POLG_GBVB
ID POLG_GBVB Reviewed; 2864 AA.
AC Q69422; Q6QLR5; Q6QLR6; Q6QLR7; Q6QLR8; Q6QLR9; Q6QLS0; Q8JKE4; Q999T0;
AC Q9QEW5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Core protein;
DE Contains:
DE RecName: Full=Envelope glycoprotein E1;
DE Contains:
DE RecName: Full=Envelope glycoprotein E2;
DE AltName: Full=NS1;
DE Contains:
DE RecName: Full=p13;
DE Contains:
DE RecName: Full=p6;
DE Contains:
DE RecName: Full=Viroporin p7;
DE Contains:
DE RecName: Full=Protease NS2;
DE EC=3.4.22.- {ECO:0000250|UniProtKB:P26663};
DE AltName: Full=Non-structural protein 2;
DE Short=NS2;
DE Contains:
DE RecName: Full=Serine protease/helicase NS3;
DE EC=3.4.21.98 {ECO:0000250|UniProtKB:P27958};
DE EC=3.6.1.15 {ECO:0000269|PubMed:10497107};
DE EC=3.6.4.13 {ECO:0000269|PubMed:10497107};
DE AltName: Full=Hepacivirin;
DE AltName: Full=NS3 helicase {ECO:0000250|UniProtKB:P27958};
DE AltName: Full=NS3 protease {ECO:0000250|UniProtKB:P27958};
DE AltName: Full=NS3P;
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 {ECO:0000250|UniProtKB:P27958};
DE AltName: Full=NS5B;
OS Hepatitis GB virus B (GBV-B) (GB virus B).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=2847087;
OH NCBI_TaxID=9483; Callithrix jacchus (White-tufted-ear marmoset).
OH NCBI_TaxID=9486; Saguinus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7724574; DOI=10.1073/pnas.92.8.3401;
RA Simons J.N., Pilot-Matias T.J., Leary T.P., Dawson G.J., Desai S.M.,
RA Schlauder G.G., Muerhoff A.S., Erker J.C., Buijk S.L., Chalmers M.L.,
RA van Sant C.L., Mushahwar I.K.;
RT "Identification of two flavivirus-like genomes in the GB hepatitis agent.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3401-3405(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10502525; DOI=10.1006/viro.1999.9941;
RA Bukh J., Apgar C.L., Yanagi M.;
RT "Toward a surrogate model for hepatitis C virus: an infectious molecular
RT clone of the GB virus-B hepatitis agent.";
RL Virology 262:470-478(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11562537; DOI=10.1099/0022-1317-82-10-2437;
RA Sbardellati A., Scarselli E., Verschoor E., De Tomassi A., Lazzaro D.,
RA Traboni C.;
RT "Generation of infectious and transmissible virions from a GB virus B full-
RT length consensus clone in tamarins.";
RL J. Gen. Virol. 82:2437-2448(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 940-2864.
RX PubMed=12097587; DOI=10.1128/jvi.76.15.7736-7746.2002;
RA De Tomassi A., Pizzuti M., Graziani R., Sbardellati A., Altamura S.,
RA Paonessa G., Traboni C.;
RT "Cell clones selected from the Huh7 human hepatoma cell line support
RT efficient replication of a subgenomic GB virus B replicon.";
RL J. Virol. 76:7736-7746(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1864-2274.
RA Viazov S., Kioureguian K.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CATALYTIC ACTIVITY (SERINE PROTEASE/HELICASE NS3), MUTAGENESIS OF LYS-1150,
RP COFACTOR (SERINE PROTEASE/HELICASE NS3), AND BIOPHYSICOCHEMICAL PROPERTIES
RP (SERINE PROTEASE/HELICASE NS3).
RX PubMed=10497107; DOI=10.1006/viro.1999.9871;
RA Zhong W., Ingravallo P., Wright-Minogue J., Skelton A., Uss A.S., Chase R.,
RA Yao N., Lau J.Y.N., Hong Z.;
RT "Nucleoside triphosphatase and RNA helicase activities associated with GB
RT virus B nonstructural protein 3.";
RL Virology 261:216-226(1999).
RN [7]
RP PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
RX PubMed=15060070; DOI=10.1074/jbc.m401148200;
RA Ghibaudo D., Cohen L., Penin F., Martin A.;
RT "Characterization of GB virus B polyprotein processing reveals the
RT existence of a novel 13-kDa protein with partial homology to hepatitis C
RT virus p7 protein.";
RL J. Biol. Chem. 279:24965-24975(2004).
RN [8]
RP FUNCTION (P13), PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN), AND
RP MUTAGENESIS OF GLY-613; 730-ALA--ALA-732 AND GLY-669.
RX PubMed=16492760; DOI=10.1073/pnas.0511297103;
RA Takikawa S., Engle R.E., Emerson S.U., Purcell R.H., St Claire M., Bukh J.;
RT "Functional analyses of GB virus B p13 protein: development of a
RT recombinant GB virus B hepatitis virus with a p7 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3345-3350(2006).
RN [9]
RP INTERACTION WITH HUMAN MAVS (SERINE PROTEASE/HELICASE NS3), AND FUNCTION
RP (SERINE PROTEASE/HELICASE NS3).
RX PubMed=17093192; DOI=10.1128/jvi.02076-06;
RA Chen Z., Benureau Y., Rijnbrand R., Yi J., Wang T., Warter L.,
RA Lanford R.E., Weinman S.A., Lemon S.M., Martin A., Li K.;
RT "GB virus B disrupts RIG-I signaling by NS3/4A-mediated cleavage of the
RT adaptor protein MAVS.";
RL J. Virol. 81:964-976(2007).
CC -!- FUNCTION: [Core protein]: Packages viral RNA to form a viral
CC nucleocapsid, and promotes virion budding (Probable). Participates in
CC the viral particle production as a result of its interaction with the
CC non-structural protein 5A (By similarity). Binds RNA and may function
CC as a RNA chaperone to induce the RNA structural rearrangements taking
CC place during virus replication (By similarity). Modulates viral
CC translation initiation by interacting with viral IRES and 40S ribosomal
CC subunit (By similarity). Probably affects various cell signaling
CC pathways, host immunity and lipid metabolism (Probable).
CC {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958,
CC ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}.
CC -!- FUNCTION: [Envelope glycoprotein E1]: Forms a heterodimer with envelope
CC glycoprotein E2, which mediates virus attachment to the host cell,
CC virion internalization through clathrin-dependent endocytosis and
CC fusion with host membrane (By similarity). Fusion with the host cell is
CC most likely mediated by both E1 and E2, through conformational
CC rearrangements of the heterodimer required for fusion rather than a
CC classical class II fusion mechanism (By similarity).
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- FUNCTION: [Envelope glycoprotein E2]: Forms a heterodimer with envelope
CC glycoprotein E1, which mediates virus attachment to the host cell,
CC virion internalization through clathrin-dependent endocytosis and
CC fusion with host membrane (By similarity). Fusion with the host cell is
CC most likely mediated by both E1 and E2, through conformational
CC rearrangements of the heterodimer required for fusion rather than a
CC classical class II fusion mechanism (By similarity).
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- FUNCTION: [p13]: May function as a multimeric ion channel protein
CC (viroporin). {ECO:0000269|PubMed:16492760}.
CC -!- FUNCTION: [Protease NS2]: Cysteine protease required for the
CC proteolytic auto-cleavage between the non-structural proteins NS2 and
CC NS3 (By similarity). The N-terminus of NS3 is required for the function
CC of NS2 protease (active region NS2-3) (By similarity). Promotes the
CC initiation of viral particle assembly by mediating the interaction
CC between structural and non-structural proteins (By similarity).
CC {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}.
CC -!- FUNCTION: [Serine protease/helicase NS3]: Displays three enzymatic
CC activities: serine protease with a chymotrypsin-like fold, NTPase and
CC RNA helicase (PubMed:10497107). NS3 serine protease, in association
CC with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B,
CC NS4B-NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents
CC phosphorylation of host IRF3, thus preventing the establishment of
CC dsRNA induced antiviral state (By similarity). NS3 RNA helicase binds
CC to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and
CC likely resolves RNA complicated stable secondary structures in the
CC template strand (By similarity). Cleaves host MAVS/CARDIF thereby
CC preventing the establishment of an antiviral state (PubMed:17093192).
CC {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:10497107,
CC ECO:0000269|PubMed:17093192}.
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). This membrane alteration gives rise to the so-called
CC ER-derived membranous web that contains the replication complex (By
CC similarity). NS4B self-interaction contributes to its function in
CC membranous web formation (By similarity).
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- FUNCTION: [Non-structural protein 5A]: Phosphorylated protein that is
CC indispensable for viral replication and assembly.
CC {ECO:0000250|UniProtKB:Q99IB8}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase
CC that performs primer-template recognition and RNA synthesis during
CC viral replication. {ECO:0000250|UniProtKB:P27958}.
CC -!- CATALYTIC ACTIVITY: [Serine protease/helicase NS3]:
CC Reaction=Hydrolysis of four peptide bonds in the viral precursor
CC polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr
CC in P1 and Ser or Ala in P1'.; EC=3.4.21.98;
CC Evidence={ECO:0000250|UniProtKB:P27958};
CC -!- CATALYTIC ACTIVITY: [Serine protease/helicase 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 Evidence={ECO:0000269|PubMed:10497107};
CC -!- CATALYTIC ACTIVITY: [Serine protease/helicase 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 Evidence={ECO:0000269|PubMed:10497107};
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 -!- COFACTOR: [Protease NS2]:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P26663};
CC Note=Activity of protease NS2 is dependent on zinc ions and completely
CC inhibited by EDTA. This is probably due to the fact that NS2 protease
CC activity needs NS3 N-terminus that binds a zinc atom (active region
CC NS2-3). {ECO:0000250|UniProtKB:P26663};
CC -!- COFACTOR: [Serine protease/helicase NS3]:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P26663};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10497107};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10497107};
CC Note=Binds 1 zinc ion, which has a structural role (By similarity).
CC Magnesium or manganese ions are essential for the helicase activity
CC (PubMed:10497107). {ECO:0000250|UniProtKB:P26663,
CC ECO:0000269|PubMed:10497107};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.64 mM for ATP for NS3 NTPase;
CC KM=1.41 mM for CTP for NS3 NTPase;
CC KM=1.12 mM for UTP for NS3 NTPase;
CC KM=1.87 mM for dATP for NS3 NTPase;
CC KM=1.22 mM for dCTP for NS3 NTPase;
CC KM=0.65 mM for dTTP for NS3 NTPase;
CC pH dependence:
CC Stable from 6 to 8.5. {ECO:0000269|PubMed:10497107};
CC -!- SUBUNIT: [Core protein]: Homooligomer (By similarity). Interacts with
CC E1 (via C-terminus) (By similarity). Interacts with the non-structural
CC protein 5A (By similarity). Part of the viral assembly initiation
CC complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the core protein
CC (By similarity). {ECO:0000250|UniProtKB:P26664,
CC ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8}.
CC -!- SUBUNIT: [Envelope glycoprotein E1]: Forms a heterodimer with envelope
CC glycoprotein E2 (By similarity). Interacts with the core protein (By
CC similarity). Interacts with protease NS2 (By similarity). Part of the
CC viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A,
CC NS5A and the core protein (By similarity).
CC {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8}.
CC -!- SUBUNIT: [Envelope glycoprotein E2]: Forms a heterodimer with envelope
CC glycoprotein E1 (By similarity). Part of the viral assembly initiation
CC complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the core protein
CC (By similarity). {ECO:0000250|UniProtKB:P27958,
CC ECO:0000250|UniProtKB:Q99IB8}.
CC -!- SUBUNIT: [Protease NS2]: Homodimer (By similarity). Interacts with
CC envelope glycoprotein E1 (By similarity). Interacts with envelope
CC glycoprotein E2 (By similarity). Interacts with viroporin p7 (By
CC similarity). Interacts with serine protease/helicase NS3 (By
CC similarity). Part of the replication complex composed of NS2, NS3,
CC NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-
CC derived membranous web (By similarity). Part of the viral assembly
CC initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the
CC core protein (By similarity). {ECO:0000250|UniProtKB:P27958,
CC ECO:0000250|UniProtKB:Q99IB8}.
CC -!- SUBUNIT: [Serine protease/helicase NS3]: Interacts with protease NS2
CC (By similarity). Interacts with non-structural protein 4A; this
CC interaction stabilizes the folding of NS3 serine protease (By
CC similarity). NS3-NS4A interaction is essential for NS3 activation and
CC allows membrane anchorage of the latter (By similarity). Interacts with
CC host MAVS; this interaction leads to the cleavage and inhibition of
CC host MAVS (Probable). Part of the replication complex composed of NS2,
CC NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in
CC an ER-derived membranous web (By similarity). Part of the viral
CC assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A
CC and the core protein (By similarity). {ECO:0000250|UniProtKB:P26663,
CC ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8,
CC ECO:0000305|PubMed:17093192}.
CC -!- SUBUNIT: [Non-structural protein 4A]: Interacts with NS3 serine
CC protease; this interaction stabilizes the folding of NS3 serine
CC protease (By similarity). NS3-NS4A interaction is essential for NS3
CC activation and allows membrane anchorage of the latter (By similarity).
CC Interacts with non-structural protein 5A (via N-terminus) (By
CC similarity). Part of the replication complex composed of NS2, NS3,
CC NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-
CC derived membranous web (By similarity). Part of the viral assembly
CC initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the
CC core protein (By similarity). {ECO:0000250|UniProtKB:P26662,
CC ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958,
CC ECO:0000250|UniProtKB:Q99IB8}.
CC -!- SUBUNIT: [Non-structural protein 5A]: Monomer (By similarity).
CC Homodimer; dimerization is required for RNA-binding (By similarity).
CC Interacts with the core protein (By similarity). Interacts (via N-
CC terminus) with non-structural protein 4A (By similarity). Interacts
CC with non-structural protein 4B (By similarity). Interacts with RNA-
CC directed RNA polymerase (By similarity). Part of the viral assembly
CC initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the
CC core protein (By similarity). Part of the replication complex composed
CC of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase (By
CC similarity). {ECO:0000250|UniProtKB:P26662,
CC ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8}.
CC -!- SUBCELLULAR LOCATION: [Core protein]: Virion
CC {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q99IB8}. Host lipid droplet
CC {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core
CC protein is present in the nucleus (By similarity). Probably present on
CC the surface of lipid droplets (By similarity).
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E1]: Virion membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host
CC endoplasmic reticulum membrane; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane
CC domain acts as a signal sequence and forms a hairpin structure before
CC cleavage by host signal peptidase (By similarity). After cleavage, the
CC membrane sequence is retained at the C-terminus of the protein, serving
CC as ER membrane anchor (By similarity). A reorientation of the second
CC hydrophobic stretch occurs after cleavage producing a single reoriented
CC transmembrane domain (By similarity). These events explain the final
CC topology of the protein (By similarity).
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Virion membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host
CC endoplasmic reticulum membrane; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P27958}. Host lipid droplet
CC {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane
CC domain acts as a signal sequence and forms a hairpin structure before
CC cleavage by host signal peptidase (By similarity). After cleavage, the
CC membrane sequence is retained at the C-terminus of the protein, serving
CC as ER membrane anchor (By similarity). A reorientation of the second
CC hydrophobic stretch occurs after cleavage producing a single reoriented
CC transmembrane domain (By similarity). These events explain the final
CC topology of the protein (By similarity).
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- SUBCELLULAR LOCATION: [p13]: Host endoplasmic reticulum membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protease NS2]: Host endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P27958}. Host lipid droplet
CC {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of
CC lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}.
CC -!- SUBCELLULAR LOCATION: [Serine protease/helicase NS3]: Host endoplasmic
CC reticulum membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}. Note=NS3 is associated to the ER membrane through its
CC binding to NS4A. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
CC reticulum membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Host membrane insertion occurs after processing by
CC the NS3 protease.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N-
CC terminus into the ER lumen occurs post-translationally.
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 5A]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion
CC {ECO:0000250|UniProtKB:P26662}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P27958}. Host nucleus
CC {ECO:0000250|UniProtKB:P26662}. Host lipid droplet
CC {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs
CC after processing by the NS3 protease (By similarity). Localizes at the
CC surface of lipid droplets (By similarity).
CC {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane;
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}.
CC Note=Host membrane insertion occurs after processing by the NS3
CC protease. {ECO:0000250|UniProtKB:P27958}.
CC -!- DOMAIN: [Envelope glycoprotein E1]: The transmembrane regions of
CC envelope E1 and E2 glycoproteins are involved in heterodimer formation,
CC ER localization, and assembly of these proteins.
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- DOMAIN: [Envelope glycoprotein E2]: The transmembrane regions of
CC envelope E1 and E2 glycoproteins are involved in heterodimer formation,
CC ER localization, and assembly of these proteins.
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- DOMAIN: [Protease NS2]: The N-terminus of NS3 is required for the
CC catalytic activity of protease NS2 (By similarity). The minimal
CC catalytic region includes the C-terminus of NS2 and the N-terminus NS3
CC protease domain (active region NS2-3) (By similarity).
CC {ECO:0000250|UniProtKB:P26663}.
CC -!- DOMAIN: [Serine protease/helicase NS3]: The N-terminal one-third
CC contains the protease activity (By similarity). This region contains a
CC zinc atom that does not belong to the active site, but may play a
CC structural rather than a catalytic role (By similarity). This region is
CC essential for the activity of protease NS2, maybe by contributing to
CC the folding of the latter (By similarity). The NTPase/helicase activity
CC is located in the twothirds C-terminus of NS3, this domain contains the
CC NTPase and RNA-binding regions (By similarity).
CC {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}.
CC -!- DOMAIN: [Non-structural protein 4B]: Contains a glycine zipper region
CC that critically contributes to the biogenesis of functional ER-derived
CC replication organelles. {ECO:0000250|UniProtKB:Q99IB8}.
CC -!- DOMAIN: [Non-structural protein 5A]: The N-terminus of NS5A acts as
CC membrane anchor. {ECO:0000250|UniProtKB:P27958}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins (By similarity). The structural proteins, core, E1, E2
CC and p7 are produced by proteolytic processing by host signal peptidases
CC (By similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and
CC NS5B) are cleaved by the viral proteases (By similarity).
CC Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine
CC protease catalytic domain and regulated by the NS3 N-terminal domain
CC (By similarity). P13 may be further cleaved into p6 and p7 if the
CC internal cleavage site is used (PubMed:15060070, PubMed:16492760).
CC {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958,
CC ECO:0000269|PubMed:15060070, ECO:0000269|PubMed:16492760}.
CC -!- PTM: [Envelope glycoprotein E1]: Highly N-glycosylated.
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- PTM: [Envelope glycoprotein E2]: Highly N-glycosylated.
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- PTM: [Non-structural protein 4B]: Palmitoylated. This modification may
CC play a role in its polymerization or in protein-protein interactions.
CC {ECO:0000250|UniProtKB:P27958}.
CC -!- MISCELLANEOUS: Of all animal viruses, GBV-B is the most closely related
CC to HCV.
CC -!- CAUTION: The core gene probably also codes for alternative reading
CC frame proteins (ARFPs). Many functions depicted for the core protein
CC might belong to the ARFPs. {ECO:0000305}.
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DR EMBL; U22304; AAC54059.1; -; Genomic_RNA.
DR EMBL; AF179612; AAF01368.1; -; Genomic_RNA.
DR EMBL; AJ277947; CAC33083.1; -; Genomic_RNA.
DR EMBL; AJ428955; CAD21957.1; -; Genomic_RNA.
DR EMBL; AY534873; AAS45125.1; -; Genomic_RNA.
DR EMBL; AY534874; AAS45126.1; -; Genomic_RNA.
DR EMBL; AY534875; AAS45127.1; -; Genomic_RNA.
DR EMBL; AY534876; AAS45128.1; -; Genomic_RNA.
DR EMBL; AY534877; AAS45129.1; -; Genomic_RNA.
DR EMBL; AY534878; AAS45130.1; -; Genomic_RNA.
DR RefSeq; NP_056931.1; NC_001655.1.
DR PDB; 2LZP; NMR; -; A=734-764.
DR PDB; 2LZQ; NMR; -; A=764-789.
DR PDB; 2MKB; NMR; -; A=845-869.
DR PDBsum; 2LZP; -.
DR PDBsum; 2LZQ; -.
DR PDBsum; 2MKB; -.
DR BMRB; Q69422; -.
DR SMR; Q69422; -.
DR BindingDB; Q69422; -.
DR ChEMBL; CHEMBL5981; -.
DR MEROPS; S29.002; -.
DR TCDB; 1.A.53.1.11; the hepatitis c virus p7 viroporin cation-selective channel (hcv-p7) family.
DR PRIDE; Q69422; -.
DR GeneID; 1403460; -.
DR KEGG; vg:1403460; -.
DR PRO; PR:Q69422; -.
DR Proteomes; UP000114117; Genome.
DR Proteomes; UP000165726; Genome.
DR Proteomes; UP000172018; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044186; C:host cell lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; 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:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; 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:0003677; F:DNA binding; IDA:CAFA.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:CAFA.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0033592; F:RNA strand annealing activity; IDA:CAFA.
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:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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:0043489; P:RNA stabilization; IDA:CAFA.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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 DisProt; DP00674; -.
DR Gene3D; 2.20.25.210; -; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002521; HCV_Core_C.
DR InterPro; IPR002519; HCV_Env.
DR InterPro; IPR002518; HCV_NS2.
DR InterPro; IPR000745; HCV_NS4a.
DR InterPro; IPR001490; HCV_NS4b.
DR InterPro; IPR002868; HCV_NS5a.
DR InterPro; IPR013192; HCV_NS5A_1a.
DR InterPro; IPR013193; HCV_NS5a_1B_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR004109; NS3_Peptidase_S29.
DR InterPro; IPR038170; NS5A_1a_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF01542; HCV_core; 1.
DR Pfam; PF01539; HCV_env; 1.
DR Pfam; PF01538; HCV_NS2; 1.
DR Pfam; PF01006; HCV_NS4a; 1.
DR Pfam; PF01001; HCV_NS4b; 1.
DR Pfam; PF01506; HCV_NS5a; 1.
DR Pfam; PF08300; HCV_NS5a_1a; 1.
DR Pfam; PF08301; HCV_NS5a_1b; 1.
DR Pfam; PF02907; Peptidase_S29; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51693; HCV_NS2_PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51822; HV_PV_NS3_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; Apoptosis;
KW ATP-binding; Capsid protein;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW Host cytoplasm; Host endoplasmic reticulum; Host lipid droplet;
KW Host membrane; Host mitochondrion; Host nucleus; Host-virus interaction;
KW Hydrolase; Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
KW Interferon antiviral system evasion; Ion channel; Ion transport;
KW Lipoprotein; Magnesium; Manganese; Membrane; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Oncogene; Palmitate; Phosphoprotein; Protease; Ribonucleoprotein;
KW RNA-binding; RNA-directed RNA polymerase; Serine protease; SH3-binding;
KW Thiol protease; Transcription; Transcription regulation; Transferase;
KW Transmembrane; Transmembrane helix; Transport;
KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion;
KW Viral ion channel; Viral nucleoprotein;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus entry into host cell; Zinc.
FT CHAIN 1..2864
FT /note="Genome polyprotein"
FT /id="PRO_0000450895"
FT CHAIN 1..156
FT /note="Core protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037678"
FT CHAIN 157..349
FT /note="Envelope glycoprotein E1"
FT /id="PRO_0000037679"
FT CHAIN 350..613
FT /note="Envelope glycoprotein E2"
FT /id="PRO_0000037680"
FT CHAIN 614..732
FT /note="p13"
FT /evidence="ECO:0000305"
FT /id="PRO_0000037681"
FT CHAIN 614..669
FT /note="p6"
FT /id="PRO_0000284104"
FT CHAIN 670..732
FT /note="Viroporin p7"
FT /id="PRO_0000284105"
FT CHAIN 733..940
FT /note="Protease NS2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
FT /id="PRO_0000037682"
FT CHAIN 941..1564
FT /note="Serine protease/helicase NS3"
FT /id="PRO_0000037683"
FT CHAIN 1565..1615
FT /note="Non-structural protein 4A"
FT /id="PRO_0000037684"
FT CHAIN 1616..1863
FT /note="Non-structural protein 4B"
FT /id="PRO_0000037685"
FT CHAIN 1864..2274
FT /note="Non-structural protein 5A"
FT /id="PRO_0000037686"
FT CHAIN 2275..2864
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000037687"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1565..1585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1653..1673
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1678..1698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1722..1742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1783..1803
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1864..1884
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2844..2864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 819..940
FT /note="Peptidase C18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
FT DOMAIN 941..1122
FT /note="Peptidase S29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
FT DOMAIN 1131..1281
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1284..1449
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2485..2603
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2139..2178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2209..2266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1228..1231
FT /note="DECH box"
FT /evidence="ECO:0000250|UniProtKB:Q99IB8"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2225..2241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 870
FT /note="For protease NS2 activity; shared with dimeric
FT partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
FT ACT_SITE 888
FT /note="For protease NS2 activity; shared with dimeric
FT partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
FT ACT_SITE 909
FT /note="For protease NS2 activity; shared with dimeric
FT partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
FT ACT_SITE 997
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
FT ACT_SITE 1021
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
FT ACT_SITE 1079
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
FT BINDING 1037
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural; for NS3 protease activity and
FT NS2/3 auto-cleavage activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
FT BINDING 1039
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural; for NS3 protease activity and
FT NS2/3 auto-cleavage activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
FT BINDING 1085
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural; for NS3 protease activity and
FT NS2/3 auto-cleavage activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
FT BINDING 1089
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural; for NS3 protease activity and
FT NS2/3 auto-cleavage activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
FT BINDING 1144..1151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 1151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for NS3 helicase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9WMX2"
FT BINDING 1229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for NS3 helicase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9WMX2"
FT BINDING 1905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9WMX2"
FT BINDING 1923
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9WMX2"
FT BINDING 1925
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9WMX2"
FT BINDING 1947
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9WMX2"
FT BINDING 2491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P26663"
FT BINDING 2589
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P26663"
FT BINDING 2590
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P26663"
FT SITE 156..157
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P26662"
FT SITE 349..350
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P26662"
FT SITE 613..614
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000305"
FT SITE 669..670
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 732..733
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000305"
FT SITE 940..941
FT /note="Cleavage; by protease NS2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
FT SITE 1564..1565
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P27958"
FT SITE 1615..1616
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P27958"
FT SITE 1863..1864
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P27958"
FT SITE 2274..2275
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P27958"
FT LIPID 1863
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250|UniProtKB:P27958"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1273
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1559
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2640
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2722
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 395
FT /note="V -> I"
FT VARIANT 703
FT /note="D -> N"
FT VARIANT 706
FT /note="P -> H"
FT VARIANT 727
FT /note="A -> V"
FT VARIANT 791
FT /note="L -> F"
FT VARIANT 804
FT /note="T -> A"
FT VARIANT 940
FT /note="T -> M"
FT VARIANT 1879
FT /note="F -> L"
FT VARIANT 1895
FT /note="V -> A"
FT VARIANT 1919
FT /note="L -> P"
FT VARIANT 1945
FT /note="R -> K"
FT VARIANT 1966
FT /note="R -> G"
FT VARIANT 1973
FT /note="T -> P"
FT VARIANT 1979
FT /note="Y -> C"
FT VARIANT 1990
FT /note="L -> M"
FT VARIANT 2052
FT /note="K -> Q"
FT VARIANT 2082
FT /note="I -> T"
FT VARIANT 2095
FT /note="L -> P"
FT VARIANT 2097
FT /note="F -> I"
FT VARIANT 2174
FT /note="S -> P"
FT VARIANT 2196
FT /note="F -> L"
FT VARIANT 2201
FT /note="C -> R"
FT VARIANT 2203
FT /note="M -> V"
FT VARIANT 2221
FT /note="E -> G"
FT VARIANT 2228
FT /note="G -> E"
FT VARIANT 2233
FT /note="T -> A"
FT VARIANT 2244
FT /note="P -> L"
FT VARIANT 2268
FT /note="G -> E"
FT VARIANT 2271
FT /note="E -> K"
FT VARIANT 2833
FT /note="V -> I"
FT MUTAGEN 613
FT /note="G->A: Reduces cleavage between E2 and p13."
FT /evidence="ECO:0000269|PubMed:16492760"
FT MUTAGEN 669
FT /note="G->N: Reduces cleavage between E2 and p13."
FT /evidence="ECO:0000269|PubMed:16492760"
FT MUTAGEN 730..732
FT /note="ASA->NSN: Reduces cleavage between p13 and NS2-3."
FT /evidence="ECO:0000269|PubMed:16492760"
FT MUTAGEN 1150
FT /note="K->A: Complete loss of ATPase and dsRNA unwinding
FT activities."
FT /evidence="ECO:0000269|PubMed:10497107"
FT HELIX 745..761
FT /evidence="ECO:0007829|PDB:2LZP"
FT TURN 766..768
FT /evidence="ECO:0007829|PDB:2LZQ"
FT HELIX 769..785
FT /evidence="ECO:0007829|PDB:2LZQ"
FT HELIX 849..865
FT /evidence="ECO:0007829|PDB:2MKB"
SQ SEQUENCE 2864 AA; 312705 MW; 5F5A7D8FAF0CDE81 CRC64;
MPVISTQTSP VPAPRTRKNK QTQASYPVSI KTSVERGQRA KRKVQRDARP RNYKIAGIHD
GLQTLAQAAL PAHGWGRQDP RHKSRNLGIL LDYPLGWIGD VTTHTPLVGP LVAGAVVRPV
CQIVRLLEDG VNWATGWFGV HLFVVCLLSL ACPCSGARVT DPDTNTTILT NCCQRNQVIY
CSPSTCLHEP GCVICADECW VPANPYISHP SNWTGTDSFL ADHIDFVMGA LVTCDALDIG
ELCGACVLVG DWLVRHWLIH IDLNETGTCY LEVPTGIDPG FLGFIGWMAG KVEAVIFLTK
LASQVPYAIA TMFSSVHYLA VGALIYYASR GKWYQLLLAL MLYIEATSGN PIRVPTGCSI
AEFCSPLMIP CPCHSYLSEN VSEVICYSPK WTRPVTLEYN NSISWYPYTI PGARGCMVKF
KNNTWGCCRI RNVPSYCTMG TDAVWNDTRN TYEACGVTPW LTTAWHNGSA LKLAILQYPG
SKEMFKPHNW MSGHLYFEGS DTPIVYFYDP VNSTLLPPER WARLPGTPPV VRGSWLQVPQ
GFYSDVKDLA TGLITKDKAW KNYQVLYSAT GALSLTGVTT KAVVLILLGL CGSKYLILAY
LCYLSLCFGR ASGYPLRPVL PSQSYLQAGW DVLSKAQVAP FALIFFICCY LRCRLRYAAL
LGFVPMAAGL PLTFFVAAAA AQPDYDWWVR LLVAGLVLWA GRDRGPRIAL LVGPWPLVAL
LTLLHLATPA SAFDTEIIGG LTIPPVVALV VMSRFGFFAH LLPRCALVNS YLWQRWENWF
WNVTLRPERF LLVLVCFPGA TYDTLVTFCV CHVALLCLTS SAASFFGTDS RVRAHRMLVR
LGKCHAWYSH YVLKFFLLVF GENGVFFYKH LHGDVLPNDF ASKLPLQEPF FPFEGKARVY
RNEGRRLACG DTVDGLPVVA RLGDLVFAGL AMPPDGWAIT APFTLQCLSE RGTLSAMAVV
MTGIDPRTWT GTIFRLGSLA TSYMGFVCDN VLYTAHHGSK GRRLAHPTGS IHPITVDAAN
DQDIYQPPCG AGSLTRCSCG ETKGYLVTRL GSLVEVNKSD DPYWCVCGAL PMAVAKGSSG
APILCSSGHV IGMFTAARNS GGSVSQIRVR PLVCAGYHPQ YTAHATLDTK PTVPNEYSVQ
ILIAPTGSGK STKLPLSYMQ EKYEVLVLNP SVATTASMPK YMHATYGVNP NCYFNGKCTN
TGASLTYSTY GMYLTGACSR NYDVIICDEC HATDATTVLG IGKVLTEAPS KNVRLVVLAT
ATPPGVIPTP HANITEIQLT DEGTIPFHGK KIKEENLKKG RHLIFEATKK HCDELANELA
RKGITAVSYY RGCDISKIPE GDCVVVATDA LCTGYTGDFD SVYDCSLMVE GTCHVDLDPT
FTMGVRVCGV SAIVKGQRRG RTGRGRAGIY YYVDGSCTPS GMVPECNIVE AFDAAKAWYG
LSSTEAQTIL DTYRTQPGLP AIGANLDEWA DLFSMVNPEP SFVNTAKRTA DNYVLLTAAQ
LQLCHQYGYA APNDAPRWQG ARLGKKPCGV LWRLDGADAC PGPEPSEVTR YQMCFTEVNT
SGTAALAVGV GVAMAYLAID TFGATCVRRC WSITSVPTGA TVAPVVDEEE IVEECASFIP
LEAMVAAIDK LKSTITTTSP FTLETALEKL NTFLGPHAAT ILAIIEYCCG LVTLPDNPFA
SCVFAFIAGI TTPLPHKIKM FLSLFGGAIA SKLTDARGAL AFMMAGAAGT ALGTWTSVGF
VFDMLGGYAA ASSTACLTFK CLMGEWPTMD QLAGLVYSAF NPAAGVVGVL SACAMFALTT
AGPDHWPNRL LTMLARSNTV CNEYFIATRD IRRKILGILE ASTPWSVISA CIRWLHTPTE
DDCGLIAWGL EIWQYVCNFF VICFNVLKAG VQSMVNIPGC PFYSCQKGYK GPWIGSGMLQ
ARCPCGAELI FSVENGFAKL YKGPRTCSNY WRGAVPVNAR LCGSARPDPT DWTSLVVNYG
VRDYCKYEKL GDHIFVTAVS SPNVCFTQVP PTLRAAVAVD GVQVQCYLGE PKTPWTTSAC
CYGPDGKGKT VKLPFRVDGH TPGVRMQLNL RDALETNDCN SINNTPSDEA AVSALVFKQE
LRRTNQLLEA ISAGVDTTKL PAPSIEEVVV RKRQFRARTG SLTLPPPPRS VPGVSCPESL
QRSDPLEGPS NLPSSPPVLQ LAMPMPLLGA GECNPFTAIG CAMTETGGGP DDLPSYPPKK
EVSEWSDGSW STTTTASSYV TGPPYPKIRG KDSTQSAPAK RPTKKKLGKS EFSCSMSYTW
TDVISFKTAS KVLSATRAIT SGFLKQRSLV YVTEPRDAEL RKQKVTINRQ PLFPPSYHKQ
VRLAKEKASK VVGVMWDYDE VAAHTPSKSA KSHITGLRGT DVRSGAARKA VLDLQKCVEA
GEIPSHYRQT VIVPKEEVFV KTPQKPTKKP PRLISYPHLE MRCVEKMYYG QVAPDVVKAV
MGDAYGFVDP RTRVKRLLSM WSPDAVGATC DTVCFDSTIT PEDIMVETDI YSAAKLSDQH
RAGIHTIARQ LYAGGPMIAY DGREIGYRRC RSSGVYTTSS SNSLTCWLKV NAAAEQAGMK
NPRFLICGDD CTVIWKSAGA DADKQAMRVF ASWMKVMGAP QDCVPQPKYS LEELTSCSSN
VTSGITKSGK PYYFLTRDPR IPLGRCSAEG LGYNPSAAWI GYLIHHYPCL WVSRVLAVHF
MEQMLFEDKL PETVTFDWYG KNYTVPVEDL PSIIAGVHGI EAFSVVRYTN AEILRVSQSL
TDMTMPPLRA WRKKARAVLA SAKRRGGAHA KLARFLLWHA TSRPLPDLDK TSVARYTTFN
YCDVYSPEGD VFVTPQRRLQ KFLVKYLAVI VFALGLIAVG LAIS
