R1AB_WBV24
ID R1AB_WBV24 Reviewed; 6872 AA.
AC Q008X6;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=nsp9;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=nsp10;
DE Contains:
DE RecName: Full=Exoribonuclease;
DE Short=ExoN;
DE EC=3.1.13.-;
DE AltName: Full=nsp11;
DE Contains:
DE RecName: Full=Non-structural protein 12;
DE Short=nsp12;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease;
DE EC=3.1.-.-;
DE AltName: Full=NendoU;
DE AltName: Full=nsp13;
DE Contains:
DE RecName: Full=Putative 2'-O-methyl transferase;
DE EC=2.1.1.-;
DE AltName: Full=nsp14;
GN Name=rep; ORFNames=1a-1b;
OS White bream virus (isolate Blicca bjoerkna L./Germany/DF24/00) (WBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Tornidovirineae; Tobaniviridae; Piscanivirinae; Bafinivirus;
OC Blicbavirus.
OX NCBI_TaxID=766180;
OH NCBI_TaxID=58317; Blicca bjoerkna (white bream).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16987966; DOI=10.1128/jvi.01758-06;
RA Schuetze H., Ulferts R., Schelle B., Bayer S., Granzow H., Hoffmann B.,
RA Mettenleiter T.C., Ziebuhr J.;
RT "Characterization of White bream virus reveals a novel genetic cluster of
RT nidoviruses.";
RL J. Virol. 80:11598-11609(2006).
RN [2]
RP CHARACTERIZATION, ACTIVE SITES, AND MUTAGENESIS OF HIS-3492; ASP-3509;
RP ASP-3518 AND SER-3589.
RX PubMed=21068254; DOI=10.1128/jvi.01716-10;
RA Ulferts R., Mettenleiter T.C., Ziebuhr J.;
RT "Characterization of Bafinivirus main protease autoprocessing activities.";
RL J. Virol. 85:1348-1359(2011).
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;
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=Q008X6-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=Q008X5-1; 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. Two distinct
CC N-terminal and C-terminal processing sites can be used, potentially
CC resulting in four different processing products. The preferential
CC autocatalytic cleavage sites are displayed. The polyprotein is
CC certainly cleaved into more products, like in toroviruses.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
CC ribosomal frameshifting at the 1a-1b genes boundary.
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DR EMBL; DQ898157; ABI97394.1; -; Genomic_RNA.
DR RefSeq; YP_803213.1; NC_008516.1.
DR MEROPS; S75.001; -.
DR PRIDE; Q008X6; -.
DR GeneID; 4443112; -.
DR KEGG; vg:4443112; -.
DR Proteomes; UP000000680; 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 CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21403; ZBD_tv_SF1_Hel-like; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.150; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR044336; SF1_Hel_ZBD_tv.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF53335; SSF53335; 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; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Endonuclease; Exonuclease; Helicase;
KW Host membrane; Hydrolase; Membrane; Metal-binding; Methyltransferase;
KW Nuclease; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Reference proteome; Repeat; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication; Zinc; Zinc-finger.
FT CHAIN 1..6872
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000408881"
FT CHAIN 1..3071
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408882"
FT CHAIN 3072..3442
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408883"
FT CHAIN 3443..3709
FT /note="3C-like serine proteinase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000408884"
FT CHAIN 3710..3985
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408885"
FT CHAIN 3986..4157
FT /note="Non-structural protein 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408886"
FT CHAIN 4158..4375
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408887"
FT CHAIN 4376..4452
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408888"
FT CHAIN 4453..5396
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408889"
FT CHAIN 5397..5951
FT /note="Helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408890"
FT CHAIN 5952..6314
FT /note="Exoribonuclease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408891"
FT CHAIN 6315..6462
FT /note="Non-structural protein 12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408892"
FT CHAIN 6463..6604
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408893"
FT CHAIN 6605..6872
FT /note="Putative 2'-O-methyl transferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000408894"
FT TRANSMEM 2542..2564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2571..2593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2644..2664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2744..2764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2773..2793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3079..3099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3247..3267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3278..3298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3319..3339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3725..3745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3751..3771
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3789..3809
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3813..3833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3844..3864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3888..3908
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3911..3931
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1637..1827
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 4551..4779
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 5090..5245
FT /note="RdRp catalytic"
FT DOMAIN 5397..5479
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5623..5801
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5802..5958
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5962..6186
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6464..6601
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6613..6872
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT REGION 159..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2037..2112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2293..2683
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2889..3156
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3546..3732
FT /note="HD3"
FT /evidence="ECO:0000250"
FT COILED 4212..4250
FT /evidence="ECO:0000255"
FT COMPBIAS 159..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3492
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000305|PubMed:21068254"
FT ACT_SITE 3518
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000305|PubMed:21068254"
FT ACT_SITE 3589
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000305|PubMed:21068254"
FT ACT_SITE 5980
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5982
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6086
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6729
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6758
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6790
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 5401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5649..5656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 6101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
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 6161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT SITE 3071..3072
FT /note="Cleavage; by 3C-like serine proteinase"
FT SITE 3442..3443
FT /note="Cleavage; by 3C-like serine proteinase"
FT SITE 3603
FT /note="Substrate binding"
FT /evidence="ECO:0000255"
FT SITE 3709..3710
FT /note="Cleavage; by 3C-like serine proteinase"
FT SITE 3985..3986
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4157..4158
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4375..4376
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 4452..4453
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 5396..5397
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 5951..5952
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT SITE 6313..6314
FT /note="Cleavage; by 3C-like serine proteinase"
FT /evidence="ECO:0000255"
FT MUTAGEN 3492
FT /note="H->A: Loss of proteolytic processing."
FT /evidence="ECO:0000269|PubMed:21068254"
FT MUTAGEN 3509
FT /note="D->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:21068254"
FT MUTAGEN 3518
FT /note="D->A: Reduced proteolytic processing."
FT /evidence="ECO:0000269|PubMed:21068254"
FT MUTAGEN 3584
FT /note="T->A: Reduced proteolytic processing."
FT MUTAGEN 3589
FT /note="S->A: Loss of proteolytic processing."
FT /evidence="ECO:0000269|PubMed:21068254"
FT MUTAGEN 3603
FT /note="H->A: Loss of proteolytic processing."
SQ SEQUENCE 6872 AA; 769510 MW; B9ECD1AE5CF8F93E CRC64;
MSILFGNRQA NATKRSDMAS VARAVYEVDL ISTKYARRTQ ERLAHNKHAK PSYPSVFFGR
RMKAVKEPTF TPSTLFFEEA TLPKVLASKA KPDTGIKTRR VYVADSLTIN GHTYPIVGHF
VEMAVSKKEA FPIQPKRVKP KPLMAKPIPN IRRTFLTPEE RTNTPTTPTT TTTTPFVAGE
TAGPTIEYTP TSIDLPFAMP TVKQIKENAH TILREQDDCL RFAQTALFKH LGTVTHTTPN
HATTFQVKGR TSLLTFEWRK TTQSPLTDGH FYLQTANNHA ELMQPVEGKL TTIFTTTIQQ
GTTHSLHLIK QESARTLKTR KPLKLVTYKQ ETPTTTITPQ SLKKTITYIP GSFCINVAEP
TLQSVMRRQP LTPTPNDALL QIYHKLGCTT KSPNHASTFE LFGNTYTWYP VQHTNNLLHK
DPNRRFFLHI TGQTPQLLIR TERKTFLTLQ DEVTYISGKL FVMNHAPIQG EYKTQTAEWV
GSYNMAKTPK AIKPAKTVEY INTTPCHKPA TMPAPITYRQ CPYTWTLHEP SISKVQRNLF
HIPKTATNCL DRIQKALFPE IVTSNQHFPI GFTIQTDTTM QSYEWAILCK KVTRTYYLAV
QNHHATLWYK CAQVYMCLSD DIAPTTELQG SVYILNKVTD PGFYQNTRQW CGSNDDLHEP
KHLIKNLANG DVNNIAHCSL TPWTTTPLVY STQKNKLTRK LIHYYNATYT VQVPKENPNA
QPSTMKCAYK AYIDLATPTE LQIHLDLEIQ GKLYSQTAQK KGSKFNKLDI PTFGDILKGT
LYVFSSKVLL YEQPKRCTSV CFHLPNNAQS FFFNTETIQT FEDLFARISS EEVEDNLVLI
KGFVPCLGAI YITKDLKFIQ PELKEDFKHP TTYYTFTTTV DPEQVLYSLH PSFTDIVPPH
GFPYYTFAKL NNHIDAWNIT DDQADTLAEA QPIIFQWPTE EATITTPYKV LHYEHLEGLD
YISLSSFNTV ECPEETQSAH DSSSESESED EELPAHPLSN APSQASLSSV ASTAPPTSPT
SSPTPSPTPL QQQVGLKGKE VPVGGWVLVS EEETPSEEVD SPKLLPNEVP LSFDFDLPIE
PITRPISPEL QQPILTHYEH PTSPTPSVEI EIDFGSYENL TLQTEETVTT EVQPEPTPAP
TPEPTIVTET VQETPVPTET TQESTPESTP ESTPEPTPES TSESTLEPEH VATPSQSPTH
ITVTEITHEP ETPDSWSERY DSTSNIPEVF NQLSFGSTDS VKITTPKTET PDEPQQPTVE
TVSAAQQLLQ IVQTATPDIA QLMSELPPYR LICIGSYCPI LAENISKQLP TAVTTPTDAD
IPTVIFNVSE ETMDTVINTV KTKHQANHLT FSLTTIIALD VPKDKSLPLQ QIYDKLTQQD
YNTDFIYESH HRQPKESLTH ASVLSAYTAS YKTTAIKSIA DNAVVLDIGY GKGNDGPRYA
VRPLTVTGID TAARMLAIAD QNKPENVTLV KQGFFTHITK TSNTYTHVIA FNSLHYPLAS
SHPDTLVQRL PTCPANILIP CHHLLEGIQT PTYSVVKDED MWCVKVTKNE FIESSYNYDV
FVKALESKYH VTIGSLLDCV EKPSTRSITP TLWTAMRNFV NNDQEMQRIL SGYITFNLTP
LPPKVEIIND WLDNNATVTI NNPFASNEGV TFAVHNIGAI TTTEGEFIVN AANKQLNNGT
GVTGAIFAAH DKELKLTQAI KALPTYGASD KLESHQHVVQ TIIKNNNSTH AINILHAAAP
IKVKCTSKNP EVLLAHNETA QSELKETYKA IVDYAQLNKL THIYLPLFGA GAYGHKPLDS
LEAFLDAMRN RSPQSTTQYT LLLSDPVKPL DNPSFSYEFL NLLVTNLNIN KQFAQLIVNK
YHNTCALQSA IQMNTTTDTH NFLATFIYLL YTMPYSMNTF RQTHTPEEPF TPGKMVTVVD
TTIAFLTTLD ILPPCGQPCG YLPPSITKDG EYICACQKTS NWSLPFHFYN ARYNKVYHTG
LNNILTHKHS AFHKSRNAAH FIAKTGPSTS SYPVYMAPVP EILAYNASYR DSCQDNAIEE
QSDSQASQSP SSPVTIPVSL PTASPASSVK SALRSDIPIT TDQQSTTSAS ISTATTASTI
PTAPLTSSDS NTSVVTSLYG NMEELTYLDA SGTSQDFILS ETTPFIAHIY HNNEATFIPP
GYQLLDTNTN DPIEMYITPP RPIDGSPMIS LASTASTTPM TYPLLSIRLT TEELTSFFKT
KTDKFHLISH KSCLTVHLFD SPTLNSIAAD STSDAHLYQQ HLKDLYTFSD CCSMYTRTEV
YNCIEADTPL IRQSEQTKFH PINLDTLIEM VATFPPIVKR YSQTTTPDFT NLTVYFVSNG
DIITTPTGST SEQPPQLKIF LDYQTSSKFT TLVDLTLHEQ TEANTIITYH HGEHQLLKPN
PSAFYIEFQT YSSFFSRFQT FSTNFFWTLF INFLINVRFC ITADSAYFHW QGKPIETTNL
NIVYSIGRLD FVLSKHTTPW LTKPTDTLNP LTLIKNTLVQ PIAINFHGRI RPLQSTNTRF
GATHTPTKLP VHLLNTSLRT HYLSLLSLFQ CTFSVFLAYI ALLYSFSGHG IFTVVAYFTM
LFARYYITSF INFCTSQLTA TQVTQWFAAI KAKYTGIYES SQDRVLTVNV TGTNVPYIVK
YSTILTVTMY VAFMAFVWTV STYAAQYTAG ERYDRPPYQT VFQKTLNVLG LTETVTYYYP
YASLNEACAA STSILCRLGS PFNFHYPSDY TQVRTVQTDT SSPFWLFIIF MPPSFLFIVL
PWLILCTITP TVSIAQLLVP SIILNATIVF IYIRRKFTGH CCGPHTCIKH ADISRSLQFR
PTSQIQHSLT FCGTLCAKHN WYCNNSDSPT HTLGIQLAQL IETTYKLQPG TIKPDSSYTH
TTETATLPIM KVSTTSTDFT TSEPNTTVEH LHLQVIAHVT GTRISIESSS NKVQQQNTQH
TRLTNKPVTG FMHTTLLQKL KRQHKDELSS YLCNFVPSDN KKDCILPHSV VHMTLTENQR
TFLLKNFTFS TNVTVDPTTT GFIPSSLNIS TLPHKHFMIN VIESAMLAKL PKEVQDTLRT
THLETTTLER QAMSLTTQAI LTTFALIMAT FVVAFLAFFS TAQVGKTPYA GLNPTMVGNV
NAEPYIQPTT LENSILIPLH GASKVCWRAQ NGTLFFTDAI PTTECARAAV PYIGYKSEFT
QTCASSNLRY PFTVYLGSIK VMYLRDGISY LTSTLSHNSN TKKLCVQVGS NAVRCASVLP
TGASSNVAAL LMASVVVISM VLFYLYLLQI FKFYTNSVIM SFVIQLLTLL ATTVSTPLAV
TVQLFVITYG YTNWILLTLS LLNLTVLLST PVGITFVVIY GLYKAYTLFT SSGQGCVYNE
GGTIRFSGSF EQVANSTFPL TNASCVQLLS DLGITYQQLN VYASSRDRNV RRLAQALLHR
QLDSASECIL YEGCSGNTIT RQALQRIRQA VTVVVTPASQ NLCKITSNQA NGIGLSCTGT
FFTSTEIITC AHGIGTSDIT AVHKGITYDC KVKSINNDIA ILITTTVNLS VQNIKLDSSF
SQKSDNYQRN FVQFVSFVDQ QNSDAVTINN TVMLPSGHFF AIGTEAGESG SPYTLNGNII
GIHYGIDNAG SWMLASRPDG SFYVPATQHG NSAKVTFSTD AFAQQFPAIV TNKTSDQLVN
EIAATNNTAF ELDTTDVSHL SNLLKHLKNN NETPKSLSDY LPVAPVTQQT SVTVGQTLTS
PVNNMQTALY TLMLVSEVIT YILTPNSDLS VLISMFVTSA FLKFGASKLF YNTEMLRNTI
TTFVVYRYTT LLIALVFSQY YLHILSYALK LNTLVLTVIA LTFLVTPLVL LTIRRVYYYS
QNYLISCVFI ISCFASHTYT LYILTDTTVD FQTFIISEPI FSTLLCNLFI GFTLISVVPN
PLYVCVVFMY ILLDCEALGF IVTCFMASYL CPKPLRSLTT FLCTDTLVLT APAYLHWYGA
KGTQREYSVI YAVFDSILTP ETTIQIPVTI MEGIEQQVKF IFAVPKSANI QDEEEAYVEY
NQNSDIKDLA IKNEEKVCTI TGMFRKTRTI KGTLMESFYP RHQPDSYILN QVVRHNYVLA
HDPETIILTT VNPTHLESEP FQTIVKKVRK LHALYQEISE QSSDDTELCH AYILALIKST
VLEAQMPTEK INFVSSQTML SPAMILIFAE AYQILTESRS FTNHITPQSD IGSMQTTLAS
LAEMDTDEMT PQERKIHIKR MNVLKQEIAK MESASLKLEK FLDNMHKAEI SKRGKEDILL
KVSNMLRLHL NKVANAAHCT IQTPSAGLIT LASAFDVHSL CVTQHSESVL IQTPDDDTFL
VYVDGQIYTC YNPTDITGKK LVPINVMSPD NVQFPTYPVV FSLSKQDYAE EITEQNNIGY
TERTHNFKLK ELASGLAVTL DGLVVVTETK ELATAFKIGQ RYFKFLNTNK TPVARNNTHA
IIQLLRNNIS QQAVVRIGGS RVSNDHIAIS QVPVQTIGYL TYAGISVCRQ CATKQDHTCQ
YAGYFVQIPR EHVSNIFNLT DTPPCLHNKF TCTTCQPLQQ QSKTQQPPLN LVGQCLGLTL
DTAFCPFQTG EYKPSSREFY INILNNNVAS LRKVFKKNTA SIPSENGTIM LKDTGTAHEI
YVAKQLLAKG LPVLQHARFN HDGTDYLIRY YTTPYSLGDL VYAYMVGDFK HMLLALDITD
ETCLDPGNYS SYYNFKEQLR NKLASVIPNV NKILAAELPL AITLDNIDLN GFLYDFGDYP
TNGKVTNYHV VSCMRQIATF CSLDITQFPS PLGYTVDRPK LQQTLITGSY IDKLLAINAL
VASNPETPAT ASTLFIEASA PTTQTAAISN PILGMHVLDW DLIKANHTGV ELDLIQTQDP
SIYAKPDVLS VGDTIFYYGR RRYKHDAYKR PFYDLDLIQR MNSAGLNLSE TTGYHYQCGT
TTEAVEDFMY YNYNSPKSFD PSYLKSVYTY MRDKFMKIIS TDEKLNHQSG APRMSSMGVG
VSGFFQKTVW NALPEDFSPR LLDTASKTVM PFSTNIVKKF QRQKKTRVRT LGGSSFITSS
IFRMLHKPVT NKMVQTAQAN IGPFLIGISK FNLGFHKYLS AHHPNGIEDC QVMGADYTKC
DRSFPVVCRA LSAALFYELG HLEPNNHWFL NEMFAFLLDP SFISGHIFNK PGGTTSGDST
TAFSNSFYNY FVHLYIQYLT FLTTEMPPSY QPLCNLAHQA FSTGNTETYD LYFSMADDLN
STEYFLHFLS DDSFIISKPT AFPIFTPANF SMKLQNVLGC YVDPAKSWSA DGEIHEFCSS
HICKINEKYQ YVPDPNNMLA GLICAPEPTP QDKLIWKLVA TCAELAVFHF VNPTLFNNIF
HLLQSLHAEF VSEHSVNLLP PKLLEIDFYT DLIDSEDVEQ YSFLADTLTE KNIIMQSASQ
CYFCDNATVS TCSDCTVQYP MCAHCAYEHL MLTDHTPTQV LPCHVCDQTD PRHLNHTFVM
GTVKVACDNH VEGMALPLVD HARKLVKIPL YQKCEQQKTS VSAIKYTKLF DENDQPLDPN
FFFYDHEQSA EHNYLKILND CYLLDEHTVQ TSTTYDFQCL EGNTIQVFHK PAETFGNTAY
AEILDSKGRV VLKVTLDPIS AQNPNHYYIT TTKGVLYRKY SKIRRTIHKP RLANRHILNT
LKKATFIIGP PGTGKTTYVM KNFIDTASPA NKVAYIAPTH KLVQSMDQAI WDKYNHTVSV
SVVKSELNNN KYNYPLNSAT KTIMLGTPGA VCTHAGCTLI FDEVTLSQLN TIINAISVVK
PSQVIFLGDP LQLGPVTHMR SLSYSYTNFP LFQFCNDSRV LSICYRCPSN IFNLWVKPYT
DSNVRIDPHA AGGDAKIIVS DQCSNPDAYQ YVQKLARNNP DKVLLCNYKK PIIGLENAVT
IDSSQGKTYK HTIVVLLGNT NFTQVINRAI VAMSRSTHSI EVHCSPFIHT KFSELFGWPQ
NVEKENQITK QLHEYSVTSN ITLLPVSELP NHLGSLVVCD LEFFHVRHET TPKVKCTLEV
GEMAIITTSL LKQIIIPRKS AFTAETHHKH TFGVPKGKPD MNWDYMKSHK AISQQINTDR
THKIFSHMAA TTLNRVVYVL YGAGNDLRAL TNLNIVGDYT CEKCTKEATF YTIHREIVHT
FCNHHAPSQF PLMGTINAQA IDIQHASANK QSLTNTHAEV CNQQHGDAHT ASADTIMTGC
LASNFLMKSA IKLDNILTTS AFKPYAPYIQ TGSHLTVSSI KFRTLGTGVF SMIDDKLYHF
DILPHHSKLS HFLQHSSNQP HSTIVTEIPA GYPSCVKIKG KGCTFCANTI AVITELYEDL
AKLGLTLSRP IIQQAYTQVE TQILQNITNV SYNQFGEMLI QLKDDTVIPF INDFQTSIHN
YSLRSNQPLP NPAIFKNLGI KATLGFSTPW VPVTTTTTEP HIMSTKILKD NNDYYHLSPV
QLKASPHAFS SITAGYYIYT TPMINIPNET PAYYLTHFVH GQSTPLDLGY TSTNRLTTKQ
FIYTPNEDEY KSKLGHHVSV GDTSNVSWTI GGMHVLTAFQ NITNYQLVSG PANPIMRINV
ALERGNKVET TALDTTLQDY YKIATTNKVT VSKTTFFTLD GGQYRMMNFA NPDGTIQTSY
PVAQAQSQLI TNYRIYPSYI TWPTFFTNEA TDCWAIPNYN APPKNQTCNI NIQKYDQMCD
LFAIDLKIPV KGHIHHLGNA GNKYSPGDVV LRQYFDQAHL TSYDLREVVS DIPVLHPNDE
WKAHFILSDV YAPDTDFTSL ALEYMQNHLR LGGSIMWKMT ETSILQVNEI VKYFGSWKAV
TFAVNYSSSE TFLFCAGYTG VEYNTSIVQN GYMSLLGGYR KDLLFVPFCN DYTGSKAYKD
TGRVKVVANH LADKLTPAHY ATASIFLNTA LH
