POLG_CSFVB
ID POLG_CSFVB Reviewed; 3898 AA.
AC P21530;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=N-terminal protease;
DE Short=N-pro;
DE EC=3.4.22.-;
DE AltName: Full=Autoprotease p20;
DE Contains:
DE RecName: Full=Capsid protein C;
DE Contains:
DE RecName: Full=E(rns) glycoprotein;
DE AltName: Full=gp44/48;
DE Contains:
DE RecName: Full=Envelope glycoprotein E1;
DE AltName: Full=gp33;
DE Contains:
DE RecName: Full=Envelope glycoprotein E2;
DE AltName: Full=gp55;
DE Contains:
DE RecName: Full=Viroporin p7 {ECO:0000250|UniProtKB:P19712};
DE Contains:
DE RecName: Full=Non-structural protein 2-3;
DE Short=NS2-3;
DE Contains:
DE RecName: Full=Cysteine protease NS2;
DE EC=3.4.22.-;
DE AltName: Full=Non-structural protein 2;
DE Contains:
DE RecName: Full=Serine protease NS3;
DE EC=3.4.21.113;
DE EC=3.6.1.15;
DE EC=3.6.4.13;
DE AltName: Full=Non-structural protein 3;
DE Contains:
DE RecName: Full=Non-structural protein 4A;
DE Short=NS4A;
DE Contains:
DE RecName: Full=Non-structural protein 4B;
DE Short=NS4B;
DE Contains:
DE RecName: Full=Non-structural protein 5A;
DE Short=NS5A;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=NS5B;
OS Classical swine fever virus (strain Brescia) (CSFV) (Hog cholera virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus.
OX NCBI_TaxID=11098;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2162104; DOI=10.1016/0042-6822(90)90472-4;
RA Moormann R.J.M., Warmerdam P.A.M., van der Meer B., Schaaper W.M.M.,
RA Wensvoort G., Hulst M.M.;
RT "Molecular cloning and nucleotide sequence of hog cholera virus strain
RT Brescia and mapping of the genomic region encoding envelope protein E1.";
RL Virology 177:184-198(1990).
RN [2]
RP INDUCTION.
RX PubMed=9573242; DOI=10.1128/jvi.72.6.4775-4782.1998;
RA Sizova D.V., Kolupaeva V.G., Pestova T.V., Shatsky I.N., Hellen C.U.;
RT "Specific interaction of eukaryotic translation initiation factor 3 with
RT the 5' nontranslated regions of hepatitis C virus and classical swine fever
RT virus RNAs.";
RL J. Virol. 72:4775-4782(1998).
CC -!- FUNCTION: [N-terminal protease]: Leader cysteine autoprotease that
CC cleaves itself from the nascent polyprotein during translation of the
CC viral mRNA. Once released, plays a role in the inhibition of host
CC innate immune response by interacting with host IRF3 and inducing its
CC proteasomal degradation. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Capsid protein C]: Packages viral RNA to form a viral
CC nucleocapsid and thereby protects viral RNA. Also plays a role in
CC transcription regulation. Protects the incoming virus against IFN-
CC induced effectors. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [E(rns) glycoprotein]: Plays a role in viral entry. Interacts
CC with host RPSA that acts as a cellular attachment receptor for the
CC virus. Possesses also intrinsic ribonuclease (RNase) activity that can
CC inhibit the production of type I interferon and assist in the
CC development of persistent infections. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Envelope glycoprotein E1]: Plays a role in cell attachment
CC and subsequent fusion of viral and cellular membranes. Therefore,
CC mediates together with envelope glycoprotein E2 the viral entry.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Envelope glycoprotein E2]: Plays a role in cell attachment
CC and subsequent fusion of viral and cellular membranes. Therefore,
CC mediates together with envelope glycoprotein E1 the viral entry.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Viroporin p7]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin. Forms ion conductive pores,
CC which alters the cell permeability allowing the transport of ions and
CC other small molecules. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 2-3]: Autoprotease that associates
CC with the host chaperone JIV and cleaves the NS2-3 protein between NS2
CC and NS3. Also plays a role in the formation of infectious particles.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Cysteine protease NS2]: Plays a role in the regulation of
CC viral RNA replication. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Serine protease NS3]: Multifunctional protein that contains
CC an N-terminal protease and a C-terminal helicase, playing essential
CC roles in viral polyprotein processing and viral genome replication. The
CC chymotrypsin-like serine protease activity utilizes NS4A as an
CC essential cofactor and catalyzes the cleavage of the polyprotein
CC leading to the release of NS4A, NS4B, NS5A, and NS5B. Plays a role in
CC the inhibition of host NF-kappa-B activation by interacting with and
CC inhibiting host TRAF6. Interacts with NS5B to enhance RNA-dependent RNA
CC polymerase activity. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 4A]: Acts as a cofactor for the NS3
CC protease activity. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 4B]: Induces a specific membrane
CC alteration that serves as a scaffold for the virus replication complex
CC (By similarity). Antagonizes host cell apoptosis by interacting with
CC host ferritin heavy chain. The ORF4 protein physically binds host
CC FTH1/FHC, resulting in the reduction of FTH1 protein levels in host
CC cells. Reduction of FTH1 concentration further inhibits the
CC accumulation of reactive oxygen in host cells, leading to reduced
CC apoptosis. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 5A]: Regulates viral RNA replication
CC by interacting with the 3'-untranslated region of viral RNA in a dose-
CC dependent manner. At small concentrations promotes viral synthesis by
CC interacting with the polymerase NS5B while at large concentrations,
CC inhibits replication. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral (+) and
CC (-) genome. {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=Leu is conserved at position P1 for all four cleavage sites.
CC Alanine is found at position P1' of the NS4A-NS4B cleavage site,
CC whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A
CC and NS5A-NS5B cleavage sites.; EC=3.4.21.113;
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
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: [Serine protease NS3]:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
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 -!- SUBUNIT: [N-terminal protease]: Interacts with host IRF3.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Capsid protein C]: Interacts with host OS9.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [E(rns) glycoprotein]: Homodimer; disulfide-linked. Interacts
CC with host RPSA. {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Envelope glycoprotein E1]: Homodimer; disulfide-linked (By
CC similarity). Heterodimer with E1; disulfide-linked (By similarity).
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Envelope glycoprotein E2]: Homodimer; disulfide-linked (By
CC similarity). Heterodimer with E1; disulfide-linked (By similarity).
CC Interacts with host TRX2 (By similarity).
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Serine protease NS3]: Interacts with host TRAF6; this
CC interaction inhibits host NF-kappa-B pathway. Interacts with NS5B; this
CC interaction enhances RNA-dependent RNA polymerase activity. Interacts
CC with protein NS4A. {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with host RAB5, this
CC interaction facilitates the formation of NS4B-related complex.
CC Interacts with host FTH1; this interaction plays a positive role in
CC viral anti-apoptosis. {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Non-structural protein 5A]: Interacts with RNA-directed RNA
CC polymerase. Interacts with host RSAD2; this interaction inhibits viral
CC replication. {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with NS5A; this
CC interaction promotes viral replication. {ECO:0000250|UniProtKB:P19712}.
CC -!- INTERACTION:
CC PRO_0000038062; P25963: NFKBIA; Xeno; NbExp=4; IntAct=EBI-12558622, EBI-307386;
CC PRO_0000038062; Q08353: NFKBIA; Xeno; NbExp=4; IntAct=EBI-12558622, EBI-12558699;
CC PRO_0000038063; K9IWF9: IQGAP1; Xeno; NbExp=3; IntAct=EBI-12515736, EBI-12515741;
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [E(rns) glycoprotein]: Host membrane; Peripheral
CC membrane protein. Virion membrane; Peripheral membrane protein
CC {ECO:0000305}. Note=The C-terminus membrane anchor of Erns represents
CC an amphipathic helix embedded in plane into the membrane.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Host cell surface
CC {ECO:0000250|UniProtKB:P19712}. Virion membrane
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [Cysteine protease NS2]: Host membrane
CC {ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU01029}.
CC -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 5A]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- INDUCTION: Translated cap independently from an internal ribosome entry
CC site (IRES). {ECO:0000269|PubMed:9573242}.
CC -!- PTM: [E(rns) glycoprotein]: Heavily glycosylated.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- PTM: The viral RNA of pestiviruses is expressed as a single polyprotein
CC which undergoes post-translational proteolytic processing resulting in
CC the production of at least eleven individual proteins. The N-terminal
CC protease cleaves itself from the nascent polyprotein autocatalytically
CC and thereby generates the N-terminus of the adjacent viral capsid
CC protein C. {ECO:0000250|UniProtKB:P19712}.
CC -!- PTM: [Genome polyprotein]: Cleavage between E2 and p7 is partial.
CC -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M31768; AAA43843.1; -; Genomic_RNA.
DR PIR; A35317; GNWVHB.
DR SMR; P21530; -.
DR IntAct; P21530; 61.
DR MEROPS; S31.001; -.
DR PRIDE; P21530; -.
DR Proteomes; UP000008569; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
DR GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0033897; F:ribonuclease T2 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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030839; P:regulation of intermediate filament polymerization; IMP:AgBase.
DR GO; GO:1903525; P:regulation of membrane tubulation; IMP:AgBase.
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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; IDA:AgBase.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0019076; P:viral release from host cell; IMP:AgBase.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.30.140.40; -; 1.
DR Gene3D; 2.60.320.20; -; 1.
DR Gene3D; 2.60.40.3000; -; 1.
DR Gene3D; 2.60.40.4200; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR021824; Capsid-C_pestivirus.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022120; NS2.
DR InterPro; IPR030399; NS2_C74.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008751; Peptidase_C53.
DR InterPro; IPR042542; Peptidase_C53_interaction.
DR InterPro; IPR032521; Pestivirus_E2.
DR InterPro; IPR042309; Pestivirus_E2_A.
DR InterPro; IPR042310; Pestivirus_E2_B.
DR InterPro; IPR042311; Pestivirus_E2_D.
DR InterPro; IPR000280; Pestivirus_NS3_S31.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR Pfam; PF11889; DUF3409; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF05550; Peptidase_C53; 1.
DR Pfam; PF12387; Peptidase_C74; 1.
DR Pfam; PF05578; Peptidase_S31; 1.
DR Pfam; PF16329; Pestivirus_E2; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR PRINTS; PR00729; CDVENDOPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
DR PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
DR PROSITE; PS51876; PV_NPRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 1: Evidence at protein level;
KW Activation of host autophagy by virus; ATP-binding; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW Host cytoplasm; 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 Ion channel; Ion transport; Membrane; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; RNA-directed RNA polymerase;
KW Serine protease; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Transport; Viral attachment to host cell;
KW Viral immunoevasion; Viral ion channel;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus entry into host cell.
FT CHAIN 1..3898
FT /note="Genome polyprotein"
FT /id="PRO_0000450894"
FT CHAIN 1..168
FT /note="N-terminal protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038062"
FT CHAIN 169..267
FT /note="Capsid protein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038063"
FT CHAIN 268..494
FT /note="E(rns) glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038064"
FT CHAIN 495..656
FT /note="Envelope glycoprotein E1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038065"
FT CHAIN 657..1062
FT /note="Envelope glycoprotein E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038066"
FT CHAIN 1063..1132
FT /note="Viroporin p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038067"
FT CHAIN 1133..2272
FT /note="Non-structural protein 2-3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038068"
FT CHAIN 1133..1589
FT /note="Cysteine protease NS2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT /id="PRO_0000349362"
FT CHAIN 1590..2272
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038069"
FT CHAIN 2273..2336
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038070"
FT CHAIN 2337..2683
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038071"
FT CHAIN 2684..3180
FT /note="Non-structural protein 5A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038072"
FT CHAIN 3181..3898
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038073"
FT TRANSMEM 1140..1164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1217..1237
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1247..1267
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1281..1301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1360..1380
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1568..1588
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT DOMAIN 1..168
FT /note="Peptidase C53"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT DOMAIN 1441..1589
FT /note="Peptidase C74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT DOMAIN 1590..1763
FT /note="Peptidase S31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT DOMAIN 1802..1960
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1978..2179
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 3519..3642
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2968..2987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 49
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT ACT_SITE 69
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT ACT_SITE 1447
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1461
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1512
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1658
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1695
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1752
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT SITE 168..169
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT SITE 267..268
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 494..495
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 656..657
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1062..1063
FT /note="Cleavage; by host signal peptidase; partial"
FT /evidence="ECO:0000250"
FT SITE 1132..1133
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1589..1590
FT /note="Cleavage; partial; by cysteine protease NS2"
FT /evidence="ECO:0000250"
FT SITE 2272..2273
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 2336..2337
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 2683..2684
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 3180..3181
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 918
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1713
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2134
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2217
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2419
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2494
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2787
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2815
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2891
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3103
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3211
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3316
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3689
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3698
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3794
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 3898 AA; 438430 MW; EC6EB207A09D59FD CRC64;
MELNHFELLY KTNKQKPMGV EEPVYDVTGR PLFGDPSEVH PQSTLKLPHD RGRGNIKTTL
KNLPRRGDCR SGNHLGPVSG IYVKPGPVFY QDYMGPVYHR APLEFFDEAQ FCEVTKRIGR
VTGSDGKLYH IYVCIDGCIL LKLAKRGEPR TLKWIRNLTD CPLWVTSCSD DGASASKEKK
PDRINKGKLK IAPKEHEKDS RTKPPDATIV VEGVKYQVKK KGKVKGKNTQ DGLYHNKNKP
PESRKKLEKA LLAWAVIAIM LYQPVAAENI TQWNLRDNGT NGIQHAMYLR GVSRSLHGIW
PEKICKGVPT YLATDTELRE IQGMMVASEG TNYTCCKLQR HEWNKHGWCN WYNIDPWIQL
MNRTQANLAE GPPSKECAVT CRYDKNADIN VVTQARNRPT TLTGCKKGTN FSFAGTVIEG
PCNFNVSVED ILYGDHECGS LLQDTALYLV DGMTNTIERA RQGAARVTSW LGRQLRIAGK
RLEGRSKTWF GAYALSPYCN VTTKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI
LHEMGGHLSE FLLLSLVVLS DFAPETASAL YLILHYVIPQ SHEEPEGCDT NQLNLTVELR
TEDVIPSSVW NVGKYVCVRP DWWPYETKVA LLFEEAGQVV KLALRALRDL TRVWNSASTT
AFLICLIKVL RGQVVQGVIW LLLVTGAQGR LACKEDHRYA ISTTNEIGLH GAEGLTTTWK
EYNHNLQLDD GTVKAICMAG SFKVTALNVV SRRYLASLHK DALPTSVTFE LLFDGTSPLT
EEMGDDFGFG LCPYDTSPVV KGKYNTTLLN GSAFYLVCPI GWTGVIECTA VSPTTLRTEV
VKTFRREKPF PYRRDCVTTT VENEDLFYCK WGGNWTCVKG EPVTYTGGPV KQCRWCGFDF
NEPDGLPHYP IGKCILANET GYRIVDSTDC NRDGVVISTE GSHECLIGNT TVKVHALDER
LGPMPCRPKE IVSSAGPVRK TSCTFNYAKT LRNRYYEPRD SYFQQYMLKG EYQYWFDLDV
TDRHSDYFAE FIVLVVVALL GGRYVLWLIV TYIVLTEQLA AGLQLGQGEV VLIGNLITHT
DIEVVVYFLL LYLVMRDEPI KKWILLLFHA MTNNPVKTIT VALLMVSGVA KGGKIDGGWQ
RLPETNFDIQ LALTVIVVAV MLLAKKDPTT VPLVITVATL RTAKITNGLS TDLAIATVST
ALLTWTYISD YYKYKTLLQY LISTVTGIFL IRVLKGVGEL DLHTPTLPSY RPLFFILVYL
ISTAVVTRWN LDIAGLLLQC VPTLLMVFTM WADILTLILI LPTYELTKLY YLKEVKIGAE
RGWLWKTNFK RVNDIYEVDQ AGEGVYLFPS KQKTGTITGT MLPLIKAILI SCISNKWQFI
YLLYLIFEVS YYLHKKIIDE IAGGTNFISR LVAALIEANW AFDNEEVRGL KKFFLLSSRV
KELIIKHKVR NEVMVHWFGD EEVYGMPKLV GLVKAATLSK NKHCILCTVC ENREWRGETC
PKCGRFGPPV TCGMTLADFE EKHYKRIFFR EDQSEGPVRE EYAGYLQYRA RGQLFLRNLP
VLATKVKMLL VGNLGTEVGD LEHLGWVLRG PAVCKKVTEH EKCTTSIMDK LTAFFGVMPR
GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ GGISSVDHVT CGKDLLVCDT MGRTRVVCQS
NNKMTDESEY GVKTDSGCPE GARCYVFNRE AVNISGTKGA MVHLQKTGGE FTCVTASGTP
AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK STTDLTEMVK
KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE SVYQYMRQKH
PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMPQPKLRAA MVEYSFIFLD EYHCSTPEQL
AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG QKHPIEEYIA PEVMKGEDLG PEYLDIAGLK
IPVEEMKSNM LVFVPTRNMA VETAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT
NAIESGVTLP DLDVVVDTGL KCEKRIRLSP KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK
PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE EDSLMITQLE
ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP VLFPKIKNGE VTDSYDNYTF
LNARKLGDDV PPYVYATEDE DLAVELLGLD WPDPGNQGTV EAGRALKQVV GLSTAENALL
VALFGYVGYQ ALSKRHIPVV TDIYSIEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD
VQRCMEAMTN YARDGIQFMK SQALKVKETP TYKETMDTVA DYVKKFMEAL ADSKEDIIKY
GLWGTHTALY KSIGARLGNE TAFATLVVKW LAFGGESIAD HVKQAATDLV VYYIINRPQF
PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE PALATLPYAA TALKLFAPTR
LESVVILSTA IYKTYLSIRR GKSDGLLGTG VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN
AIEASEQKRT LLMKVFVKNF LDQAATDELV KESPEKIIMA LFEAVQTVGN PLRLVYHVYG
VFYKGWEAKE LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDSIK
SSVRQMAISW APAPFSCDWT PTDDRIGLPQ DNFLRVETKC PCGYKMKAVK NCAGELRLLE
EEGSFLCRNK FGRGSRNYRV TKYYDDNLSE IKPVIRMEGH VELYYKGATI KLDFNNSKTI
LATDKWEVDH STLVRVLKRH TGAGYCGAYL GEKPNHKHLI ERDCATITKD KVCFLKMKRG
CAFTYDLSLH NLTRLIELVH KNNLEDKEIP AVTVTTWLAY TFVNEDIGTI KPAFGEKITP
EMQEEITLQP AVLVDATDVT VTVVGETPTM TTGETPTTFT SSGPDPKGQQ VLKLGVGEGQ
YPGTNPQRAS LHEAIQSADE RPSVLILGSD KATSNRVKTV KNVKVYRGRD PLEVRDMMRR
GKILVIALSR VDNALLKFVD YKGTFLTRET LEALSLGRPK KKNITKAEAQ WLLRLEDQME
ELPDWFAAGE PIFLEANIKH DRYHLVGDIA TIKEKAKQLG ATDSTKISKE VGAKVYSMKL
SNWVMQEENK QSNLTPLFEE LLQQCPPGGQ NKTAHMVSAY QLAQGNWMPT SCHVFMGTIS
ARRTKTHPYE AYVKLRELVE EHKMKTLCPG SSLRNDNEWV IGKIKYQGNL RTKHMLNPGK
VAEQLHREGH RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR DKIDKEENLQ
TPGLHKKLME VFNALKRPEL ESSYDAVEWE ELERGINRKG AAGFFERKNI GEILDSEKIK
VEEIIDNLKK GRNIKYYETA IPKNEKRDVN DDWTAGDFVD EKKPRVIQYP EAKTRLAITK
VMYKWVKQKP VVIPGYEGKT PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTNDLEL
IKDIQKYYFK KKWHKFIDTL TMHMSEVPVI TADGEVYIRK GQRGSGQPDT SAGNSMLNVL
TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL YEAGKPQKIT
EGDKMKVAYQ FADIEFCSHT PIQVRWSDNT SSYMPGRNTT TILAKMATRL DSSGERGTIA
YEKAVAFSFL LMYSWNPLIR RICLLVLSTE LQVKPGKSTT YYYEGDPISA YKEVIGHNLF
DLKRTSFEKL AKLNLSMSVL GAWTRHTSKR LLQDCVNMGV KEGNWLVNAD RLVSSKTGNR
YVPGEGHTLQ GRHYEELALA RKQINSFQGT DRYNLGPIVN MVLRRLRVMM MTLIGRGV
