R1AB_BRV1
ID R1AB_BRV1 Reviewed; 6733 AA.
AC P0C6V8; Q3T8J1; Q3T8J2; Q9YP98;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 EC=3.4.22.-;
DE AltName: Full=Papain-like proteinase;
DE Short=PL-PRO;
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 Breda virus 1 (BRV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus;
OC Renitovirus.
OX NCBI_TaxID=360393;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16137782; DOI=10.1016/j.virusres.2005.07.005;
RA Draker R., Roper R.L., Petric M., Tellier R.;
RT "The complete sequence of the bovine torovirus genome.";
RL Virus Res. 115:56-68(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6380-6639.
RC STRAIN=GC32;
RA Gu M., Petric M.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The 3C-like serine proteinase is responsible for the majority
CC of cleavages. {ECO:0000250}.
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=P0C6V8-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6F4-1; 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.
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DR EMBL; AY427798; AAS17963.1; -; Genomic_RNA.
DR EMBL; U50390; AAD11480.1; -; mRNA.
DR MEROPS; S65.001; -.
DR PRIDE; P0C6V8; -.
DR Proteomes; UP000000355; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; cd21413; unc_tv_SF1_Hel-like; 1.
DR CDD; cd21403; ZBD_tv_SF1_Hel-like; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
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; 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; 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 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; SSF142877; SSF142877; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
DR SUPFAM; SSF56672; SSF56672; 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 2: Evidence at transcript level;
KW ATP-binding; Endonuclease; Exonuclease; Helicase; Host membrane; Hydrolase;
KW Membrane; Metal-binding; Methyltransferase; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; Reference proteome; Repeat;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Transmembrane; Transmembrane helix; Viral RNA replication;
KW Zinc; Zinc-finger.
FT CHAIN 1..2753
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283859"
FT CHAIN 2754..3131
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283860"
FT CHAIN 3132..3418
FT /note="3C-like serine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283862"
FT CHAIN 3419..3677
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283863"
FT CHAIN 3678..3854
FT /note="Non-structural protein 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283864"
FT CHAIN 3855..4036
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283865"
FT CHAIN 4037..4121
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283866"
FT CHAIN 4122..4274
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283867"
FT CHAIN 4275..5286
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283868"
FT CHAIN 5287..5844
FT /note="Helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283869"
FT CHAIN 5845..6174
FT /note="Exoribonuclease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283870"
FT CHAIN 6175..6318
FT /note="Non-structural protein 13"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283871"
FT CHAIN 6319..6468
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283872"
FT CHAIN 6469..6733
FT /note="Putative 2'-O-methyl transferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283873"
FT TRANSMEM 2191..2211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2219..2239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2266..2286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2411..2431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2521..2541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2546..2566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2769..2789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2937..2957
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2986..3006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3022..3042
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3422..3442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3456..3478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3486..3506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3514..3534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3538..3558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3573..3593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3598..3613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1633..1814
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1821..1969
FT /note="Peptidase C28"
FT DOMAIN 4442..4673
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4981..5132
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5287..5368
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5509..5688
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5689..5848
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5846..6059
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6327..6467
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6469..6733
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT REGION 2183..2565
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2769..3042
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3430..3613
FT /note="HD3"
FT /evidence="ECO:0000250"
FT ACT_SITE 3184
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255"
FT ACT_SITE 3222
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255"
FT ACT_SITE 3291
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255"
FT ACT_SITE 5860
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5862
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5961
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6037
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6042
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6647
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 5293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 6025
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6029
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6033
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6048
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT SITE 2753..2754
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 3131..3132
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000250"
FT SITE 3418..3419
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000250"
FT SITE 3677..3678
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 3854..3855
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4036..4037
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4121..4122
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4274..4275
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 5286..5287
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 5844..5845
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 6174..6175
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 6468..6469
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 6733 AA; 765975 MW; 7947CE8F5F1FA90D CRC64;
MSKTSRELTN ETELHLCSST LDLISKSQLL AQCLGTPQNL VSLSKMVPSI LESPTLEPRY
TSTHSSSLQS LQLLALNTSS TLYKWTTGSI SKLRGHLERE LCRGLVPLND FIPKGNYVEL
SLMIPSVLTG QGTSTTTTLQ EMCSDMVQSC IKSMETDLLK GVLALKDQTS CQEYFLSANY
QSLIPPQPLV NAMRMSSVVD LSPLILENTR LLLKLSPFHG GTSVSYTSMI REFVDCSRRD
EKCLKRRLTK KQKRQEEGSF DANKVITLGG KMYRYRVVIL KCSDEVDDLI GFDGKVGEFD
YNFENVPHCW RDLVKRRCLI RAKATWNLAG GVDENLDHVY IDESQXDFRC ADGSSDSPSA
CVEDPHLEER IFSRVWLKQT SRFFGTKIQQ VSELFKSIGL PELETTYCGV NPVKVGNKWL
SFRDQGRSRV FFVYTDSNVY LATTRQKVCC DYILTKFKSV KWIGNKPDQC RVVKVLAWLI
SVNKVKNCTR VITPMLTVQG KISHRRVDYL DISVLDSYVS DTAGLNCVQK VKKFLSMYYN
CGADLGLLDN FLTPIECGTK QLVFERCNCP NHQFYVAQFD NHVVLGLGRP TGVVYPEEIP
SCANIYAVGF ATQKRVVEVH YYSEMDRHQL PQDYYYFAYD QEFQHVGGDD YVNHHLDDVE
DQPFPPVLFD DVYDSGDSLD DGGSDLDCFD VGYDFFWPEA PIPVPSPYGY YQGQRLRDLC
VAGGDFGCDC PRCDGTFIYH PFRPRHYHSF DEVGPFIQMC EFTLTYSGQN YNLFYGLEPK
VCLQDLVEAS DKLLQLLVRG QLENISLPND ILACLSSLKL GANIHPFLWP APFFNANGEW
VDIFGGGDFT VFGEDFCLKA KSMVESVYFL VENFFSVDCP IGNLYCNLHL DGDVKKMLWS
TIHMKYIYLA LIHSEKVFNI ILNSRQLSHQ ELVKLVIIGT FDVSIVAPCA CSGDCNHGKV
YNWTNLLSSV YRFVTLDQLV GLSYCEKRSL VLRKVQQYLE VEEGYQRPVQ LLMAPFYGFN
DNAEPDEQPL TGVFHQQVMQ MFDTCVMLDV ICGLKRPRAS VYNLFGVLAD YFRRPFTFRY
YQVAEFSGSE STQVFTDVTS ALTSKDPCSN RPYIYHDYAV CRVVEPRTAA VTTRGAIYPP
EVIEMIRSYL PIEFDVGVMN YVDGNCDFKY CNLEFCLSGR GLVKLDTGEL LDYKTNLFVV
RYKTLPLLYV TSNPIYLSDF SLDNAVCLTG DFKLSFDVEP GSTLFGLYFT NGRCYRDVWE
TLPRFGLGTL SPPKCHSKCE PFENLAEVFF FKRRVQLVPL VNNYTPVFRH RPDIPKVLTV
ELMPYYSSIG YQGFVAPKCV LPGCVATQYC KLRHQLDRCV QVTKLAVAYA FYFKPLNIGS
LYHLDPMRGT SYGKPAVVQF EPVGLIKEVN ILVYQFGKHV AIHYFPECPT YVAYGHYPSH
SVGVWLGYLP SVEECVIAQR NYRVYVPTCF RLSRTGCYHI QQDEDFERTH ITVSYHYARD
FDTKSLTPMF QMFSKIFGKS KQDLICALNS LSEESQSVLT LFCEEFDSAY TLQTISDEVS
FETSTSPELV ACVLAYAIGY ELCLTVKTDG ECESLDVGSS LEQVYVDYDV SKNVWDLSTH
LQDDSSDDLE LPFNQYYEFK VGRASVVLVQ DDFKSVYDFL KSEQGVDYVV NPANNQLKHG
GGIAKVISCM CGPKLTSWSN NYIKQYKKLG VTCAIRSPGF QLGKGVQIIH VVGPKSADSD
VVNKLEASWR SVFQNVKPDT TVLTSMLSTG IFGCSVTDSA TTLLSNLVDL DKDVVVFVVT
NVSDQYIEAL GVVESFQSAH GLPNFGNTCW FNALYQLLKS FAVKEQIVQD LVNCFDDFYE
CPTRQCVEWV CDQLGVVFGE QYDAVEMLVK IFDVFKCNVR VGYDCLARLQ QVALGSCREV
PADAVLMFFG QDKSGHWVAA RKVCGVWYTF DDKVVVKKDP DWSKVVLVLR ERGLFKATDF
ETPRPRRRRV AYRVPRDTIS QDAIMFLEER QFSSGTMLAH SCVESVESFH VEGVQPSPLQ
SVDGLDDVAD LSCDNHVCDN SDLQEPQVVV SQPSEVLTTS MSIECPVLEN SECSVETDLN
PVCEENEQVG ESGIKEQDGV TTSDSQQVFS KSLDPIIKQH EVESVEPQDL PVFSQQPQVM
LSMTWRDVLF QQYLGFKSDL LSLTHVNKFK IVVYLMVLWF VLLYCFSDFS LLSRFCLYVF
LLWLSHVVLV VKKLDLGLVN SGGESYVLRI LSSVKVPNCI AFNCDGVHWL ILKLLFYSFH
FYDFFVKTLV VVFQMPQLRC FTWPLLKLGF ADTFLSHHIL AFPTKQVSQS CLPVFGDERK
YIYVPYWCKE SFRTLVARAK QLTATGRTKT LDNWHYQCCS KTVKPSSCFN VRDFVFDDAC
NNHKHYGFFS ALWFYVVFYS GFVSFWLPLM FCYCALFMCT FKNLPVNITR PIRWTVLQQV
VDDLLSIITK PLFGRPACPP LSAYLTATTA DEAVRASRSL LGRFCTPVGF QQPIMNVENG
VAVSSLGFIN PLMWPLFIVV LLDNRFVWFF NVLSYIMLPV FVIILFYFYL RKICGCVNVK
GVVKNCTRHF QNFSKPLVAA GVHGNRTNFT YQPMQENWCD RHSWYCPKEE HYMTPEMAMF
IKNYYNLATS PMADTIWCDY VKSVPNMTWA NFKFSLFKSN ETVMCGPSSH ADSMLLSWYA
FLHGIRFAVN PSVIDIPSQT QPIYVSSDSD DSLDKGCDVS LRPTKNKGKF KKQSVAYFSA
GPVDLWYYVM LIIALGAIFV FMYSCFMVGQ YVVMPRDKFF GVNPTGYSYV NAQPYLHASP
PVLRNSDGMV LATPLKVPSI SYSVYRLLSG HLYFTKLIVA ENECTPPFGA XRLSHEFTCN
DFTYILPAHL RIFGRYIMLI HPDQLHMLPF EVEHSTHTRL CYVTGTNIVE CLPTFEIISP
YVFVVLVAIF TIVFLFLLRM YIVMYSYFKV FTYVVFKLLF VNTVMVLFVV CLPPLVPGVV
FVLALWLCDS VVFLLYLAVL SLFILPWFYV MLFVLIVGGF VFWWMMKSSD VVHLTPDGLT
FNGTFEQVSK CVFPLNPLIV NRLLLDCRMS HSDLVEKSKL KTTEGKLATE MMKVFMTGET
AYYQPSNFSF QSVFSKVVSP FTLHARPPMP MFRLYVYFNG QCVGTTCTGT GFAIDDSTIV
TAKHLFECDD LKPTHLSVEL SCRSYWCTWK EPNVLSWKFE GENAYISVEN LRDFYGIDFK
YLPFQQIECE FYKRMEAVTI YSIKYGSEFA TQAWQTVNGH FVCCNTEGGD SGAPLVWRDS
VIGVHQGLCD SFKTTLASDS KGVMMTEVKG YHVDPPVYYK PIIMSAAYNK FVADSDVSVG
ECTNYHNFVN EDFFSMHDEL EKVSFGDKMF RYCQSLPRYL EPLHYFHVPS FWQPFKKQSV
SSNVSWVVEN LHFIFSVYFL VCDFVAYWWL DDPFSVVLPL FFVVQLLSTV VLKNVLFWNT
SYLVTLAVTF YVHSEVAESM YLLGLFSDQI VNRVGLILVV SVMCLFVVVR VVVNVKRAIF
VVVVSVLLIV VNVVLGVVQF NSLVAVCMFD IYAVFAALLT PQPVVAIMML ILFDTKCLMS
FAFVVIVLSF RVFKNYKFVR VLHNLCNFDF VLTQLSLFRY RHHNQGNNPS HYEALWLFLK
ELYYGVQDVK YEVFSPQAGT YNVRFLTDMT EQDQLEAVEQ VQRRLQRFSI VQDKNSQRLV
LYSKNVDFLR SQIQHQRVLG ANPFIITTLT PKDIAIDNVE VHNPSQFKPE DLQAHMWFYS
KSPIFVGQVP IPTNVQTAAV LDTTYNCQDL TADEKNNVAA NLQIQNAALT LSLFEECNRF
LESELGDVPT LMWQSEDVVD VKQLEVQIEK LRVVLDGMQL GTSEYKATRK QINILQSQLD
KALAFERKLA KFLEKVDQQQ AITNETAKQL SAFKNLVKQV YESYMSSLKV RVVESNDASC
LLTSTDLPRK LVLMRPITGL DNIKIVEKAN GCEITAFGDT FTTGLGSNLA GLAYSSTQPL
SAYPFIFNLE GIFKQQANIG YKTVECNMSS DNGSVLYKGK IVAVPSEDNP DFVVCGKGYK
LDCGINVLMI PSIVRYITLN LTDHLQRQSL KPRRRLQYKQ QGVRLGGVNL GEHQAFSNEL
ISSVGYTTWV SSTVCTDKSH KHPWFVQIPS SEKDPEWFMH NTQVKNNQWV VDAKPTHWLV
DADTNEQLFA LALTDEEYLK AESILAKWSP ITQDVECWFK DLRGYYTVSG LQPLWPVCPK
KICSLKIVPI FQSQSVAYAD EPTHFLSLPV VNKNFLEAFY ELQEGFPGEK QVAPHISLTM
LKLTEEDVAK VEDILDEMVL PNTYATITNP HMMGQYYVFE VEGLQALHDE VVSVLRQHGI
ACDQTRMWKP HLTIGEIKDG SVFNKFKDFG ITCKLEDCDF VKLGAPKANA RYEFIATLPV
GDFKLLRDVW CACRHLCFQN GAYQSSRSKH YIDLATEYNA GIVKVNKSNT HSVEYKGQRF
MIKRVKDQHE FALARTAFLP SIIPHHMVHQ NGEWFLVRGP TTQWSLGDLV YAIWLGDQAY
LDECGFVFNP SRDEFLDDAN QRSYLANLLE PAILSFCEIF HCVKGCQVPY KITLDNLDLK
GQLYDFGDYP CPNKVDNQSA LFVLAEVWSM TRKPFPTKFA QVLAKEMNVP ADFQMYFQHT
LLSGKYFDKA MCLNNVRPLL RDPANLTTTP FFSQHSGVWT HFYNPIYGLV ECDLEEFSNL
PEVLQQLITV QGPITSAMTP AISIGEGVYA ANVPPVAAAK QKIPLYDVGL CQELTDAGVD
CGEAFKYFYY LSNPAGALAD VCFYDYQGTG FYSPKLLAGV YDFMKRVTTC YKTDERFTYE
QAKPRKSSMG INITGYQQDA VYRALGPENI TKLFEYAQKA PLPFCTKIIT KFALSAKARA
RTVSSCSFIA STIFRFAHKP VTSKMVEVAQ NSQGFCLIGV SKYGLKFSKF LKDKYGAIEQ
FDVFGSDYTK CDRTFPLSFR ALTAALLYEL GGWEEDSWLY LNEVNSYMLD TMLCDGMLLN
KPGGTSSGDA TTAHSNTFYN YMVHYVVAFK TILSDLSDCN KVMRIAAHNA YTTGDYGVFN
TLLEEQFQTN YFLNFLSDDS FIFSKPGALK IFTCENFSNK LQTILHTKVD LTKSWATTGH
IEEFCSAHII KTDGEYHFLP SRGRLLASLL ILDKLSDVDI YYMRFVAILC ESAVYSRYQP
EFFNGLFQVF LDKVQQFRKD YCCDPCPTQL LDRQFYENLV FTSNTEVGLV DCYLENFKLQ
CEFKQQAGFD RVCFCCPNPA VSVCEECYVP LPLCAYCYYV HVVISSHCKI EDKFKCPCGQ
DDIRELFIVL NNSICIYQCR SCVESDRLRI SLLSDVDQVV RLPGFKANSA SIAKNGVAQL
LTPVDNVDVS LDWNHQETVQ QNVARIVYHS ANMTQMSIEV VYVNFSLVRN DGSSAILDIP
NFKCPDTSYC LFYKPGKTGV LKFTGKGTLT SCYDSNNLTW FKVTCPDFNQ PWRLATCFVI
QQHDAVYPPI KSTQYENVTF VMGPPGTGKT TFVYNTYLSK ASPSNRFVYC APTHRLVGDM
DEKVDGAVVV SAYNDRTYRN PVWKKDDSYD VLLCTHNTLP FIKSAVLIVD EVSLIPPHVM
IKILSMGFKK VVLLGDPFQL SPVYKNHKVH FKYDTFYLLQ LATQKRYLTA CYRCPPQILS
AFSKPYCDVG VDLVSFNNKP GKFDIIVSKQ LANMQDFSVL SVLSKEYPGY VILVNYRAAV
DYAMQNGLGD VTTIDSSQGT TAANHLLVLF GASNFSKTIN RVIVGCSRST THLVVVCCPE
LYKHFQPILN WPEPVYRYFG MEKQSDFNII PEVASLVFCD IEFWHYKADP NSKTRTVYPG
QIAVVTSQTL QLYLGVFDDA GYKSALRGLP KDVFVPPNWV WMRKHYPSFE QHAYNMQRLF
KFIIDTTCGQ PWFILYSCSN DLKSLKFYVE FGTNYFCSCG ELAICLMRDG LYKCRNCYGN
MSISKLVNCK YLDVQKERIK LQDAHDAICQ QFHGDSHEAL CDAVMTKCLY LASYDAAFKD
TIHVKYKDLC LEIQYKITSP YVRYDGVNKR YLYRDHGAMH YFKTPKSPMQ NVYRYEVGAH
TEYSINICNS YEGCQSFGKT CTKCIHIHCI VEQFMADDRY RDFILVSVVK SDFVEQALSP
AAKALMLTVT RVEGKSFYTS NGQRYDLYDY DLSKSVMRVV GASVKPLPLY SVVVGLGINC
TVGCVLPNVP MKLKDELLST DVPLSTLRLD LPTWYYVTWP TLSNRTSRWK LAGAQVYDCS
VHIYVEATGE QPLYYLQLGN GESLRELPET LFSTGRLYNL EHDPSKNFNV QQLAIETIPK
NHHVFAGDFT DVGTDIGGVH HVVALNGYKG SIIPNYVKPI ATGLINVGRS VKRTTLVDVC
ANQLYEKVKQ QIAGVKVSKV IFVNIDFQEV QFMVFAKGED DIQTFYPQKE FIRSYYEWPT
ILPELESHYD LKNYGQDPQF MPQPVNFAKY TQICTFIQEH VKVARNSLIW HVGAAGIDGC
SPGDIVLSSF FKECLVYSWD VKDYDTLLEK HNYDCNFRPN LIVSDVYNVS SNVSEVLEDC
VHRLALGGTI IFKTTESSRP DIQLSKVTKY FAAVHFFTAG VNTSSSEVFV VLKYKLHSEP
IGEELCSPNI LRRIAAYRNK LCIVPNFKVF STSLSYRFSS VKFVQKCFYV SVPRQFCASG
LIQEVPLLCQ MKH
