Reviewed
Aedes [TaxID: 7158]; Capra Hircus (Goat) [TaxID: 9925]; Homo Sapiens (Human) [TaxID: 9606]; Ovis Aries (Sheep) [TaxID: 9940]
Not Available
♦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)
♦ Non-structural protein 2A-alpha (NS2A-alpha)
♦ 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)]
♦ Protein prM
♦ Peptide pr
♦ Small envelope protein M (Matrix protein)
♦ Envelope protein E
♦ Non-structural protein 1 (NS1)
♦ Non-structural protein 2A (NS2A)
♦ Non-structural protein 2A-alpha (NS2A-alpha)
♦ 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)]
Wesselsbron Virus (WSLV)
Viruses> SsRNA Viruses> SsRNA Positive-strand Viruses> No DNA Stage> Flaviviridae> Flavivirus (arboviruses Group B)> Yellow Fever Virus Group> Wesselsbron Virus (WSLV)
Various pathway(s) in which protein is involved
Not Available
MATKGMNKSRARSRGVNMVAARVKNLAVKVKNKTKQSARGLRGFLLFLVAQIFWARKLTPQVKRLWRMVDKVQGLRILKNIRNIVTNLMKGLAGRKKKRS
LTVPLVLLLIPLIAYSATVTRQRGLGLLLNVTFADVGKTYEVEGGNCSVNTLDAGKWCEDYVEYECVTLSEGEEPDDLDCWCYGVDNVRVTYGRCKSGGS
RRSRRSAVITPHVDKGLTTRQEKWLPTKIGEQQLQKVEKWIMRNPLYALGAVALAYFVGTSNVQRVVIAILLLGIGPAYSTHCLGIPKRDFIRGLDGNTW
VSVVLEQGSCVTLIADNKPSVDIWLSSIVVDTPTLVRKVCYASSVTGSKATGACPTMGDAHMSEEGNEEWECKRSYSDRGWGNGCGLFGKGSIVACAKFS
CTHEMEVYQIDATKIEYTISAQVHSGAKKDDWENHTKLVTFVPTTGTSTVAFTGYGNFGLECHVQMMVDLSNSYLVKVGTDAWLVNKQWVHDITLPWQSG
TGGHWRDKHFMVDFEEPHAVTMKALVLGSQEGALRTALSGAMVVELNSNRYSLKGGHVTCKAYMNNLILKGSTYSMCKRGMSFAKQPVETDHGTAVMQIK
VTTGAPCRIPVIAADSMAGTENRGSVITTNPIAASNNDEVLVEISPPFGESYIIVGNGDDKLTYHWQRSGSTIGNLFTETMKGAQRMIITGEHSWDFGST
GGFFSSIAKAVHTVFGAAFHAIFGGLSWITKILIGGLLIWLGLNSRSSSMSMGFICIGALLLVLATGVGAEVGCSLSWKQREMKCGDGVFVFKDSDDWFS
KYQYIPEDPKTMATLIHQAHQDGLCGLSSVSDLEHRMWYSRVDEINAILDENEVDLTVVVQESDAVYLRGSHAFPRPKSELKYGWKTWGKNIIFNPSRKN
GTFIIDGKSKAECPFNKRVWNSIRVEEFGTGVYQTRVFMRPEFDYTKLCDTGTLGAAVKGSVSAHGDPMFWMESEEINGTWMITTLEALNYRECEWPSSH
TLDGAKVVESDMFMPRSLAGPISKHNHIPGYKVQTSGPWHNVPLEIKREECPGTTVVVDEKCDDRAKSVRSTTDSGKIIPEWCCRSCTMPPVSFWGPDGC
WYSMEVRPKHTNEAHLVKSWVVASKGDVDPFSLGLLMLFLCSDMFLMKRFSMRAILVGSLVMLGAMTLGSLSYLDLLRYAITVGMYMAEINSGGDVTHLA
LLAVFRVRAGFVSMLALKRLWSPREGFVATCGIVMVQLALGDILSTDIMEWLNAAGMAVLIIKSIVEPKRCNAVLPLLCLLTPLTVAEIQRAVMFVCSIV
IFVTVWQTDSVSTRKTIPLVALTVCSFFKWTSPFLGIVCYLAFTRLPQRSWPLGETMAAVGLVGVLAGMGLKDMNGMLGPVAVGGVLLIVMSLSGKVDGL
VIKKVADVTWDEDAEISGASHRYDVEQTDTGEFKLRNEEPAPWIQVAVLTIAILSAATHPACLAVVTIGWFAWQKTTTRSGVLWDIPTVVPPEEVSYLED
GVYTINQNSFLGLAQKGVGVVKDGVFHTMWHVTRGAFLLHAGKRMTPSWANVKEDLISYGGGWKLDAKWDGSEEVQLIAVSPGKVPVNVQTTPSVFQLKN
GKEIGAVNLDYPSGTSGSPILNKNGDVIGLYGNGILIGNNTYVSAIAQSDSVEEGGTEQLQDIPTMLKKGMLTVLDFHPGAGKTRIYLPQILKECEKLKL
KTLVLAPTRVVLSEMREAMPKMSIKYHTQAFSNTSTGKEIIDAMCHATLTHRMLEPTRVTNWEVVIMDEAHFMDPASIAARGWAAHRSRARECATIFMSA
TPPGTSNEFPESNGMIEDVKKDVPSEPWTKGHEWILEDRRPTAWFLPSIRIANSIANCLRKADRTVVVLNRKTFEKEYPTIKSKKPDFILATDIAEMGAN
LKVERVIDCRTAYKPILVDDATKVMVKGPLRISASSAAQRRGRIGRDPNRDTDTYIYGDSTTEDNGHYVCWTEGSMLLDNMEIRNGMIAPLYGVEGTKTT
TSPGETRLREDQRKVFRELVKRLDMPVWFSWQVAKAGLKVQDRSWCFDGEDDNTLLNDNGEPILARSPGGAKKPLKPRWVDTRVCSDNASLIDFIKFAEG
RRSASGILLGLQGFPEFLSGKMREAIDTVTVLYTSDTGSRAYKHALAMMPEATTIFLLVMLAIICTSGVIMFFLAPKGLSRMSMAMMTMLVSAYLMSLGG
MNPVQISCVMLVFFIFMVVLIPEPGTQRSTYDNQIIYLLVGVLSLILLVAANEMELLEKTKRDIFGAVVVEEAKRWTFPEFDLRPGAAWTVYVGLVTPGN
PMLHHWIKIDYGNISLSGITQNAQVLGLMDRGIPFIKMNMSVVILLLSAWNGITLLPLFAGMGAAALHWGFILPGLRAQAAKAAQKRVYHGVAKNPVVDG
NPTVDIDDAPGMPAMYEKKLALVILLALSILNLVLTRTPFATAEMVVLGSAAVGPLIEGDTNAYWNGPIAVAFSGLMRGNYYATIGLAYNGWLAKQTRRG
KAAGVTLGEVWKRQLNMLGKQEFERYKVPDITEVDRTAARRYLKEGRTDVGISVSRGAAKIRWLHERGYLRITGRVLDLGCGRGGWSYYAAAQKEVMSVK
GYTLGIEGHEKPIHMQTLGWNIVKFKDKSNVFTMPTEPSDTLLCDIGESSSNPLVERDRTMKVLENFERWKHVNTENFCVKVLAPYHPDVIEKLERLQLR
FGGGIVRVPFSRNSTHEMYYISGARNNITHMVNTTSRSLLRRMTRPSGKAIIEGDVFLPTGTRSVASEAGTIDHEALKLRVDQIKAEYSKTWTHDSNHPY
RTWHYLGSYLCKATGSSSSMINGIVKMLSMPWDKFESVTLLAMTDTTPFGQQRVFKEKVDTKAPPPPPGTRAIMRVVNAWLFQHLARKKKPRICTREEFV
AKVRSHAALGAYLEEQDKWKSASEAVQDPQFWKLVDDERKLHLQGQCRTCVYNMMGKREKKPSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWVSR
ENSGGGVEGTGLQYLGYILKELGGKTGGNMYADDTAGWDTRITEEDLEDEQEILKYMDEKHKKLAWAVTELAYKNKVVKVMRPGPGGLTFMDIISRRDQR
GSGQVVTYALNTVTNLKVQLIRMAEAEHVITNFDVDTVSQKTLQDLRCWLDRFGADRLSRMAVSGDDCVVKPIDDQFADALTHLNSMSKIRKDIDDWKPS
QGWASWEDVPFCSHHFHELILKDGRSIIAPCRDQDELIGRARVSPGNGWMIRETACLSKAYAQMWLLMYFHRRDLRVMANAINSTVPVDWVPTGRTTWSI
HGKGEWMTTEDMLQVWNRVWIEDNPHQTDKTPITEWRDIPYLPKSIDKTCNSLVGTTQRASWARDIKHTVHRIRGLVGNEKYTDYLATMDRFRELDESGP
GEVLW
LTVPLVLLLIPLIAYSATVTRQRGLGLLLNVTFADVGKTYEVEGGNCSVNTLDAGKWCEDYVEYECVTLSEGEEPDDLDCWCYGVDNVRVTYGRCKSGGS
RRSRRSAVITPHVDKGLTTRQEKWLPTKIGEQQLQKVEKWIMRNPLYALGAVALAYFVGTSNVQRVVIAILLLGIGPAYSTHCLGIPKRDFIRGLDGNTW
VSVVLEQGSCVTLIADNKPSVDIWLSSIVVDTPTLVRKVCYASSVTGSKATGACPTMGDAHMSEEGNEEWECKRSYSDRGWGNGCGLFGKGSIVACAKFS
CTHEMEVYQIDATKIEYTISAQVHSGAKKDDWENHTKLVTFVPTTGTSTVAFTGYGNFGLECHVQMMVDLSNSYLVKVGTDAWLVNKQWVHDITLPWQSG
TGGHWRDKHFMVDFEEPHAVTMKALVLGSQEGALRTALSGAMVVELNSNRYSLKGGHVTCKAYMNNLILKGSTYSMCKRGMSFAKQPVETDHGTAVMQIK
VTTGAPCRIPVIAADSMAGTENRGSVITTNPIAASNNDEVLVEISPPFGESYIIVGNGDDKLTYHWQRSGSTIGNLFTETMKGAQRMIITGEHSWDFGST
GGFFSSIAKAVHTVFGAAFHAIFGGLSWITKILIGGLLIWLGLNSRSSSMSMGFICIGALLLVLATGVGAEVGCSLSWKQREMKCGDGVFVFKDSDDWFS
KYQYIPEDPKTMATLIHQAHQDGLCGLSSVSDLEHRMWYSRVDEINAILDENEVDLTVVVQESDAVYLRGSHAFPRPKSELKYGWKTWGKNIIFNPSRKN
GTFIIDGKSKAECPFNKRVWNSIRVEEFGTGVYQTRVFMRPEFDYTKLCDTGTLGAAVKGSVSAHGDPMFWMESEEINGTWMITTLEALNYRECEWPSSH
TLDGAKVVESDMFMPRSLAGPISKHNHIPGYKVQTSGPWHNVPLEIKREECPGTTVVVDEKCDDRAKSVRSTTDSGKIIPEWCCRSCTMPPVSFWGPDGC
WYSMEVRPKHTNEAHLVKSWVVASKGDVDPFSLGLLMLFLCSDMFLMKRFSMRAILVGSLVMLGAMTLGSLSYLDLLRYAITVGMYMAEINSGGDVTHLA
LLAVFRVRAGFVSMLALKRLWSPREGFVATCGIVMVQLALGDILSTDIMEWLNAAGMAVLIIKSIVEPKRCNAVLPLLCLLTPLTVAEIQRAVMFVCSIV
IFVTVWQTDSVSTRKTIPLVALTVCSFFKWTSPFLGIVCYLAFTRLPQRSWPLGETMAAVGLVGVLAGMGLKDMNGMLGPVAVGGVLLIVMSLSGKVDGL
VIKKVADVTWDEDAEISGASHRYDVEQTDTGEFKLRNEEPAPWIQVAVLTIAILSAATHPACLAVVTIGWFAWQKTTTRSGVLWDIPTVVPPEEVSYLED
GVYTINQNSFLGLAQKGVGVVKDGVFHTMWHVTRGAFLLHAGKRMTPSWANVKEDLISYGGGWKLDAKWDGSEEVQLIAVSPGKVPVNVQTTPSVFQLKN
GKEIGAVNLDYPSGTSGSPILNKNGDVIGLYGNGILIGNNTYVSAIAQSDSVEEGGTEQLQDIPTMLKKGMLTVLDFHPGAGKTRIYLPQILKECEKLKL
KTLVLAPTRVVLSEMREAMPKMSIKYHTQAFSNTSTGKEIIDAMCHATLTHRMLEPTRVTNWEVVIMDEAHFMDPASIAARGWAAHRSRARECATIFMSA
TPPGTSNEFPESNGMIEDVKKDVPSEPWTKGHEWILEDRRPTAWFLPSIRIANSIANCLRKADRTVVVLNRKTFEKEYPTIKSKKPDFILATDIAEMGAN
LKVERVIDCRTAYKPILVDDATKVMVKGPLRISASSAAQRRGRIGRDPNRDTDTYIYGDSTTEDNGHYVCWTEGSMLLDNMEIRNGMIAPLYGVEGTKTT
TSPGETRLREDQRKVFRELVKRLDMPVWFSWQVAKAGLKVQDRSWCFDGEDDNTLLNDNGEPILARSPGGAKKPLKPRWVDTRVCSDNASLIDFIKFAEG
RRSASGILLGLQGFPEFLSGKMREAIDTVTVLYTSDTGSRAYKHALAMMPEATTIFLLVMLAIICTSGVIMFFLAPKGLSRMSMAMMTMLVSAYLMSLGG
MNPVQISCVMLVFFIFMVVLIPEPGTQRSTYDNQIIYLLVGVLSLILLVAANEMELLEKTKRDIFGAVVVEEAKRWTFPEFDLRPGAAWTVYVGLVTPGN
PMLHHWIKIDYGNISLSGITQNAQVLGLMDRGIPFIKMNMSVVILLLSAWNGITLLPLFAGMGAAALHWGFILPGLRAQAAKAAQKRVYHGVAKNPVVDG
NPTVDIDDAPGMPAMYEKKLALVILLALSILNLVLTRTPFATAEMVVLGSAAVGPLIEGDTNAYWNGPIAVAFSGLMRGNYYATIGLAYNGWLAKQTRRG
KAAGVTLGEVWKRQLNMLGKQEFERYKVPDITEVDRTAARRYLKEGRTDVGISVSRGAAKIRWLHERGYLRITGRVLDLGCGRGGWSYYAAAQKEVMSVK
GYTLGIEGHEKPIHMQTLGWNIVKFKDKSNVFTMPTEPSDTLLCDIGESSSNPLVERDRTMKVLENFERWKHVNTENFCVKVLAPYHPDVIEKLERLQLR
FGGGIVRVPFSRNSTHEMYYISGARNNITHMVNTTSRSLLRRMTRPSGKAIIEGDVFLPTGTRSVASEAGTIDHEALKLRVDQIKAEYSKTWTHDSNHPY
RTWHYLGSYLCKATGSSSSMINGIVKMLSMPWDKFESVTLLAMTDTTPFGQQRVFKEKVDTKAPPPPPGTRAIMRVVNAWLFQHLARKKKPRICTREEFV
AKVRSHAALGAYLEEQDKWKSASEAVQDPQFWKLVDDERKLHLQGQCRTCVYNMMGKREKKPSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWVSR
ENSGGGVEGTGLQYLGYILKELGGKTGGNMYADDTAGWDTRITEEDLEDEQEILKYMDEKHKKLAWAVTELAYKNKVVKVMRPGPGGLTFMDIISRRDQR
GSGQVVTYALNTVTNLKVQLIRMAEAEHVITNFDVDTVSQKTLQDLRCWLDRFGADRLSRMAVSGDDCVVKPIDDQFADALTHLNSMSKIRKDIDDWKPS
QGWASWEDVPFCSHHFHELILKDGRSIIAPCRDQDELIGRARVSPGNGWMIRETACLSKAYAQMWLLMYFHRRDLRVMANAINSTVPVDWVPTGRTTWSI
HGKGEWMTTEDMLQVWNRVWIEDNPHQTDKTPITEWRDIPYLPKSIDKTCNSLVGTTQRASWARDIKHTVHRIRGLVGNEKYTDYLATMDRFRELDESGP
GEVLW
3405
Not Available
Not Available
28-07-2009
Inferred from homology
| Amino Acid | Count | % Frequency | Amino Acid | Count | % Frequency |
|---|---|---|---|---|---|
| Alanine (A) | Leucine (L) | ||||
| Arginine (R) | Lysine (K) | ||||
| Asparagine (N) | Methionine (M) | ||||
| Aspartic Acid (D) | Phenylalanine (F) | ||||
| Cysteine (C) | Proline (P) | ||||
| Glutamine (Q) | Serine (S) | ||||
| Glutamic Acid (E) | Threonine (T) | ||||
| Glycine (G) | Tryptophan (W) | ||||
| Histidine (H) | Tyrosine (Y) | ||||
| Isoleucine (I) | Valine (V) |
| % Number of Residues in Helices | % Number of Residues in Strands | % Number of Residues in Coils |
|---|---|---|
♦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.
♦ Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.
♦ 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.
♦ 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.
♦ 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.
♦ 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.
♦ 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).
♦ Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.
♦ Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).
♦ 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).
♦ Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.
♦ Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.
♦ 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.
♦ 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.
♦ Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.
♦ 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.
♦ 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.
♦ 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.
♦ 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.
♦ 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).
♦ Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.
♦ Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).
♦ 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).
♦ Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.
♦ Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.
♦ 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.
♦ 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.
3.4.21.91 , 3.6.1.15 , 3.6.4.13 , 2.1.1.56 , 2.1.1.57 , 2.7.7.48
GO:0003724 ; GO:0003725 ; GO:0003968 ; GO:0004252 ; GO:0004482 ;
GO:0004483 ; GO:0005198 ; GO:0005524 ; GO:0005525 ; GO:0005576 ;
GO:0008026 ; GO:0016021 ; GO:0019028 ; GO:0019031 ; GO:0019062 ;
GO:0039502 ; GO:0039520 ; GO:0039563 ; GO:0039564 ; GO:0039654 ;
GO:0039694 ; GO:0042025 ; GO:0044167 ; GO:0044220 ; GO:0046872 ;
GO:0046983 ; GO:0055036
GO:0004483 ; GO:0005198 ; GO:0005524 ; GO:0005525 ; GO:0005576 ;
GO:0008026 ; GO:0016021 ; GO:0019028 ; GO:0019031 ; GO:0019062 ;
GO:0039502 ; GO:0039520 ; GO:0039563 ; GO:0039564 ; GO:0039654 ;
GO:0039694 ; GO:0042025 ; GO:0044167 ; GO:0044220 ; GO:0046872 ;
GO:0046983 ; GO:0055036
♦ Capsid protein C: Virion . Host nucleus . Host cytoplasm, host perinuclear region . Host cytoplasm .
♦ Peptide pr: Secreted .
♦ Small envelope protein M: Virion membrane
♦ Multi-pass membrane protein . Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein . Note=ER membrane retention is mediated by the transmembrane domains. .
♦ Envelope protein E: Virion membrane
♦ Multi-pass membrane protein . Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein . Note=ER membrane retention is mediated by the transmembrane domains. .
♦ Non-structural protein 1: Secreted . Host endoplasmic reticulum membrane
♦ Peripheral membrane protein
♦ Lumenal side . Note=Located in RE-derived vesicles hosting the replication complex. Q6P4.
♦ Non-structural protein 2A: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein .
♦ Serine protease subunit NS2B: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein .
♦ Serine protease NS3: Host endoplasmic reticulum membrane PROSITE-ProRule:PRU00860
♦ Peripheral membrane protein PROSITE-ProRule:PRU00860
♦ Cytoplasmic side PROSITE-ProRule:PRU00860. Note=Remains non-covalently associated to serine protease subunit NS2B. PROSITE-ProRule:PRU00860.
♦ Non-structural protein 4A: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein . Note=Located in RE-associated vesicles hosting the replication complex. .
♦ Non-structural protein 4B: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein . Note=Located in RE-derived vesicles hosting the replication complex. Q6P4.
♦ RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side. Host nucleus . Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. .
♦ Peptide pr: Secreted .
♦ Small envelope protein M: Virion membrane
♦ Multi-pass membrane protein . Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein . Note=ER membrane retention is mediated by the transmembrane domains. .
♦ Envelope protein E: Virion membrane
♦ Multi-pass membrane protein . Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein . Note=ER membrane retention is mediated by the transmembrane domains. .
♦ Non-structural protein 1: Secreted . Host endoplasmic reticulum membrane
♦ Peripheral membrane protein
♦ Lumenal side . Note=Located in RE-derived vesicles hosting the replication complex. Q6P4.
♦ Non-structural protein 2A: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein .
♦ Serine protease subunit NS2B: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein .
♦ Serine protease NS3: Host endoplasmic reticulum membrane PROSITE-ProRule:PRU00860
♦ Peripheral membrane protein PROSITE-ProRule:PRU00860
♦ Cytoplasmic side PROSITE-ProRule:PRU00860. Note=Remains non-covalently associated to serine protease subunit NS2B. PROSITE-ProRule:PRU00860.
♦ Non-structural protein 4A: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein . Note=Located in RE-associated vesicles hosting the replication complex. .
♦ Non-structural protein 4B: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein . Note=Located in RE-derived vesicles hosting the replication complex. Q6P4.
♦ RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side. Host nucleus . Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. .
♦DOMAIN 1480 1659 Peptidase S7.
♦ DOMAIN 1664 1820 Helicase ATP-binding.
♦ DOMAIN 1831 1992 Helicase C-terminal.
♦ DOMAIN 2500 2764 mRNA cap 0-1 NS5-type MT.
♦ DOMAIN 3028 3180 RdRp catalytic.
♦ DOMAIN 1664 1820 Helicase ATP-binding.
♦ DOMAIN 1831 1992 Helicase C-terminal.
♦ DOMAIN 2500 2764 mRNA cap 0-1 NS5-type MT.
♦ DOMAIN 3028 3180 RdRp catalytic.
MOTIF 1768 1771 DEAH box. ; MOTIF 2871 2904 Nuclear localization signal.
Predicted/Modelled
Not Available
♦ACT_SITE 1531 1531 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1555 1555 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1616 1616 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 2560 2560 For 2'-O-MTase activity.
♦ ACT_SITE 2645 2645 For 2'-O-MTase activity.
♦ ACT_SITE 2681 2681 For 2'-O-MTase activity.
♦ ACT_SITE 2717 2717 For 2'-O-MTase activity.
♦ for serine protease NS3 activity.
♦ ACT_SITE 1555 1555 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1616 1616 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 2560 2560 For 2'-O-MTase activity.
♦ ACT_SITE 2645 2645 For 2'-O-MTase activity.
♦ ACT_SITE 2681 2681 For 2'-O-MTase activity.
♦ ACT_SITE 2717 2717 For 2'-O-MTase activity.
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.
Not Available
- Million Molecules
Best 20 Hit molecules
Not Available