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Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

 POLG_ALKV               Reviewed;        3416 AA.
Q91B85;
27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
18-JUL-2018, entry version 133.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein 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=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;
Alkhumra hemorrhagic fever virus (ALKV) (Alkhurma hemorrhagic fever
virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=172148;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=34626; Hyalomma dromedarii.
NCBI_TaxID=69826; Ornithodoros savignyi.
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=1176 {ECO:0000312|EMBL:AAL08421.1};
PubMed=11554750; DOI=10.1006/bbrc.2001.5610;
Charrel R.N., Zaki A.M., Attoui H., Fakeeh M., Billoir F.,
Yousef A.I., de Chesse R., De Micco P., Gould E.A., de Lamballerie X.;
"Complete coding sequence of the Alkhurma virus, a tick-borne
flavivirus causing severe hemorrhagic fever in humans in Saudi
Arabia.";
Biochem. Biophys. Res. Commun. 287:455-461(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=1176 {ECO:0000312|EMBL:AAL08421.1};
PubMed=15890119;
Charrel R.N., Zaki A.M., Fakeeh M., Yousef A.I., de Chesse R.,
Attoui H., de Lamballerie X.;
"Low diversity of Alkhurma hemorrhagic fever virus, Saudi Arabia,
1994-1999.";
Emerg. Infect. Dis. 11:683-688(2005).
[3]
ELECTRON MICROSCOPY OF THE VIRION.
PubMed=28051359; DOI=10.1089/vbz.2016.2064;
Madani T.A., Abuelzein E.M., Jalalah S.M., Abu-Araki H., Azhar E.I.,
Hassan A.M., Al-Bar H.M.;
"Electron microscopy of Alkhumra hemorrhagic fever virus.";
Vector Borne Zoonotic Dis. 17:195-199(2017).
-!- 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: 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 particle 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.
{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.
Inhibits STAT2 translocation in the nucleus after IFN-alpha
treatment. {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. 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.
Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
activation of JAK-STAT signaling pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- 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
NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase
NS5; this interaction stimulates RNA-directed RNA polymerase NS5
guanylyltransferase activity. Non-structural protein 4B: Interacts
with serine protease NS3. RNA-directed RNA polymerase NS5:
Homodimer. Interacts with host STAT2; this interaction inhibits
the phosphorylation of the latter, and, when all viral proteins
are present (polyprotein), targets STAT2 for degradation.
Interacts with serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
-!- 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:P14335}; 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:P14335}; 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:P06935}.
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. Cleavages in the lumen of endoplasmic
reticulum are performed by host signal peptidase, whereas
cleavages in the cytoplasmic side are performed by serine protease
NS3. Signal cleavage at the 2K-4B site requires a prior NS3
protease-mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763}.
-!- 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: 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; AF331718; AAL08421.1; -; Genomic_DNA.
RefSeq; NP_722551.1; NC_004355.1.
ProteinModelPortal; Q91B85; -.
SMR; Q91B85; -.
IntAct; Q91B85; 37.
MINT; Q91B85; -.
GeneID; 955851; -.
KEGG; vg:955851; -.
Proteomes; UP000136346; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
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: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:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
Gene3D; 3.30.387.10; -; 2.
Gene3D; 3.30.67.10; -; 4.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_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; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
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; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
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; 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; 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.
1: Evidence at protein level;
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; 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; Viral attachment to host cell;
Viral immunoevasion; Viral penetration into host cytoplasm;
Viral RNA replication; Virion; Virus entry into host cell; Zinc.
CHAIN 1 3416 Genome polyprotein.
/FTId=PRO_0000441424.
CHAIN 1 96 Capsid protein C.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441425.
PROPEP 97 117 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441426.
CHAIN 118 281 Protein prM.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441427.
CHAIN 118 206 Peptide pr.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441428.
CHAIN 207 281 Small envelope protein M.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441429.
CHAIN 282 777 Envelope protein E.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441430.
CHAIN 778 1130 Non-structural protein 1.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441431.
CHAIN 1131 1360 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441432.
CHAIN 1361 1491 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441433.
CHAIN 1492 2112 Serine protease NS3.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441434.
CHAIN 2113 2238 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441435.
PEPTIDE 2239 2261 Peptide 2k.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441436.
CHAIN 2262 2513 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441437.
CHAIN 2514 3416 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000441438.
TOPO_DOM 1 99 Cytoplasmic. {ECO:0000255}.
TRANSMEM 100 120 Helical. {ECO:0000255}.
TOPO_DOM 121 243 Extracellular. {ECO:0000255}.
TRANSMEM 244 261 Helical. {ECO:0000305}.
TOPO_DOM 262 262 Cytoplasmic. {ECO:0000255}.
TRANSMEM 263 281 Helical. {ECO:0000305}.
TOPO_DOM 282 728 Extracellular. {ECO:0000255}.
TRANSMEM 729 749 Helical. {ECO:0000255}.
TOPO_DOM 750 756 Cytoplasmic. {ECO:0000255}.
TRANSMEM 757 777 Helical. {ECO:0000255}.
TOPO_DOM 778 1134 Extracellular. {ECO:0000255}.
TRANSMEM 1135 1155 Helical. {ECO:0000255}.
TOPO_DOM 1156 1162 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1163 1183 Helical. {ECO:0000255}.
TOPO_DOM 1184 1189 Lumenal. {ECO:0000255}.
TRANSMEM 1190 1210 Helical. {ECO:0000255}.
TOPO_DOM 1211 1235 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1236 1256 Helical. {ECO:0000255}.
TOPO_DOM 1257 1295 Lumenal. {ECO:0000255}.
TRANSMEM 1296 1316 Helical. {ECO:0000255}.
TOPO_DOM 1317 1361 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1362 1379 Helical. {ECO:0000255}.
TOPO_DOM 1380 1384 Lumenal. {ECO:0000255}.
TRANSMEM 1385 1405 Helical. {ECO:0000255}.
TOPO_DOM 1406 1458 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1459 1479 Helical. {ECO:0000255}.
TOPO_DOM 1480 2162 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2163 2183 Helical. {ECO:0000255}.
TOPO_DOM 2184 2191 Lumenal. {ECO:0000255}.
INTRAMEM 2192 2211 Helical. {ECO:0000255}.
TOPO_DOM 2212 2212 Lumenal. {ECO:0000255}.
TRANSMEM 2213 2233 Helical. {ECO:0000255}.
TOPO_DOM 2234 2246 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2247 2267 Helical. {ECO:0000255}.
TOPO_DOM 2268 2301 Lumenal. {ECO:0000255}.
INTRAMEM 2302 2322 Helical. {ECO:0000255}.
TOPO_DOM 2323 2345 Lumenal. {ECO:0000255}.
INTRAMEM 2346 2366 Helical. {ECO:0000255}.
TOPO_DOM 2367 2368 Lumenal. {ECO:0000255}.
TRANSMEM 2369 2389 Helical. {ECO:0000255}.
TOPO_DOM 2390 2432 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2433 2453 Helical. {ECO:0000255}.
TOPO_DOM 2454 2476 Lumenal. {ECO:0000255}.
TRANSMEM 2477 2497 Helical. {ECO:0000255}.
TOPO_DOM 2498 3416 Cytoplasmic. {ECO:0000255}.
DOMAIN 1492 1671 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1677 1833 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1844 2002 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2514 2778 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3042 3191 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1690 1697 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 379 392 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1412 1451 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 2732 2736 Interaction with host SCRIB.
{ECO:0000250|UniProtKB:Q01299}.
MOTIF 1781 1784 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
COMPBIAS 2203 2206 Poly-Leu. {ECO:0000255}.
ACT_SITE 1545 1545 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1569 1569 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1629 1629 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2574 2574 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2659 2659 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2696 2696 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2732 2732 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2952 2952 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2956 2956 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2961 2961 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2964 2964 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3226 3226 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3242 3242 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3361 3361 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2526 2526 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2529 2529 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2530 2530 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2532 2532 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2541 2541 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2569 2569 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2599 2599 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2600 2600 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2617 2617 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2618 2618 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2644 2644 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2645 2645 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2663 2663 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2727 2727 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2729 2729 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2734 2734 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 97 98 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 118 119 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 206 207 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P06935}.
SITE 281 282 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 777 778 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 1130 1131 Cleavage; by host.
{ECO:0000250|UniProtKB:P06935}.
SITE 1360 1361 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 1491 1492 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03314}.
SITE 1951 1951 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1954 1954 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2112 2113 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03314}.
SITE 2238 2239 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 2261 2262 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 2513 2514 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 2537 2537 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2574 2574 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2659 2659 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2660 2660 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2696 2696 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2732 2732 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2569 2569 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 862 862 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 985 985 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1001 1001 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 284 311 {ECO:0000250|UniProtKB:P06935}.
DISULFID 341 402 {ECO:0000250|UniProtKB:P17763}.
DISULFID 341 397 {ECO:0000250|UniProtKB:P06935}.
DISULFID 355 386 {ECO:0000250|UniProtKB:P06935}.
DISULFID 373 402 {ECO:0000250|UniProtKB:P06935}.
DISULFID 373 397 {ECO:0000250|UniProtKB:P17763}.
DISULFID 467 571 {ECO:0000250|UniProtKB:P06935}.
DISULFID 588 619 {ECO:0000250|UniProtKB:P06935}.
DISULFID 781 792 {ECO:0000250|UniProtKB:P17763}.
DISULFID 832 922 {ECO:0000250|UniProtKB:P17763}.
DISULFID 957 1002 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1059 1108 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1070 1092 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1091 1095 {ECO:0000250|UniProtKB:P17763}.
SEQUENCE 3416 AA; 378122 MW; EDAB88E8A9DD7A27 CRC64;
MAKGAVLKGK GGGPPRRVPK ETAKKTRQGP GRLPNGLVLM RMMGVLWHMI AGTARSPILK
RFWATVPVRQ AIAALRKIRK TVGLLLDSLN RRRGKRRSTT GLLTSILLAC LATLVISATI
RRERTGDMVI RAEGKDAATQ VEVVNGTCII LATDMGSWCD DSIMYECVTI DSGEEPVDVD
CFCRGVERVS LEYGRCGKPV GGRSRRSVSI PVHAHSDLTG RGHKWLRGDS VKTHLTRVEG
WVWKNKLLTM AFCAVVWMVT DSLPTRFIVI TVALCLAPTY ATRCTHLQNR DFVSGIQGTT
RVSLVLELGG CVTLTAEGKP SVDVWLDDIH QENPAKTREY CLHAKLASSK VVARCPAMGP
ATLPEEHQAS TVCRRDQSDR GWGNHCGLFG KGSIVACAKF ACEAKKKATG YVYDVNKITY
VVKVEPHTGD YLAANESHSN RKTASFTTQS EKTILTLGDY GDISLTCRVT SGVDPAQTVV
LELDKTAEHL PKAWQVHRDW FEDLSLPWRH EGAHEWNHAD RLVEFGEPHA VKMDIFNLGD
QTGILLKSLA GVPVANIEGS KYHLQSGHVT CDVGLEKLKM KGMTYTVCEG SKFAWKRPPT
DSGHDTVVME VTYTGSKPCR IPVRAVAHGE PNVNVASLIT PNPSMETTGG GFVELQLPPG
DNIIYVGELS HQWFQKGSTI GRVLEKTRRG IERLTVVGEH AWDFGSVGGV LSSVGKALHT
AFGAAFNTIF GGVGFLPRIL LGVALAWLGL NSRNPTLSVG FLITGGLVLT MTLGVGADMG
CAIDANRMEL RCGEGLVVWR EVTDWYDGYA FHPESPPVLA ASLKEAYEEG VCGIVPQNRL
EMAMWRRVEA VLNLALAESD ANLTVVVDRR DPSDYRGGKV GILKRSGKEM KTSWKGWSQS
FVWSVPESPR RFMVGIEGTG ECPLDKRRTG VFTVAEFGMG MRTKIFLDLR ETSSSDCDTG
VMGAAVKSGH AVHTDQSLWM KSHRNATGVF ISELIVTDLR NCTWPASHTL DNAGVVDSKL
FLPVSLAGPR SHYNHIPGYA EQVRGPWNQT PLRVVREPCP GTTVKIDQNC DKRGSSLRST
TESGKAIPEW CCRTCELPPV TFRSGTDCWY AMEIRPVHQQ GGLVRSMVLA DNGAMLSEGG
VPGIVAVFVV LELVIRRRPT TGTSVVWCGV VVLGLVVTGL VTIEGLCRYV VAVGILMSME
LGPEIVALVL LQAVFDMRTG LLVAFAVKRA YTTREAVVTY FLLLVLELGF PEASLSNIWK
WADSLAMGTL ILQACSQEGR ARVGYLLAAM MTQKDMAIIH TGLTIFLSAA TAMAVWSMIK
GQRDQKGLSW ATPLVGLFGG EGVGLRLLAF RRLAERRNRR SFSEPLTVVG VMLTVASGMV
RHTSQEALCA LVAGAFLLLM MVLGTRKMQL IAEWCGEVEW NPDLVNEGGE VNLKVRQDAM
GNLHLTEVEK EERAMALWLL AGLVASAFHW AGILIVLAIW TFFEMLSSGR RSELVFSGQG
TRTERNRPFE IKDGAYRIYS PGLLWGHRQI GVGYGAKGVL HTMWHVTRGA ALVVEEAISG
PYWADVREDV VCYGGAWSLE SRWRGETVQV HAFPPGRPQE THQCQPGELI LENGRKLGAV
PIDLSKGTSG SPIINAQGEV VGLYGNGLKT NEAYVSSIAQ GEAEKSRPEL PLSVQGTGWM
SKGQITVLDM HPGSGKTHRV LPELVRQCAN RGMRTLVLAP TRVVLKEMEK ALAGKKVRFH
SPAVEGQSTA GAVVDVMCHA TYVHRRLLPQ GRQNWEVAIM DEAHWTDPHS IAARGHLYSL
AKENRCALVL MTATPPGRGD PFPESNGAIM SEERAIPDGE WREGFDWITE YEGRTAWFVP
SISKGGAIAR TLRQRGKSVI CLNSKTFEKD YLRVREEKPD FVVTTDISEM GANLDVSRVI
DGRTNIKPEE VDGKVEMTGT RKITTASAAQ RRGRVGRTSG RTDEYIYSGQ CDDDDTSLVQ
WKEAQILLDN ITTLRGPVAT FYGPEQMKMP EVAGHYRLNE EKRKHFRHLM TQCDFTPWLA
WHVATNTSNV LDRSWTWQGP EGNAIDGADG DLVRFKTPGG SERVLQPVWK DCRMFREGRD
VKDFILYASG RRSVGDVLGG LAGVPGLLRH RCASALDVVY TLLNENPGSR AMRMAERDAP
EAFLTIVEVA VLGVATLGIL WCFVARTSVS RMFLGTVVLF AALLLLWIGG VDYGYMAGIA
LIFYIFLTVL QPEPGKQRSS DDNRLAYFLL GLLSLAGLVT ANEMGMLDKT KADLAGLMWH
GEQRHPAWEE WTNVDIQPAR SWGTYVLIVS LFTPYMLHQL QTKIQQLVNS SVASGAQAMR
DLGGGTPFFG VAGHVIALGV TSLVGATPLS LGLGVALAAF HLAIVASGLE AELTQRAHRV
FFSAMVKNPM VDGDVINPFP DGEPKPVLYE RRMSLILAIA LCMVSVVLNR TAASMTEAGA
VGLAALGQLV HPETETLWTM PMACGMAGLV RGSFWGLLPM GHRLWLKTTG TRRGGADGET
LGDIWKRRLN GCSREEFFQY RRSGVMETER DRARELLKRG ETNMGLAVSR GTAKLAWLEE
RGYATLKGEV VDLGCGRGGW SYYAASRPAV MGVKAYTIGG KGHEVPRLIT SLGWNLIKFR
TGMDVYSLEA HRADTILCDI GESNPDPLVE GERSRRVILL MEKWKLRNPD ASCVFKVLAP
YRPEVLEALH RFQLQWGGGL VRVPFSRNST HEMYFSTAVS GNIVNSVNIQ SRKLLARFGD
QRGPAKVPEV DLGTGTRCVV LAEDKVREAD VAERITALKT QYGDSWHVDK EHPYRTWQYW
GSYKTEATGS AASLINGVVK LLSWPWNARE DVVRMAMTDT TAFGQQRVFK EKVDTKAQEP
QVGTKIIMRA VNDWILERLA GKKTPRLCTR EEFIAKVRSN AALGAWSDEQ NRWSNAREAV
EDPEFWRLVD EERERHLRGR CAQCVYNMMG KREKKLGEFG VAKGSRAIWY MWLGSRYLEF
EALGFLNEDH WASRDLSGAG VEGISLNYLG WHLKRLSELE GGLFYADDTA GWDTRITNAD
LEDEEQILRY LRGEHRTLAK TILEKAYHAK VVKVARPSSS GGCVMDIITR RDQRGSGQVV
TYALNTLTNI KVQLIRMMEG EGVIGPSDSQ DPRLLRVEAW LKEYGEERLT RMLVSGDDCV
VRPIDDRFGK ALYFLNDMAK VRKDIGEWEP SEGYSSWEEV PFCSHHFHEL TMKDGRVIIV
PCRDQDELVG RARVSPGCGW SVRETACLSK AYGQMWLLSY FHRRDLRTLG LAICSAVPID
WVPQGRTTWS IHASGAWMTT EDMLEVWNRV WILDNPFMSD KGKVKEWRDI PYLPKSQDGL
CSSLVGRRER AEWAKNIWGS VEKVRRMIGP ERYADYLSCM DRHELHWDLK LESNII


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