLSVLSKE YPGYVILVNY
RAAVDYAMQN GLGDVTTIDS SQGTTAANHL LVLFGASNFS KTVNRVIVGC SRSTTHLVVV
CCPELFKHFQ PILNWPEPKY RYFGMEKQSD FNIIPEVSSL VFCDIEFWHY KADPNSKTRT
VYPGQIAVVT SQTLQLYLGV FDDTGYKSAL RGLPKDVYVP PNWVWMRKHY PSYEQHAYNM
QRLFKFIIDT TFGQPWFILY SCSNDLKSLK FYVEFDTCYF CSCGEMAICL MRDGNYKCRN
CYGGMLISKL VNCKYLDVQK ERVKLQDAHD AICQQFHGDS HEALCDAVMT KCLYLASYEA
AFKDTIHVKY KDLCLEIQYK ITSSFVRYDS VHKRYLYRDH GAMYYFRTPR SPMQNVYKYE
VGSHAEYSIN ICTSYEGCQS FGKTCTKCIH IHCIVEQFMA DERFKEFILV SVVKSDYVEQ
ALSPAAKALM LTVTKVEDKS FYISNGVRYD LYDYDLSKSV MRVVNSNVKP LPLYSVIVGL
GINCTVGCVL PNVPMKLKDE LLITDVPLST LRLDLQTWYY ISWPTLSNKN SRWKLAGAQV
YDCSVHIYIE ATGEQPLYYL QQGKGESLFE LPDTLFSTGR LYNLDHDAAQ NFNVKQLAIE
TMPNNHHVFS GDFTEVGTDI GGVHHVVALN GYKGSIIPNY VKPIATGLIN VGRAVKRTTL
VDVCANQLYE KVKQQLEGVK VSKVIFVNID FQDVQFMVFA NGEDDIQTFY PQKDFVRSYY
EWPNILPQIE SHYDLKNYGQ NPTFMPQPVN FAKYTQICTF IQDHVKVARN ALVWHLGAAG
VDGCSPGDIV LSSFFKECLV YSWDIKDYST LLDKHSYDCN FRPNLIVSDI YNVSSNVSEV
LDDCVHRLAL GGTIVFKTTE SSRPDIQLSQ FTKYFSAVQF FTAGVNTSSS EVFVVLKYKL
YSEPIGEELC SPNILSRIAA YRNKLCIVPN FKVFSTSFSY KYSGVKFVQK CFYVSVPRQF
CASGLIQEVP MLCQMEH
//
