POLG_BVDVS
ID POLG_BVDVS Reviewed; 3898 AA.
AC Q01499;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 156.
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 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 Bovine viral diarrhea virus (strain SD-1) (BVDV) (Mucosal disease virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus.
OX NCBI_TaxID=31656;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1333126; DOI=10.1016/0042-6822(92)90262-n;
RA Deng R., Brock K.V.;
RT "Molecular cloning and nucleotide sequence of a pestivirus genome,
RT noncytopathic bovine viral diarrhea virus strain SD-1.";
RL Virology 191:867-869(1992).
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]: Initial binding to target cell
CC probably involves interaction of E(rns) with glycosaminoglycans.
CC {ECO:0000250|UniProtKB:P19711}.
CC -!- FUNCTION: [Envelope glycoprotein E1]: E1 and/or E2 are probably
CC responsible of cell attachment with CD46 and subsequent fusion after
CC internalization of the virion by endocytosis.
CC {ECO:0000250|UniProtKB:P19711}.
CC -!- FUNCTION: [Envelope glycoprotein E2]: E1 and/or E2 are probably
CC responsible of cell attachment with CD46 and subsequent fusion after
CC internalization of the virion by endocytosis.
CC {ECO:0000250|UniProtKB:P19711}.
CC -!- FUNCTION: [Viroporin p7]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin (By similarity). Forms ion
CC conductive pores, which alters the cell permeability allowing the
CC transport of ions and other small molecules (By similarity). Forms a
CC leader sequence to properly orient NS2 in the membrane.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 2-3]: Uncleaved NS2-3 is required for
CC production of infectious virus.
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. Interacts with
CC NS5B to enhance RNA-dependent RNA polymerase activity.
CC {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 {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral (+) and
CC (-) genome.
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: [E(rns) glycoprotein]: Homodimer; disulfide-linked.
CC {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 {ECO:0000250|UniProtKB:P19712}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Host cell surface
CC {ECO:0000250|UniProtKB:P19711}. 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 -!- 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 -!- MISCELLANEOUS: BVDV is divided in two types: cytopathic and non-
CC cytopathic. Both types of viruses can be found in animals suffering
CC from mucosal disease, as a cytopathic BVDV can develop from a non-
CC cytopathic virus within the infected animal by deletions, mutations or
CC insertions. Both types express uncleaved NS2-3, but cytopathic strains
CC also express NS3.
CC -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M96751; AAA42860.1; -; Genomic_RNA.
DR PIR; A44217; A44217.
DR PDB; 2YQ2; X-ray; 2.58 A; A/B=696-1026.
DR PDB; 2YQ3; X-ray; 3.29 A; A/B=696-1026.
DR PDBsum; 2YQ2; -.
DR PDBsum; 2YQ3; -.
DR SMR; Q01499; -.
DR MEROPS; S31.001; -.
DR PRIDE; Q01499; -.
DR BRENDA; 3.4.21.113; 925.
DR Proteomes; UP000007619; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
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: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:0019082; P:viral protein processing; IEA:InterPro.
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 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Clathrin-mediated endocytosis of virus by host; 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 endocytosis by host; Virus entry into host cell.
FT CHAIN 1..3898
FT /note="Genome polyprotein"
FT /id="PRO_0000450892"
FT CHAIN 1..168
FT /note="N-terminal protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038037"
FT CHAIN 169..270
FT /note="Capsid protein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038038"
FT CHAIN 271..497
FT /note="E(rns) glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038039"
FT CHAIN 498..659
FT /note="Envelope glycoprotein E1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038040"
FT CHAIN 660..1066
FT /note="Envelope glycoprotein E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038041"
FT CHAIN 1067..1136
FT /note="Viroporin p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038042"
FT CHAIN 1137..2272
FT /note="Non-structural protein 2-3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038043"
FT CHAIN 1137..1589
FT /note="Cysteine protease NS2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT /id="PRO_0000038044"
FT CHAIN 1590..2272
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038045"
FT CHAIN 2273..2336
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038046"
FT CHAIN 2337..2683
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038047"
FT CHAIN 2684..3179
FT /note="Non-structural protein 5A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038048"
FT CHAIN 3180..3898
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038049"
FT TRANSMEM 1144..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..2143
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 3518..3641
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..208
FT /note="Basic and acidic residues"
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 270..271
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 497..498
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 659..660
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1066..1067
FT /note="Cleavage; by host signal peptidase; partial"
FT /evidence="ECO:0000250"
FT SITE 1136..1137
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1589..1590
FT /note="Cleavage; partial; cysteine protease NS2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
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 3179..3180
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 990
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1357
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1419
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1451
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 2494
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2682
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2751
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 2988
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3688
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3777
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3793
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT STRAND 700..706
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 718..720
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 734..750
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 756..765
FT /evidence="ECO:0007829|PDB:2YQ2"
FT HELIX 767..769
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 771..776
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 793..795
FT /evidence="ECO:0007829|PDB:2YQ2"
FT HELIX 797..799
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 801..808
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 811..814
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 817..820
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 828..835
FT /evidence="ECO:0007829|PDB:2YQ2"
FT TURN 837..839
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 842..852
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 869..875
FT /evidence="ECO:0007829|PDB:2YQ2"
FT HELIX 878..880
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 882..886
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 894..899
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 902..906
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 910..914
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 916..920
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 924..928
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 934..936
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 939..941
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 946..951
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 954..961
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 964..967
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 969..973
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 976..982
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 985..993
FT /evidence="ECO:0007829|PDB:2YQ2"
FT TURN 1005..1007
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 1011..1013
FT /evidence="ECO:0007829|PDB:2YQ2"
FT STRAND 1016..1024
FT /evidence="ECO:0007829|PDB:2YQ2"
SQ SEQUENCE 3898 AA; 437808 MW; 31ACEE140D407ED3 CRC64;
MELITNELLY KTYKQKPVGV EEPVYDQAGN PLFGERGAIH PQSTLKLPHK RGERNVPTSL
ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR APLELFEEGS MCETTKRIGR
VTGSDGKLYH IYICIDGCIT VKSATRSHQR VLRWVHNRLD CPLWVTSCSD TKEEGATKKK
QQKPDRLEKG RMKIVPKESE KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK
NKPPESRKKL EKALLAWAIL AVVLIEVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH
GIWPEKICTG VPSHLATDVE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW
ILIMNRTQAN LTEGQPPREC AVTCRYDRDS DLNVVTQARD SPTPLTGCKK GKNFSFAGVL
TRGPCNFEIA ASDVLFKEHE CTGVFQDTAH YLVDGVTNSL ESARQGTAKL TTWLGKQLGI
LGKKLENKSK TWFGAYAASP YCDVDRKIGY IWFTKNCTPA CLPKNTKIIG PGKFDTNAED
GKILHEMGGH LSEVLLLSLV VLSDFAPETA SAMYLILHFS IPQSHVDITD CDKTQLNLTI
ELTTADVIPG SVWNLGKYVC IRPDWWPYET AAVLAFEEVG QVVKIVLRAL RDLTRIWNAA
TTTAFLVCLI KMVRGQVVQG ILWLLLITGV QGHLDCKPEY SYAIAKNDRV GPLGAEGLTT
VWKDYSHEMK LEDTMVIAWC KGGKFTYLSR CTRETRYLAI LHSRALPTSV VFKKLFEGQK
QEDTVEMDDD FEFGLCPCDA KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCMLANRDTL
DTAVVRTYRR SVPFPYRQGC ITQKTLGEDL YDCALGGNWT CVTGDQSRYT GGLIESCKWC
GYKFQKSEGL PHYPIGKCRL NNETGYRLVD DTSCDREGVA IVPHGLVKCK IGDTTVQVIA
TDTKLGPMPC KPHEIISSEG PIEKTACTFN YTRTLKNKYF EPRDSYFQQY MLKGDYQYWF
DLEVTDHHRD YFAESILVVV VALLGGRYVL WLLVTYMVLS EQKASGAQYG AGEVVMMGNL
LTHDNVEVVT YFFLLYLLLR EESVKKWVLL LYHILVAHPL KSVIVILLMI GDVVKADPGG
QGYLGQIDVC FTMVVIIIIG LIIARRDPTI VPLITIVASL RVTGLTYSPG VDAAMAVITI
TLLMVSYVTD YFRYKRWLQC ILSLVSGVFL IRCLIHLGRI ETPEVTIPNW RPLTLILFYL
ISTTVVTMWK IDLAGLLLQG VPILLLITTL WADFLTLILI LPTYELVKLY YLKTIKTDIE
KSWLGGLDYK RVDSIYDVDE SGEGVYLFPS RQKAQKNFSM LLPLVRATLI SCVSSKWQLI
YMAYLSVDFM YYMHRKVIEE ISGGTNMISR IVAALIELNW SMEEEESKGL KKFYLLSGRL
RNLIIKHKVR NETVAGWYGE EEVYGMPKIM TIIKASTLNK NKHCIICTVC EGRKWKGGTC
PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGPFRQ EYNGFIQYTA RGQLFLRNLP
ILATKVKMLM VGNLGEEVGD LEHLGWILRG PAVCKKITEH ERCHINILDK LTAFFGIMPR
GTTPRAPVRF PTSLLKVRRG LETGWAYTHQ GGISSVDHVT AGKDLLVCDS MGRTRVVCQS
NNKLTDETEY GVKTDSGCPD GARCYVLNPE AVNISGSKGA VVHLQKTGGE FTCVTASGTP
AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEESKPTK IMSGIQTVSK NTADLTEMVK
KITSMNRGDF KQITLATGAG KTTELPKAVI EEIGRHKRVL VLIPLRAAAE SVYQYMRLKH
PSISFNLRIG DMKEGDMATG ITYASYGYFC QMPQPKLRAA MVEYSYIFLD EYHCATPEQL
AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG QKHPIEEFIA PEVMEGEDLG SQFLDIAGLK
IPVDEMKGNM LVFVPTRNMA VEVAKKLKAK GYNSGYYYSG EDPANLRVVT SQSPYVIVAT
NAIESGVTLP DLDTVVDTGL KCEKRVRVSS KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK
PGRYYRSQET ATGSKDYHYD LLQAQRYGIE DGINVTKSFR EMNYDWSLYE EDSLLITQLE
ILNNLLISED LPAAVKNIMA RTDHPEPIQL AYNSYEVQVP VLFPKIRNGE VTDTYENYSF
LNARKLGEDV PVYIYATEDE DLAVDLLGLD WPDPGNQQVV ETGKALKQVA GLSSAENALL
VALFGYVGYQ ALSKRHVPMI TDIYTIEDQR LEDTTHLQYA PNAIKTEGTE TELKELASGD
VEKIMGAISD YAAGGLDFVK SQAEKIKTAP LFKENVEAAR GYVQKLIDSL IEDKDVIIRY
GLWGTHTALY KSIAARLGHE TAFATLVLKW LAFGGETVSD HIRQAAVDLV VYYVMNKPSF
PGDTETQQEG RRFVASLFIS ALATYTYKTW NYNNLSKVVE PALAYLPYAT SALKMFTPTR
LESVVILSTT IYKTYLSIRK GKSDGLLGTG ISAAMEILSQ NPVSVGISVM LGVGAIAAHN
AIESSEQKRT LLMKVFVKNF LDQAATDELV KENPEKIIMA LFEAVQTIGN PLRLIYHLYG
VYYKGWEAKE LSERTAGRNL FTLIMFEAFE LLGMDSEGKI RNLSGNYILD LIHGLHKQIN
RGLKKIVLGW APAPFSCDWT PSDERIRLPT DSYLRVETKC PCGYEMKALK NVSGKLTKVE
ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE IRPVAKLEGQ VEHYYKGVTA RIDYSKGKTL
LATDKWEVEH GTLTRLTKRY TGVGFRGAYL GDEPNHRDLV ERDCATITKN TVQFLKMKKG
CAFTYDLTIS NLTRLIELVH RNNLEEKEIP TATVTTWLAY TFVNEDVGTI KPVLGERVIP
DPVVDINLQP EVQVDTSEVG ITIIGKEAVM TTGVTPVMEK VEPDTDNNQS SVKIGLDEGN
YPGPGVQTHT LVEEIHNKDA RPFIMVLGSK SSMSNRAKTA RNINLYTGND PREIRDLMAE
GRILVVALRD IDPDLSELVD FKGTFLDREA LEALSLGQPK PKQVTKAAIR DLLKEERQVE
IPDWFTSDDP VFLDIAMKKD KYHLIGDVVE VKDQAKALGA TDQTRIVKEV GSRTYTMKLS
SWFLQASSKQ MSLTPLFEEL LLRCPPATKS NKGHMASAYQ LAQGNWEPLG CGVHLGTVPA
RRVKMHPYEA YLKLKDLVEE EEKKPRIRDT VIREHNKWIL KKIKFQGNLN TKKMLNPGKL
SEQLDREGHK RNIYNNQIST VMSSAGIRLE KLPIVRAQTD TKSFHEAIRD KIDKNENRQN
PELHNKLLEI FHTIADPSLK HTYGEVTWEQ LEAGINRKGA AGFLEKKNIG EVLDSEKHLV
EQLVRDLKAG RKIRYYETAI PKNEKRDVSD DWQAGDLVDE KKPRVIQYPE AKTRLAITKV
MYNWVKQQPV VIPGYEGKTP LFNIFNKVRK EWDLFNEPVA VSFDTKAWDT QVTSRDLHLI
GEIQKYYYRK EWHKFIDTIT DHMVEVPVIT ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT
MIYAFCESTG VPYKSFNRVA KIHVCGDDGF LITEKGLGLK FSNKGMQILH EAGKPQKLTE
GEKMKVAYKF EDIEFCSHTP VPVRWSDNTS SYMAGRDTAV ILSKMATRLD SSGERGTTAY
EKAVAFSFLL MYSWNPLVRR ICLLVLSQRP ETAPSTQTTY YYKGDPIGAY KDVIGRNLSE
LKRTGFEKLA NLNLSLSTLG IWTKHTSKRI IQDCVAIGKE EGNWLVNADR LISSKTGHLY
IPDKGFTLQG KHYEQLQLGA ETNPVMGVGT ERYKLGPIVN LLLRRLKVLL MAAVGASS
