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Genome polyprotein

 POLG_BANV               Reviewed;        3393 AA.
C8XPA8;
27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 1.
27-SEP-2017, entry version 64.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Non-structural protein 2A-alpha;
Short=NS2A-alpha;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Flavivirin protease NS3 catalytic subunit;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Peptide 2k;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=Non-structural protein 5;
Banzi virus (BANV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Yellow fever virus group.
NCBI_TaxID=38837;
NCBI_TaxID=7157; Culicidae (mosquitos).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9989; Rodentia.
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=SAH 336 {ECO:0000312|EMBL:ABI54472.1};
PubMed=19741066; DOI=10.1099/vir.0.014506-0;
Grard G., Moureau G., Charrel R.N., Holmes E.C., Gould E.A.,
de Lamballerie X.;
"Genomics and evolution of Aedes-borne flaviviruses.";
J. Gen. Virol. 91:87-94(2010).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to the cell membrane and gathering the viral RNA into a
nucleocapsid that forms the core of a mature virus particle.
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can
migrate to the cell nucleus where it modulates host functions.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000250|UniProtKB:P03314}.
-!- FUNCTION: Peptide pr: Prevents premature fusion activity of
envelope proteins in trans-Golgi by binding to envelope protein E
at pH6.0. After virion release in extracellular space, gets
dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network probably to avoid
catastrophic activation of the viral fusion activity in acidic
Golgi compartment prior to virion release. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M ectodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particule is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. Essential for viral replication. Required for
formation of the replication complex and recruitment of other non-
structural proteins to the ER-derived membrane structures.
Excreted as a hexameric lipoparticle that plays a role against
host immune response. Antagonizing the complement function. Binds
to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA helicase. NS3 serine
protease, in association with NS2B, performs its autocleavage and
cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
Also plays a role in virus assembly (By similarity).
{ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 4B: Induces the formation of ER-
derived membrane vesicles where the viral replication takes place.
Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
nuclear translocation, thereby preventing the establishment of
cellular antiviral state by blocking the IFN-alpha/beta pathway.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) RNA genome, and performs the capping of genomes in the
cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
2'-O positions (By similarity). Besides its role in RNA genome
replication, also prevents the establishment of cellular antiviral
state by blocking the interferon-alpha/beta (IFN-alpha/beta)
signaling pathway. IFN-I induces binding of NS5 to host IFN-
activated transcription factor STAT2, preventing its
transcriptional activity. Host TRIM23 is the E3 ligase that
interacts with and polyubiquitinates NS5 to promote its binding to
STAT2 and trigger IFN-I signaling inhibition.
{ECO:0000250|UniProtKB:P03314}.
-!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
in which each of the Xaa can be either Arg or Lys and Yaa can be
either Ser or Ala.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{ECO:0000255|PROSITE-ProRule:PRU00924}.
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway.
Protein prM: Forms heterodimers with envelope protein E in the
endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
the endoplasmic reticulum and Golgi. Interacts with protein prM.
Interacts with non-structural protein 1. Non-structural protein 1:
Homodimer; Homohexamer when secreted. Interacts with envelope
protein E. Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3. Non-structural protein 2B: Forms a
heterodimer with serine protease NS3. May form homooligomers.
Serine protease NS3: Forms a heterodimer with NS2B. Interacts with
non-structural protein 2A (via N-terminus). Interacts with NS4B.
Interacts with unphosphorylated RNA-directed RNA polymerase NS5;
this interaction stimulates RNA-directed RNA polymerase NS5
guanylyltransferase activity. NS3 interacts with host PDCD6IP;
this interaction contributes to virion release. Non-structural
protein 4B: Interacts with serine protease NS3. RNA-directed RNA
polymerase NS5: Homodimer. Interacts with host STAT2; this
interaction prevents the establishment of cellular antiviral
state. Interacts with host TRIM23; this interaction leads to NS5
ubiquitination. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000305}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane; Peripheral membrane protein; Lumenal side
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
Peripheral membrane protein {ECO:0000255|PROSITE-
ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
ProRule:PRU00860}. Note=Remains non-covalently associated to
serine protease subunit NS2B. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-associated vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-derived vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
endoplasmic reticulum membrane; Peripheral membrane protein;
Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}.
Note=Located in RE-associated vesicles hosting the replication
complex. NS5 protein is mainly localized in the nucleus rather
than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M
and envelope protein E contain an endoplasmic reticulum retention
signal. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. The nascent capsid protein C contains a C-
terminal hydrophobic domain that act as a signal sequence for
translocation of prM into the lumen of the ER. Mature capsid
protein C is cleaved at a site upstream of this hydrophobic domain
by NS3. prM is cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
Non-structural protein 2A-alpha, a C-terminally truncated form of
non-structural protein 2A, results from partial cleavage by NS3.
Specific enzymatic cleavages in vivo yield mature proteins peptide
2K acts as a signal sequence and is removed from the N-terminus of
NS4B by the host signal peptidase in the ER lumen. Signal cleavage
at the 2K-4B site requires a prior NS3 protease-mediated cleavage
at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}.
-!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
This cleavage is incomplete as up to 30% of viral particles still
carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
is glycosylated and this is required for efficient secretion of
the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Polyubiquitinated; ubiquitination is probably mediated by
host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is
not ISGylated or sumoylated. {ECO:0000250|UniProtKB:P03314}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- SIMILARITY: In the N-terminal section; belongs to the class I-like
SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
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EMBL; DQ859056; ABI54472.1; -; Genomic_RNA.
RefSeq; YP_009222007.1; NC_029054.1.
ProteinModelPortal; C8XPA8; -.
MEROPS; S07.001; -.
GeneID; 29122460; -.
KEGG; vg:29122460; -.
Proteomes; UP000140353; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
3: Inferred from homology;
Activation of host autophagy by virus; ATP-binding; Capsid protein;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
GTP-binding; Helicase; Host cytoplasm; Host endoplasmic reticulum;
Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
Membrane; Metal-binding; Methyltransferase; mRNA capping;
mRNA processing; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
S-adenosyl-L-methionine; Secreted; Serine protease;
Suppressor of RNA silencing; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation; Viral attachment to host cell;
Viral immunoevasion; Viral penetration into host cytoplasm;
Viral RNA replication; Virion; Virus entry into host cell; Zinc.
CHAIN 1 3393 Genome polyprotein.
/FTId=PRO_0000441439.
CHAIN 1 90 Capsid protein C.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441440.
PROPEP 91 108 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441441.
CHAIN 109 272 prM. {ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000441442.
CHAIN 109 197 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000441443.
CHAIN 198 272 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000441444.
CHAIN 273 763 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000441445.
CHAIN 764 1115 Non-structural protein 1.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441446.
CHAIN 1116 1340 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441447.
CHAIN 1116 1306 Non-structural protein 2A-alpha.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000441448.
CHAIN 1341 1469 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441449.
CHAIN 1470 2089 Serine protease NS3.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441450.
CHAIN 2090 2213 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441451.
PEPTIDE 2214 2236 Peptide 2k.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441452.
CHAIN 2237 2488 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441453.
CHAIN 2489 3393 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441454.
TOPO_DOM 1 91 Cytoplasmic. {ECO:0000255}.
TRANSMEM 92 112 Helical. {ECO:0000255}.
TOPO_DOM 113 231 Extracellular. {ECO:0000255}.
TRANSMEM 232 252 Helical. {ECO:0000255}.
TOPO_DOM 253 257 Cytoplasmic. {ECO:0000255}.
TRANSMEM 258 272 Helical. {ECO:0000305}.
TOPO_DOM 273 713 Extracellular. {ECO:0000255}.
TRANSMEM 714 734 Helical. {ECO:0000255}.
TOPO_DOM 735 745 Cytoplasmic. {ECO:0000255}.
TRANSMEM 746 763 Helical. {ECO:0000305}.
TOPO_DOM 764 1112 Extracellular. {ECO:0000255}.
TRANSMEM 1113 1133 Helical. {ECO:0000255}.
TOPO_DOM 1134 1186 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1187 1207 Helical. {ECO:0000255}.
TOPO_DOM 1208 1283 Lumenal. {ECO:0000255}.
TRANSMEM 1284 1304 Helical. {ECO:0000255}.
TOPO_DOM 1305 1341 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1342 1362 Helical. {ECO:0000255}.
TOPO_DOM 1363 1365 Lumenal. {ECO:0000255}.
TRANSMEM 1366 1386 Helical. {ECO:0000255}.
TOPO_DOM 1387 1438 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1439 1459 Helical. {ECO:0000255}.
TOPO_DOM 1460 2137 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2138 2158 Helical. {ECO:0000255}.
TOPO_DOM 2159 2168 Lumenal. {ECO:0000255}.
INTRAMEM 2169 2184 Helical. {ECO:0000305}.
TOPO_DOM 2185 2185 Lumenal. {ECO:0000255}.
TRANSMEM 2186 2206 Helical. {ECO:0000255}.
TOPO_DOM 2207 2221 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2222 2236 Helical; Note=Signal for NS4B.
{ECO:0000305}.
TOPO_DOM 2237 2275 Lumenal. {ECO:0000255}.
INTRAMEM 2276 2296 Helical. {ECO:0000255}.
TOPO_DOM 2297 2344 Lumenal. {ECO:0000255}.
TRANSMEM 2345 2365 Helical. {ECO:0000255}.
TOPO_DOM 2366 2408 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2409 2429 Helical. {ECO:0000255}.
TOPO_DOM 2430 2457 Lumenal. {ECO:0000255}.
TRANSMEM 2458 2478 Helical. {ECO:0000255}.
TOPO_DOM 2479 3393 Cytoplasmic. {ECO:0000255}.
DOMAIN 1470 1649 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1653 1809 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1804 1984 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2489 2753 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3017 3169 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1666 1673 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 28 60 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 370 383 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1393 1432 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1657 1660 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1757 1760 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 2860 2893 Nuclear localization signal.
{ECO:0000250}.
ACT_SITE 1521 1521 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1545 1545 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1606 1606 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2549 2549 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2634 2634 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2670 2670 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2706 2706 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2927 2927 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2931 2931 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2936 2936 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2939 2939 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3204 3204 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3220 3220 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3339 3339 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2501 2501 mRNA cap. {ECO:0000250|UniProtKB:P03314}.
BINDING 2504 2504 mRNA cap; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P03314}.
BINDING 2505 2505 mRNA cap. {ECO:0000250|UniProtKB:P03314}.
BINDING 2507 2507 mRNA cap; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P03314}.
BINDING 2516 2516 mRNA cap. {ECO:0000250|UniProtKB:P03314}.
BINDING 2544 2544 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2574 2574 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2575 2575 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2592 2592 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2593 2593 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2619 2619 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2620 2620 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2638 2638 mRNA cap. {ECO:0000250|UniProtKB:P03314}.
BINDING 2701 2701 mRNA cap. {ECO:0000250|UniProtKB:P03314}.
BINDING 2703 2703 mRNA cap. {ECO:0000250|UniProtKB:P03314}.
BINDING 2708 2708 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 90 91 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 108 109 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 197 198 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P06935}.
SITE 272 273 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 763 764 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 1115 1116 Cleavage; by host.
{ECO:0000250|UniProtKB:P06935}.
SITE 1340 1341 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 1469 1470 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P06935}.
SITE 1927 1927 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1930 1930 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2089 2090 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P06935}.
SITE 2213 2214 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 2236 2237 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 2488 2489 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 2512 2512 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2549 2549 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2634 2634 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2635 2635 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2670 2670 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2706 2706 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2544 2544 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 893 893 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 969 969 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 970 970 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 275 302 {ECO:0000250|UniProtKB:P17763}.
DISULFID 346 377 {ECO:0000250|UniProtKB:P17763}.
DISULFID 364 388 {ECO:0000250|UniProtKB:P17763}.
DISULFID 453 553 {ECO:0000250|UniProtKB:P17763}.
DISULFID 570 600 {ECO:0000250|UniProtKB:P17763}.
DISULFID 767 778 {ECO:0000250|UniProtKB:P17763}.
DISULFID 818 905 {ECO:0000250|UniProtKB:P17763}.
DISULFID 941 986 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1043 1092 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1054 1076 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1054 1075 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1075 1079 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1076 1079 {ECO:0000250|UniProtKB:Q9Q6P4}.
SEQUENCE 3393 AA; 375607 MW; 8904BB7A51011FC4 CRC64;
MVNPKGVNVM AARVKRAAQK TKKKAVQVSR GLRGFVLFVL TQLFMGRKLT PNVRRLWKSS
DKNSLIHVLT KIKKIVGNLL MGVSRRKKRR SATTSGTVFM AMLGLTLAAS VARHAHHTLI
NITKDDAHKL LTLRNGNCTV VATDIGNWCP DNVEYDCVTL QDNEDPDDVD CWCYRVNNVR
VTYGRCKDGN TPRRSKRAVV ITAHLDQGLT TKKETWLGSS HFETQVQKVE KWIIRNPTYA
IAAILMSWYI GNSLKQRVVL LLLTLALGPA YATHCVGIPK RDFVQGVQGT TWVNLVLEQG
GCVTIMAEGK PSVDVWMDNI KFTSPTLVRR ISHTATISDT KIATACPSNG EAKLDEEHIK
EYACKRLYSD RGWGNGCGLF GKGSLVACAK YESTGHMDVY EMDMTKVEYT VKTQVHSGAK
SGDLSGVKTV SFAPTSGSQP VEFSGYGNMG LQCMIQSNVD FSTHYLVVMG NDAWLVHKAW
VEDITLPWKH GEGGTWKDKQ YMVEFGEPHA TTVKVLALGP QEGALRNALA GAMIVTYESS
GKTFKLHGGH VTCKATVSGL ALKGTTYTNC RGGLSFVKTP TDTGHGTVVM QVKVAKSAPC
RLTAIAADDA SGHVNRGTLV TSNPIAASNN DEVMIEINPP YGTSYLIVGV GDDKLVYQWK
KSGSTIGSLF SETVKGAQRM AIVGSSSWDF SSTSGFFSSV GKAIHTVFGT AFHGIFGGLS
WMTRILIGVL LVWLGLNSRN GTATTLMMLT GFIILFLSLG VGAEVGCSVN WGQKELKCGD
GIFVYNDVDD WMHKYKYHPE DPKVMAGLIA KAWEKGACGL TSVSELEHVM WVKIASEINA
ILEENEIDLT VVVHENKSVY RRGSRRFPRV ETELTYGWES WGKNFITDGK VSNNTFHVDG
KEDQCASKNR VWNSLEIEEF GFGVFHTNVF LRQKADKTNS CDTTLMGAAV KGNVAAHADP
GFWMESQENN GTWEIQSIEF TAYRECEWPV SHTVHGTQVM ESDMFMPKGI GGPVSHLNRM
QGYKVQTNGA WAYGKTVVQR ELCPDTSVVV DSSCSDRGKS IRSTTTEGKV IKEWCCRSCT
LPPVSYWTSE GCWYAMEVRP MKTPEKHLVR SWVTAGDSYP AWSIGLVAMF LFVDIMARSR
PTRKMMIGGT MLLLAIMIMG ELSYLDLLRY IIVVGEHFIE RENGGDVAYM AIMAASHLRP
GLMAMVFAKS MWSPKQRVLL ALGCAILQPF LTAQASALVW EWADSIGLVL LIVQGMVRNK
EKNWALVLLA LCSPVSMPVI RKASMIIGTG GLLLSLWKGG GSSMRKGLPL FAASAARVLG
LTKAHLSVLF ILLITKNGKR TWPISECLAA VGIFGAAFGT MFSEDETLLG PLALVGVVLI
VYTMFTQSDG LELVKAADIS WSDEAVVSGE ARRFDVALND SGEFKLLDEP PVSWLNVSFL
VVAIVASSLH PIALVVTLVA WTYWRTEKRS GVLWDVPLAP KVEACEHLED GVFRIIQKGL
FGSSQVGIGV AKDGVFHTMW HVTRGAFLMH SGKQLTPTWG SVRKDLVCYG GTWKLDGAWN
GVDEVQLIAV PPGKPATNVQ TKPGTFVLPT GDEAGAVLLD FPSGTSGSPI IDRHGNILGL
YGNGIVLENG AYASAISQAQ PGSVAEVETP GLDKMLRKGE FTMLDYHPGA GKTRKHLPNI
LKECERKRLR TLVLAPTRVV LSEMKEALTS VQAKFHTQAF NSTTTGREII DVMCHATFVH
RMLEGLRSGN WEVIIMDEAH FLDPTSIAAR GWAHHKSKTK ESAVIFMTAT PPGTSNEFPE
SNAEIEDVKK EIPSEPWSKG HEWILEDRRP TVWFLPSIKA ANVMAACLRK AERSVVVLNR
STFENVYPTI KTKKPDFILA TDIAEMGANL PVERVIDCRT AYKPVLVDER VALKGPLRIA
AAAAAQRRGR VGRNPDRDGD TYVYSEDTCE QNDHLVCWTE GSMLLDNMQV KGGFVAPLYE
EEASKTTMTP GECRLRDDQR KVFRTLIRKH DMPVWLSWQV AKSGLAADDR KWCFDGEDDN
AILGDNGEVI KARSPGGQRK ELKPRWSDAR IASDNTSLMN FIAFAEGRRS LPLSILWSVP
NQLSEKLVQS IDTLTILLRS EEGSRAHKLA LQQAPEAVST LLLLGMMAIC TLGLVILLMK
PKATDKMSMA MVTMAITGYL LKLGGMTHAQ VGGILLVFFI MMVVIIPESG TQRSINDNKL
AYVIILVGLV IGGVACNELG WLEKTKADLF GNNMTHAQTV VLPTINWNWL DFRPGAAWSL
YVGMATFLTP VFVHWIKNEY GNASLTGITP TAGILGALNQ GVPFVKLNTS VGVLLLSVWN
NFTTSSMLAA MVMLACHCLF VLPGVRAQCL REAQIRVFHG VAKNPMVDGN PTVDLEKEND
MPDLYEKKLA LVALGMAAVL NAAMVRTALT TAEMVVLGSA AVGPLLEGNT SAFWNGPLAV
AVAGVMRGNH YALIGIVYNL WLLKTARRGG SSALTYGEVW KRQLNLLGKQ EFMNYKVSDI
LEVDRSHARE VLNSGNDAVG VAVSRGSSKL NWLIERGYLR PTGRVVDLGC GRGGWSYTCA
AERQVTSVKA YTLGKEGHEK PRLIQSLGWN IIKFKDKSDI TRMTPHASDT LLCDIGESSS
NPEVEKERTL RVIEAVEKWM SPTTVSFCFK VLAPYKPDVI EALERFQLKH GGGIIRNPYS
RNSTHEMYYV SGVRNNILHM VNSTSRMLMR RMSRPSGRST VVPDLIYPTG TRSVASEAGP
LDLEKVKARI NRLKEEQEST WFVDSDHPYR TWHYHGSYVA KQSGTAASMI NGVVKLLSGP
WDRIEEVTNM AMTDTTPFGQ QRVFKEKVDT RAPEPPQGTR EIMKVVNQWL FDYLGRTKQP
RICTKEEFIN KVRSHAALGG ILTEQEGWSS AAEAVADPRF WSLVDKERQA HLEGRCETCI
YNMMGKREKK PSEFGRAKGS RAIWYMWLGA RFLEFEALGF LNEDHWLGRE NSKAGVEGIG
LQYLGYVVEE VARKGNGLVY ADDTAGWDTR ITEADLEDEQ YIMKRMSAEH RQLAWAVMEL
TYRNKVVKVP RPGPGGKILM DVISRRDQRG SGQVVTYPLN TATNMKVQLI RMAEAENVIT
RNDVEKVSLI TLKELQLWLE VNGVNRLERM AVSGDDCIVA PVDESFAGAL HHLNAMSKTR
KDISEWENSR GWTDWESVPF CSHHFHTLYL KDGRTIIAPC RCQDELIGRA RISPGNGWMI
KETAGLSKAY TQMWTLMYFH RRDLRLMANA ICSAVPIDWV PTGRTTWSIH ATGEWMSSDD
MLEVWNKVWI QDNPHVKDKT PIFAWRDVPY IQKGQDRACG SLVGTSLRAS WAESIMTSVH
RVRMLIGNER YVNYMESMDR YATQRCSAYG ELL


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