Reviewed
Homo Sapiens (Human) [TaxID: 9606]; Ixodida (ticks) [TaxID: 6935]
Not Available
♦Genome polyprotein [Cleaved into: Peptide 2k
♦ 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)
♦ 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) (NS5)]
♦ 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)
♦ 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) (NS5)]
Langat Virus (strain TP21)
Viruses> SsRNA Viruses> SsRNA Positive-strand Viruses> No DNA Stage> Flaviviridae> Flavivirus (arboviruses Group B)> Tick-borne Encephalitis Virus Group> Langat Virus> Langat Virus (strain TP21)
Various pathway(s) in which protein is involved
Not Available
Not Available
MAGKAVLKGKGGGPPRRASKVAPKKTRQLRVQMPNGLVLMRMLGVLWHALTGTARSPVLKAFWKVVPLKQATLALRKIKRTVSTLMVGLHRRGSRRTTID
WMTPLLITVMLGMCLTATVRRERDGSMVIRAEGRDAATQVRVENGTCVILATDMGSWCDDSLAYECVTIDQGEEPVDVDCFCRGVEKVTLEYGRCGRREG
SRSRRSVLIPSHAQRDLTGRGHQWLEGEAVKAHLTRVEGWVWKNKLFTLSLVMVAWLMVDGLLPRILIVVVALALVPAYASRCTHLENRDFVTGVQGTTR
LTLVLELGGCVTVTADGKPSLDVWLDSIYQESPAQTREYCLHAKLTGTKVAARCPTMGPATLPEEHQSGTVCKRDQSDRGWGNHCGLFGKGSIVTCVKFT
CEDKKKATGHVYDVNKITYTIKVEPHTGEFVAANETHSGRKSASFTVSSEKTILTLGDYGDVSLLCRVASGVDLAQTVVLALDKTHEHLPTAWQVHRDWF
NDLALPWKHDGAEAWNEAGRLVEFGTPHAVKMDVFNLGDQTGVLLKSLAGVPVASIEGTKYHLKSGHVTCEVGLEKLKMKGLTYTVCDKTKFTWKRAPTD
SGHDTVVMEVGFSGTRPCRIPVRAVAHGVPEVNVAMLITPNPTMENNGGGFIEMQLPPGDNIIYVGDLNHQWFQKGSSIGRVLQKTRKGIERLTVLGEHA
WDFGSVGGVMTSIGRAMHTVLGGAFNTLLGGVGFLPKILLGVAMAWLGLNMRNPTLSMGFLLSGGLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWRE
VSEWYDNYVFHPETPAVLASAVQRAYEEEICGIVPQNRLEMAMWRSSLVELNLALAEGEANLTVVVDKADPSDYRGGVPGLLNKGKDIKVSWRSWGRSML
WSVPEAPRRFMIGVEGGRECPFARRKTGVMTVAEFGIGLRTKVFMDLRQELTTECDTGVMGAAVKNGMAVHTDQSLWMKSIKNDTTVTIVELIVTDLRNC
TWPASHTIDNAGVVNSKLFLPASLAGPRSTYNVIPGYAEQVRGPWAHTPVRIKREECPGTRVTIDKACDKRGASVRSTTESGKVIPEWCCRTCELPPVTY
RTGTDCWYAMEIRPVHTQGGLVRSMVVADNGALLSEGGVPGVVALFVVLELVIRRRPATGGTVIWGGIAILALLVTGLVSVESLFRYLVAVGLVFQLELG
PEAVAMVLLQAVFEMRTCLLSGFVLRRSITTREIVTVYFLLLVLEMGIPVKGLEHLWRWTDALAMGAIIFRACTAEGKTGIGLLLAAFMTQSDMNIIHDG
LTAFLCVATTMAIWRYIRGQGERKGLTWIVPLAGILGGEGSGVRLLAFWELAASRGRRSFNEPMTVIGVMLTLASGMMRHTSQEAVCAMALAAFLLLMLT
LGTRKMQLLAEWSGNIEWNPELTSEGGEVSLRVRQDALGNLHLTELEKEERMMAFWLVVGLIASAFHWSGILIVMGLWTISEMLGSPRRTDLVFSGCSEG
RSDSRPLDVKNGVYRIYTPGLLWGQRQIGVGYGAKGVLHTMWHVTRGAALLVDGVAVGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRAHETH
QCQPGELILENGRKMGAIPIDLAKGTSGSPIMNSQGEVVGLYGNGLKTNDTYVSSIAQGEVEKSRPNLPQSVVGTGWTAKGQITVLDMHPGSGKTHRVLP
ELIRQCVERRLRTLVLAPTRVVLREMERALSGKNVRFHSPAVTEQHANGAIVDVMCHATYVNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAK
ENRCAFVLMTATPPGKSEPFPESNGAIASEERQIPDGEWRDGFDWITEYEGRTAWFVPSIARGGAIARALRQRGKSVICLNSKTFDKEYSRVKDEKPDFV
VTTDISEMGANLDVTRVIDGRTNIKPEEVDGRIELTGTRRVTTASAAQRRGRVGRQGGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTARGPVATFY
GPEQERMTETAGHYRLPEEKRKHFRHLLAQCDFTPWLAWHVAANVASVTDRSWTWEGPEENAVDENNGELVTFRSPNGAERTLRPVWRDARMFREGRDIR
EFVSYASGRRSVGDVLMGMSGVPALLRQRCTSAMDVFYTLMHEEPGSRAMRIGERDAPEAFLTAVEMLVLGLATLGVVWCFVVRTSVSRMVLGTLVLATS
LIFLWAGGVGYGNMAGVALVFYTLLTVLQPETGKQRSSDDNKLAYFLLTLCGLAGMVAANEMGLLEKTKADLAALFARDQGETVRWGEWTNLDIQPARSW
GTYVLVVSLFTPYMLHQLQTRIQQLVNSAVASGAQAMRDLGGGTPFFGVAGHVLALGVASLVGATPTSLILGVGLAAFHLAIVVSGLEAELTQRAHKVFF
SAMVRNPMVDGDVINPFGDGEAKPALYERKLSLILALVLCLASVVMNRTFVAVTEAGAVGVAAAMQLLRPEMDVLWTMPVACGMSGVVRGSLWGLLPLGH
RLWLRTTGTRRGGSEGDTLGDMWKARLNSCTKEEFFAYRRAGVMETDREKARELLKRGETNMGLAVSRGTSKLAWMEERGYVTLKGEVVDLGCGRGGWSY
YAASRPAVMSVRAYTIGGKGHESPRMVTSLGWNLIKFRAGMDVFSMEPHRADAILCDIGESNPDAVVEGERSRRVILLMEQWKNRNPTATCVFKVLAPYR
PEVIEALHRFQLQWGGGLVRTPFSRNSTHEMYFSTAITGNIVNSVNIQSRKLLARFGDQRGPTRVPEIDLGVGTRSVVLAEDKVKEKDVMERIQALKDQY
CDTWHEDHEHPYRTWQYWGSYKTAATGSSASLLNGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKDKVDTKAQEPQPGTKIIMRAVNDWLLERLVKK
SRPRMCSREEFIAKVRSNAALAAWSDEQNKWKSAREAVEDPEFWSLVEAERERHLQGRCAHCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEA
LGFLNEDHWASRASSGAGVEGISLNYLGWHLKKLASLSGGLFYADDTAGWDTRITNADLDDEEQILRYMDGDHKKLAATVLRKAYHAKVVRVARPSREGG
CVMDIITRRDQRGSGQVVTYALNTITNIKVQLVRMMEGEGVIEVADSHNPRLLRVEKCVEEHGEERLSRMLVSGDDCVVRPVDDRFSKALYFLNDMAKTR
KDTGEWEPSTGFASWEEVPFCSHHFHELVMKDGRALVVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFHRRDLRTLGFAICSAVPVDWV
PTGRTTWSIHASGAWMTTEDMLEVWNRVWIYDNPFMEDKTRVDEWRDTPYLPKSQDILCSSLVGRGERAEWAKNIWGAVEKVRRMIGPEHYRDYLSSMDR
HDLHWELKLESSIF
WMTPLLITVMLGMCLTATVRRERDGSMVIRAEGRDAATQVRVENGTCVILATDMGSWCDDSLAYECVTIDQGEEPVDVDCFCRGVEKVTLEYGRCGRREG
SRSRRSVLIPSHAQRDLTGRGHQWLEGEAVKAHLTRVEGWVWKNKLFTLSLVMVAWLMVDGLLPRILIVVVALALVPAYASRCTHLENRDFVTGVQGTTR
LTLVLELGGCVTVTADGKPSLDVWLDSIYQESPAQTREYCLHAKLTGTKVAARCPTMGPATLPEEHQSGTVCKRDQSDRGWGNHCGLFGKGSIVTCVKFT
CEDKKKATGHVYDVNKITYTIKVEPHTGEFVAANETHSGRKSASFTVSSEKTILTLGDYGDVSLLCRVASGVDLAQTVVLALDKTHEHLPTAWQVHRDWF
NDLALPWKHDGAEAWNEAGRLVEFGTPHAVKMDVFNLGDQTGVLLKSLAGVPVASIEGTKYHLKSGHVTCEVGLEKLKMKGLTYTVCDKTKFTWKRAPTD
SGHDTVVMEVGFSGTRPCRIPVRAVAHGVPEVNVAMLITPNPTMENNGGGFIEMQLPPGDNIIYVGDLNHQWFQKGSSIGRVLQKTRKGIERLTVLGEHA
WDFGSVGGVMTSIGRAMHTVLGGAFNTLLGGVGFLPKILLGVAMAWLGLNMRNPTLSMGFLLSGGLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWRE
VSEWYDNYVFHPETPAVLASAVQRAYEEEICGIVPQNRLEMAMWRSSLVELNLALAEGEANLTVVVDKADPSDYRGGVPGLLNKGKDIKVSWRSWGRSML
WSVPEAPRRFMIGVEGGRECPFARRKTGVMTVAEFGIGLRTKVFMDLRQELTTECDTGVMGAAVKNGMAVHTDQSLWMKSIKNDTTVTIVELIVTDLRNC
TWPASHTIDNAGVVNSKLFLPASLAGPRSTYNVIPGYAEQVRGPWAHTPVRIKREECPGTRVTIDKACDKRGASVRSTTESGKVIPEWCCRTCELPPVTY
RTGTDCWYAMEIRPVHTQGGLVRSMVVADNGALLSEGGVPGVVALFVVLELVIRRRPATGGTVIWGGIAILALLVTGLVSVESLFRYLVAVGLVFQLELG
PEAVAMVLLQAVFEMRTCLLSGFVLRRSITTREIVTVYFLLLVLEMGIPVKGLEHLWRWTDALAMGAIIFRACTAEGKTGIGLLLAAFMTQSDMNIIHDG
LTAFLCVATTMAIWRYIRGQGERKGLTWIVPLAGILGGEGSGVRLLAFWELAASRGRRSFNEPMTVIGVMLTLASGMMRHTSQEAVCAMALAAFLLLMLT
LGTRKMQLLAEWSGNIEWNPELTSEGGEVSLRVRQDALGNLHLTELEKEERMMAFWLVVGLIASAFHWSGILIVMGLWTISEMLGSPRRTDLVFSGCSEG
RSDSRPLDVKNGVYRIYTPGLLWGQRQIGVGYGAKGVLHTMWHVTRGAALLVDGVAVGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRAHETH
QCQPGELILENGRKMGAIPIDLAKGTSGSPIMNSQGEVVGLYGNGLKTNDTYVSSIAQGEVEKSRPNLPQSVVGTGWTAKGQITVLDMHPGSGKTHRVLP
ELIRQCVERRLRTLVLAPTRVVLREMERALSGKNVRFHSPAVTEQHANGAIVDVMCHATYVNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAK
ENRCAFVLMTATPPGKSEPFPESNGAIASEERQIPDGEWRDGFDWITEYEGRTAWFVPSIARGGAIARALRQRGKSVICLNSKTFDKEYSRVKDEKPDFV
VTTDISEMGANLDVTRVIDGRTNIKPEEVDGRIELTGTRRVTTASAAQRRGRVGRQGGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTARGPVATFY
GPEQERMTETAGHYRLPEEKRKHFRHLLAQCDFTPWLAWHVAANVASVTDRSWTWEGPEENAVDENNGELVTFRSPNGAERTLRPVWRDARMFREGRDIR
EFVSYASGRRSVGDVLMGMSGVPALLRQRCTSAMDVFYTLMHEEPGSRAMRIGERDAPEAFLTAVEMLVLGLATLGVVWCFVVRTSVSRMVLGTLVLATS
LIFLWAGGVGYGNMAGVALVFYTLLTVLQPETGKQRSSDDNKLAYFLLTLCGLAGMVAANEMGLLEKTKADLAALFARDQGETVRWGEWTNLDIQPARSW
GTYVLVVSLFTPYMLHQLQTRIQQLVNSAVASGAQAMRDLGGGTPFFGVAGHVLALGVASLVGATPTSLILGVGLAAFHLAIVVSGLEAELTQRAHKVFF
SAMVRNPMVDGDVINPFGDGEAKPALYERKLSLILALVLCLASVVMNRTFVAVTEAGAVGVAAAMQLLRPEMDVLWTMPVACGMSGVVRGSLWGLLPLGH
RLWLRTTGTRRGGSEGDTLGDMWKARLNSCTKEEFFAYRRAGVMETDREKARELLKRGETNMGLAVSRGTSKLAWMEERGYVTLKGEVVDLGCGRGGWSY
YAASRPAVMSVRAYTIGGKGHESPRMVTSLGWNLIKFRAGMDVFSMEPHRADAILCDIGESNPDAVVEGERSRRVILLMEQWKNRNPTATCVFKVLAPYR
PEVIEALHRFQLQWGGGLVRTPFSRNSTHEMYFSTAITGNIVNSVNIQSRKLLARFGDQRGPTRVPEIDLGVGTRSVVLAEDKVKEKDVMERIQALKDQY
CDTWHEDHEHPYRTWQYWGSYKTAATGSSASLLNGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKDKVDTKAQEPQPGTKIIMRAVNDWLLERLVKK
SRPRMCSREEFIAKVRSNAALAAWSDEQNKWKSAREAVEDPEFWSLVEAERERHLQGRCAHCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEA
LGFLNEDHWASRASSGAGVEGISLNYLGWHLKKLASLSGGLFYADDTAGWDTRITNADLDDEEQILRYMDGDHKKLAATVLRKAYHAKVVRVARPSREGG
CVMDIITRRDQRGSGQVVTYALNTITNIKVQLVRMMEGEGVIEVADSHNPRLLRVEKCVEEHGEERLSRMLVSGDDCVVRPVDDRFSKALYFLNDMAKTR
KDTGEWEPSTGFASWEEVPFCSHHFHELVMKDGRALVVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFHRRDLRTLGFAICSAVPVDWV
PTGRTTWSIHASGAWMTTEDMLEVWNRVWIYDNPFMEDKTRVDEWRDTPYLPKSQDILCSSLVGRGERAEWAKNIWGAVEKVRRMIGPEHYRDYLSSMDR
HDLHWELKLESSIF
3414
Not Available
Not Available
01-02-1994
Evidence at protein level
| 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 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 in host cytoplasm after hemifusion induced by 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. Presumably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is ineficient, 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 extodomain. 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 ineficient, 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.
♦ Non-structural protein 2B: Required cofactor for the serine protease function of NS3 (By similarity). 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.
♦ 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. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.
♦ RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:16188985). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:16188985).
♦ 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. Presumably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is ineficient, 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 extodomain. 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 ineficient, 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.
♦ Non-structural protein 2B: Required cofactor for the serine protease function of NS3 (By similarity). 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.
♦ 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. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.
♦ RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:16188985). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:16188985).
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:0005576 ; GO:0006351 ;
GO:0006355 ; GO:0008026 ; GO:0016021 ; GO:0019028 ; GO:0019031 ;
GO:0019062 ; GO:0039502 ; GO:0039520 ; GO:0039563 ; GO:0039564 ;
GO:0039574 ; GO:0039576 ; GO:0039651 ; GO:0039654 ; GO:0039694 ;
GO:0042025 ; GO:0044167 ; GO:0044220 ; GO:0046872 ; GO:0046983 ;
GO:0055036 ; GO:0075512
GO:0004483 ; GO:0005198 ; GO:0005524 ; GO:0005576 ; GO:0006351 ;
GO:0006355 ; GO:0008026 ; GO:0016021 ; GO:0019028 ; GO:0019031 ;
GO:0019062 ; GO:0039502 ; GO:0039520 ; GO:0039563 ; GO:0039564 ;
GO:0039574 ; GO:0039576 ; GO:0039651 ; GO:0039654 ; GO:0039694 ;
GO:0042025 ; GO:0044167 ; GO:0044220 ; GO:0046872 ; GO:0046983 ;
GO:0055036 ; GO:0075512
♦ 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 1490 1669 Peptidase S7.
♦ DOMAIN 1675 1831 Helicase ATP-binding.
♦ DOMAIN 1841 2000 Helicase C-terminal.
♦ DOMAIN 2512 2776 mRNA cap 0-1 NS5-type MT.
♦ DOMAIN 3040 3189 RdRp catalytic.
♦ DOMAIN 1675 1831 Helicase ATP-binding.
♦ DOMAIN 1841 2000 Helicase C-terminal.
♦ DOMAIN 2512 2776 mRNA cap 0-1 NS5-type MT.
♦ DOMAIN 3040 3189 RdRp catalytic.
MOTIF 1779 1782 DEAH box.
NMR spectroscopy (2)
♦ACT_SITE 1543 1543 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1567 1567 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1627 1627 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 2572 2572 For 2'-O-MTase activity.
♦ ACT_SITE 2657 2657 For 2'-O-MTase activity.
♦ ACT_SITE 2694 2694 For 2'-O-MTase activity.
♦ ACT_SITE 2730 2730 For 2'-O-MTase activity.
♦ for serine protease NS3 activity.
♦ ACT_SITE 1567 1567 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1627 1627 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 2572 2572 For 2'-O-MTase activity.
♦ ACT_SITE 2657 2657 For 2'-O-MTase activity.
♦ ACT_SITE 2694 2694 For 2'-O-MTase activity.
♦ ACT_SITE 2730 2730 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