| IED ID | IndEnz0002012784 |
| Enzyme Type ID | protease012784 |
| Protein Name |
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/Helicase 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 |
| Gene Name | GP1 MZ11_60484gpGP1 MZ11_60553gpGP1 |
| Organism | West Nile virus (strain NY-99) (WNV) (West Nile virus (strain NY-1999)) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Kitrinoviricota Flasuviricetes Amarillovirales Flaviviridae Flavivirus (arboviruses group B) West Nile virus (WNV) West Nile virus (strain NY-99) (WNV) (West Nile virus (strain NY-1999)) |
| Enzyme Sequence | MSKKPGGPGKSRAVNMLKRGMPRVLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAVMIGLIASVGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRAMDVGYMCDDTITYECPVLSAGNDPEDIDCWCTKSAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFVVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSDLSTKAACPTMGEAHNDKRADPAFVCRQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKAIGRTILKENIKYEVAIFVHGPTTVESHGNYSTQVGATQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTNAYYVMTVGTKTFLVHREWFMDLNLPWSSAGSTVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFLGTPADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLTPVGRLVTVNPFVSVATANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWMDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSVVVEKQEGMYKSAPKRLTATTEKLEIGWKAWGKSILFAPELANNTFVVDGPETKECPTQNRAWNSLEVEDFGFGLTSTRMFLKVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRLNDTWKLERAVLGEVKSCTWPETHTLWGDGILESDLIIPVTLAGPRSNHNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDSGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAVFFQMAYHDARQILLWEIPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGLFNPMILAAGLIACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWESDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMVCLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKKGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPIPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVPREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTKVELGEAAAIFMTATPPGTSDPFPESNSPISDLQTEIPDRAWNSGYEWITEYTGKTVWFVPSVKMGNEIALCLQRAGKKVVQLNRKSYETEYPKCKNDDWDFVITTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRIGRNPSQVGDEYCYGGHTNEDDSNFAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKAFKDFASGKRSQIGLIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGAVLGVATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVMTLVSAVAANEMGWLDKTKSDISSLFGQRIEVKENFSMGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYINTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTAATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQIMLILVSLAAVVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLIKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFTRYRKEAIIEVDRSAAKHARKEGNVTGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTIRVLEMVEDWLHRGPREFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKRTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYDVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGKIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLFENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVVPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRAIIGDEKYVDYMSSLKRYEDTTLVEDTVL |
| Enzyme Length | 3433 |
| Uniprot Accession Number | Q9Q6P4 |
| Absorption | |
| Active Site | ACT_SITE 1556; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00860; ACT_SITE 1580; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00860; ACT_SITE 1640; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00860; ACT_SITE 2589; /note=For 2'-O-MTase activity; /evidence=ECO:0000269|PubMed:17267492; ACT_SITE 2674; /note=For 2'-O-MTase activity; /evidence=ECO:0000269|PubMed:17267492; ACT_SITE 2710; /note=For 2'-O-MTase activity; /evidence=ECO:0000269|PubMed:17267492; ACT_SITE 2746; /note=For 2'-O-MTase activity; /evidence=ECO:0000269|PubMed:17267492 |
| Activity Regulation | |
| Binding Site | BINDING 2584; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:17267492"; BINDING 2614; /note="S-adenosyl-L-methionine; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"; BINDING 2615; /note="S-adenosyl-L-methionine; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"; BINDING 2632; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"; BINDING 2633; /note="S-adenosyl-L-methionine; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"; BINDING 2639; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000269|PubMed:17267492"; BINDING 2659; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"; BINDING 2660; /note="S-adenosyl-L-methionine; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"; BINDING 2674; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000269|PubMed:17267492"; BINDING 2675; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"; BINDING 2748; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:19474250}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660}; |
| DNA Binding | |
| EC Number | 3.4.21.91; 3.6.1.15; 3.6.4.13; 2.1.1.56; 2.1.1.57; 2.7.7.48 |
| Enzyme Function | 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. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {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 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:0000269|PubMed:17132743, ECO:0000269|PubMed:24245822, ECO:0000269|PubMed:24465392, ECO:0000269|PubMed:24889229, ECO:0000269|PubMed:24928049}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}.; 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/Helicase 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 (By similarity). NS3 supports the separation of RNA daughter and template strands during viral replication. The helicase part is involved in the inhibition of phosphorylation of host STAT1, and thereby inhibition of host type-I IFN signaling (PubMed:29099073). In addition, NS3 assists the initiation of replication by unwinding the RNA secondary structure in the 3' non-translated region (NTR). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:29099073}.; FUNCTION: [Non-structural protein 4A]: Facilitates host membrane remodelling necessary for viral replication by interacting with host RTN3. Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000269|PubMed:19474250, ECO:0000269|PubMed:29117567}.; 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 (PubMed:24465392). 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 (PubMed:15956546). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15956546). {ECO:0000269|PubMed:15956546, ECO:0000269|PubMed:24465392}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:19850911, PubMed:20685660). 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 (PubMed:20106931). Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:15650160). {ECO:0000269|PubMed:15650160, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20106931, ECO:0000269|PubMed:20685660}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 1699..1706; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00541 |
| Features | Active site (7); Beta strand (50); Binding site (11); Chain (13); Disulfide bond (14); Domain (5); Glycosylation (5); Helix (26); Intramembrane (3); Metal binding (7); Modified residue (1); Motif (3); Mutagenesis (23); Nucleotide binding (1); Peptide (1); Propeptide (1); Region (8); Site (29); Topological domain (22); Transmembrane (18); Turn (4) |
| Keywords | 3D-structure;ATP-binding;Activation of host autophagy by virus;Capsid protein;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 STAT1 by virus;Inhibition of host STAT2 by virus;Inhibition of host innate immune response by virus;Inhibition of host interferon signaling pathway by virus;Membrane;Metal-binding;Methyltransferase;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 RNA replication;Viral attachment to host cell;Viral immunoevasion;Viral penetration into host cytoplasm;Virion;Virus entry into host cell;Zinc;mRNA capping;mRNA processing |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; 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:0000269|PubMed:24928049}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:24465392}; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000269|PubMed:24465392}.; 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/Helicase 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:0000269|PubMed:24465392}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000269|PubMed:24465392, ECO:0000269|PubMed:29117567}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:24465392}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000269|PubMed:24465392}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Host cytoplasm {ECO:0000250|UniProtKB:P14335}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles (By similarity). Shuttles between the cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000250|UniProtKB:P17763}. |
| Modified Residue | MOD_RES 2584; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P03314 |
| Post Translational Modification | 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 (PubMed:24505133). The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:24505133}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (2); X-ray crystallography (8) |
| Cross Reference PDB | 2OY0; 3I50; 3IYW; 3J0B; 3LKZ; 4O6C; 4O6D; 4OIE; 4OII; 6UTE; |
| Mapped Pubmed ID | 32321830; |
| Motif | MOTIF 1790..1793; /note=DEAH box; /evidence=ECO:0000255|PROSITE-ProRule:PRU00541; MOTIF 2917..2919; /note=Nuclear localization signal; /evidence=ECO:0000250|UniProtKB:P14335; MOTIF 3431..3433; /note=PDZ-binding; /evidence=ECO:0000250|UniProtKB:P06935 |
| Gene Encoded By | |
| Mass | 381,176 |
| Kinetics | |
| Metal Binding | METAL 2968; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P14335; METAL 2972; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P14335; METAL 2977; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P14335; METAL 2980; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P14335; METAL 3245; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P14335; METAL 3261; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P14335; METAL 3380; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P14335 |
| Rhea ID | RHEA:21248; RHEA:23680; RHEA:13065; RHEA:67008; RHEA:67020 |
| Cross Reference Brenda |