Q9Q6P4 · POLG_WNV9
- ProteinGenome polyprotein
- GeneGP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids3433 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (PubMed:22925334).
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
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
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 alpha/beta interferon antiviral 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/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).
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).
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.
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 (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).
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).
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).
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).
Catalytic activity
- RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
RNA-directed RNA polymerase NS5
a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteineRNA-directed RNA polymerase NS5
a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H+
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 105-106 | Cleavage; by viral protease NS3 | |||
Site | 123-124 | Cleavage; by host signal peptidase | |||
Site | 215-216 | Cleavage; by host furin | |||
Site | 290-291 | Cleavage; by host signal peptidase | |||
Site | 791-792 | Cleavage; by host signal peptidase | |||
Site | 1143-1144 | Cleavage; by host | |||
Site | 1374-1375 | Cleavage; by viral protease NS3 | |||
Site | 1505-1506 | Cleavage; by autolysis | |||
Active site | 1556 | Charge relay system; for serine protease NS3 activity | |||
Active site | 1580 | Charge relay system; for serine protease NS3 activity | |||
Active site | 1640 | Charge relay system; for serine protease NS3 activity | |||
Binding site | 1699-1706 | ATP (UniProtKB | ChEBI) | |||
Site | 1754 | Inhibition of host STAT1 phosphorylation | |||
Site | 1963 | Involved in NS3 ATPase and RTPase activities | |||
Site | 1966 | Involved in NS3 ATPase and RTPase activities | |||
Site | 1991 | Inhibition of host STAT1 phosphorylation | |||
Site | 2124-2125 | Cleavage; by autolysis | |||
Site | 2250-2251 | Cleavage; by viral protease NS3 | |||
Site | 2273-2274 | Cleavage; by host signal peptidase | |||
Site | 2528-2529 | Cleavage; by viral protease NS3 | |||
Site | 2541 | mRNA cap binding | |||
Site | 2544 | mRNA cap binding; via carbonyl oxygen | |||
Site | 2545 | mRNA cap binding | |||
Site | 2547 | mRNA cap binding; via carbonyl oxygen | |||
Site | 2552 | mRNA cap binding | |||
Site | 2556 | mRNA cap binding | |||
Binding site | 2584 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Active site | 2589 | For 2'-O-MTase activity | |||
Site | 2589 | Essential for 2'-O-methyltransferase activity | |||
Binding site | 2614 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 2615 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 2632 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 2633 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 2639 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 2659 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 2660 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Active site | 2674 | For 2'-O-MTase activity | |||
Binding site | 2674 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Site | 2674 | Essential for 2'-O-methyltransferase and N-7 methyltransferase activity | |||
Binding site | 2675 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Site | 2678 | mRNA cap binding | |||
Active site | 2710 | For 2'-O-MTase activity | |||
Site | 2710 | Essential for 2'-O-methyltransferase activity | |||
Site | 2741 | mRNA cap binding | |||
Site | 2743 | mRNA cap binding | |||
Active site | 2746 | For 2'-O-MTase activity | |||
Site | 2746 | Essential for 2'-O-methyltransferase activity | |||
Binding site | 2748 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 2968 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 2972 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 2977 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 2980 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 3245 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 3261 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 3380 | Zn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
- Cleaved into 13 chains
Gene names
Organism names
- Strains
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Flasuviricetes > Amarillovirales > Flaviviridae > Orthoflavivirus > Orthoflavivirus nilense
- Virus hosts
Accessions
- Primary accessionQ9Q6P4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Capsid protein C
Peptide pr
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
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Note: Located in RE-derived vesicles hosting the replication complex.
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/Helicase NS3
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Note: Remains non-covalently associated to serine protease subunit NS2B.
Non-structural protein 4A
Host endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Located in RE-derived 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.
RNA-directed RNA polymerase NS5
Host endoplasmic reticulum membrane ; Peripheral membrane protein
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).
Shuttles between the cytoplasm and nucleus (By similarity).
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 2-108 | Cytoplasmic | |||
Transmembrane | 109-129 | Helical | |||
Topological domain | 130-248 | Extracellular | |||
Transmembrane | 249-269 | Helical | |||
Topological domain | 270-275 | Cytoplasmic | |||
Transmembrane | 276-290 | Helical | |||
Topological domain | 291-743 | Extracellular | |||
Transmembrane | 744-764 | Helical | |||
Topological domain | 765-770 | Cytoplasmic | |||
Transmembrane | 771-791 | Helical | |||
Topological domain | 792-1216 | Extracellular | |||
Transmembrane | 1217-1237 | Helical | |||
Topological domain | 1238-1245 | Cytoplasmic | |||
Transmembrane | 1246-1268 | Helical | |||
Topological domain | 1269-1288 | Lumenal | |||
Transmembrane | 1289-1309 | Helical | |||
Topological domain | 1310-1313 | Cytoplasmic | |||
Transmembrane | 1314-1331 | Helical | |||
Topological domain | 1332-1345 | Lumenal | |||
Transmembrane | 1346-1366 | Helical | |||
Topological domain | 1367-1375 | Cytoplasmic | |||
Transmembrane | 1376-1396 | Helical | |||
Topological domain | 1397-1399 | Lumenal | |||
Transmembrane | 1400-1420 | Helical | |||
Topological domain | 1421-1477 | Cytoplasmic | |||
Intramembrane | 1478-1498 | Helical | |||
Topological domain | 1499-2174 | Cytoplasmic | |||
Transmembrane | 2175-2195 | Helical | |||
Topological domain | 2196-2200 | Lumenal | |||
Intramembrane | 2201-2221 | Helical | |||
Topological domain | 2222 | Lumenal | |||
Transmembrane | 2223-2243 | Helical | |||
Topological domain | 2244-2258 | Cytoplasmic | |||
Transmembrane | 2259-2279 | Helical; Note=Signal for NS4B | |||
Topological domain | 2280-2312 | Lumenal | |||
Intramembrane | 2313-2333 | Helical | |||
Topological domain | 2334-2380 | Lumenal | |||
Transmembrane | 2381-2401 | Helical | |||
Topological domain | 2402-2444 | Cytoplasmic | |||
Transmembrane | 2445-2465 | Helical | |||
Topological domain | 2466-2470 | Lumenal | |||
Transmembrane | 2471-2491 | Helical | |||
Topological domain | 2492-3433 | Cytoplasmic | |||
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 444 | Complete loss of glycosylation. Attenuated phenotype. | |||
Mutagenesis | 446 | Complete loss of glycosylation. | |||
Mutagenesis | 446 | Complete loss of glycosylation. Attenuated phenotype. | |||
Mutagenesis | 446 | No effect on glycosylation. No effect on avian virulence properties as NYS, but enhanced host oral infectivity. | |||
Mutagenesis | 968 | No effect on TL3 signaling inhibition by NS1. | |||
Mutagenesis | 982 | No effect on TL3 signaling inhibition by NS1. | |||
Mutagenesis | 1029 | No effect on TL3 signaling inhibition by NS1. | |||
Mutagenesis | 1046 | Complete loss of TL3 signaling inhibition by NS1. | |||
Mutagenesis | 1086 | Almost no effect on TL3 signaling inhibition by NS1. | |||
Mutagenesis | 1108 | Complete loss of TL3 signaling inhibition by NS1. | |||
Mutagenesis | 1111 | About 50% loss of TL3 signaling inhibition by NS1. | |||
Mutagenesis | 1124 | About 50% loss of TL3 signaling inhibition by NS1. | |||
Mutagenesis | 2169-2173 | Complete loss of regulation of the ATPase activity of NS3 helicase by NS4A. | |||
Mutagenesis | 2557 | 85% loss of NS5-GMP formation. | |||
Mutagenesis | 2589 | Complete loss of 2'-O-methyltransferase activity. | |||
Mutagenesis | 2674 | Complete loss of 2'-O-methyltransferase activity. | |||
Mutagenesis | 2676 | 86% loss of N7 guanine methyltransferase activity; 60% loss of 2'-O-methyltransferase activity. | |||
Mutagenesis | 2688 | 78% loss of N7 guanine methyltransferase activity; no effect 2'-O-methyltransferase activity. | |||
Mutagenesis | 2691 | 50% loss of N7 guanine methyltransferase activity; no effect 2'-O-methyltransferase activity. | |||
Mutagenesis | 2692 | 10% loss of N7 guanine methyltransferase activity; 50% loss of 2'-O-methyltransferase activity. | |||
Mutagenesis | 2710 | Complete loss of 2'-O-methyltransferase activity. | |||
Mutagenesis | 2712 | 20% loss of N7 guanine methyltransferase activity7; 74% loss of 2'-O-methyltransferase activity. | |||
Mutagenesis | 2746 | Complete loss of 2'-O-methyltransferase activity. | |||
PTM/Processing
Features
Showing features for chain, propeptide, glycosylation, disulfide bond, modified residue, peptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000441577 | 1-105 | Capsid protein C | ||
Chain | PRO_0000441576 | 1-3433 | Genome polyprotein | ||
Propeptide | PRO_0000441578 | 106-123 | ER anchor for the capsid protein C, removed in mature form by serine protease NS3 | ||
Chain | PRO_0000441580 | 124-215 | Peptide pr | ||
Chain | PRO_0000441579 | 124-290 | Protein prM | ||
Glycosylation | 138 | N-linked (GlcNAc...) asparagine; by host | |||
Chain | PRO_0000441581 | 216-290 | Small envelope protein M | ||
Chain | PRO_0000441582 | 291-791 | Envelope protein E | ||
Disulfide bond | 293↔320 | ||||
Disulfide bond | 350↔406 | ||||
Disulfide bond | 350↔411 | ||||
Disulfide bond | 364↔395 | ||||
Disulfide bond | 382↔406 | ||||
Disulfide bond | 382↔411 | ||||
Glycosylation | 444 | N-linked (GlcNAc...) asparagine; by host | |||
Disulfide bond | 480↔578 | ||||
Disulfide bond | 595↔626 | ||||
Chain | PRO_0000441583 | 792-1143 | Non-structural protein 1 | ||
Disulfide bond | 795↔806 | ||||
Disulfide bond | 846↔934 | ||||
Glycosylation | 921 | N-linked (GlcNAc...) asparagine; by host | |||
Glycosylation | 966 | N-linked (GlcNAc...) asparagine; by host | |||
Disulfide bond | 970↔1014 | ||||
Glycosylation | 998 | N-linked (GlcNAc...) asparagine; by host | |||
Disulfide bond | 1071↔1120 | ||||
Disulfide bond | 1082↔1103 | ||||
Disulfide bond | 1104↔1107 | ||||
Chain | PRO_0000441584 | 1144-1374 | Non-structural protein 2A | ||
Chain | PRO_0000441585 | 1375-1505 | Serine protease subunit NS2B | ||
Chain | PRO_0000441586 | 1506-2124 | Serine protease/Helicase NS3 | ||
Modified residue | 1894 | N6-acetyllysine; by host | |||
Chain | PRO_0000441587 | 2125-2250 | Non-structural protein 4A | ||
Peptide | PRO_0000441588 | 2251-2273 | Peptide 2k | ||
Chain | PRO_0000441589 | 2274-2528 | Non-structural protein 4B | ||
Chain | PRO_0000441590 | 2529-3433 | RNA-directed RNA polymerase NS5 | ||
Modified residue | 2584 | Phosphoserine | |||
Post-translational modification
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.
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.
Envelope protein E
N-glycosylated.
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).
The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells (By similarity).
Serine protease/Helicase NS3
Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication.
RNA-directed RNA polymerase NS5
Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.
Keywords
- PTM
PTM databases
Interaction
Subunit
Capsid protein C
Homodimer (By similarity).
Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity).
Interacts with host DDX56; this interaction plays an important role in genomic RNA encapsidation (PubMed:22925334).
Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity).
Interacts with host DDX56; this interaction plays an important role in genomic RNA encapsidation (PubMed:22925334).
Protein prM
Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (By similarity).
Envelope protein E
Homodimer; in the endoplasmic reticulum and Golgi (PubMed:20956322).
Non-structural protein 1
Homodimer; Homohexamer when secreted (PubMed:24505133, PubMed:24594604).
NS1 interacts with NS4B (PubMed:22553322).
Interacts with host complement protein CFH; this interaction leads to the degradation of C3 (PubMed:17132743).
NS1 interacts with NS4B (PubMed:22553322).
Interacts with host complement protein CFH; this interaction leads to the degradation of C3 (PubMed:17132743).
Serine protease subunit NS2B
Forms a heterodimer with serine protease NS3. May form homooligomers (By similarity).
Interacts with human SPCS1 (PubMed:29593046).
Interacts with human SPCS1 (PubMed:29593046).
Serine protease/Helicase NS3
Forms a heterodimer with NS2B (By similarity).
Interacts with NS4B (By similarity).
Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity).
Interacts with NS4B (By similarity).
Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity).
Non-structural protein 4A
Interacts with host RTN3; this interaction is important to remodel host cell membranes (PubMed:29117567).
Non-structural protein 4B
Interacts with Serine protease/Helicase NS3 (By similarity).
Interacts with NS1 (PubMed:22553322).
Interacts with NS1 (PubMed:22553322).
RNA-directed RNA polymerase NS5
Homodimer (By similarity).
Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (By similarity).
Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (By similarity).
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 2-15 | Interaction with host EXOC1 | |||
Region | 37-72 | Hydrophobic; homodimerization of capsid protein C | |||
Region | 388-401 | Fusion peptide | |||
Region | 1428-1467 | Interacts with and activates NS3 protease | |||
Domain | 1506-1683 | Peptidase S7 | |||
Domain | 1686-1842 | Helicase ATP-binding | |||
Region | 1690-1693 | Important for RNA-binding | |||
Motif | 1790-1793 | DEAH box | |||
Domain | 1853-2018 | Helicase C-terminal | |||
Region | 2169-2173 | Regulates the ATPase activity of NS3 helicase | |||
Domain | 2529-2794 | mRNA cap 0-1 NS5-type MT | |||
Motif | 2917-2919 | Nuclear localization signal | |||
Domain | 3058-3210 | RdRp catalytic | |||
Motif | 3431-3433 | PDZ-binding | |||
Domain
Small envelope protein M
The transmembrane domains contain an endoplasmic reticulum retention signal.
Envelope protein E
The transmembrane domains contain an endoplasmic reticulum retention signal.
RNA-directed RNA polymerase NS5
Contains a PDZ-binding motif that binds to several PDZ-containing cellular proteins. These interactions seem necessary for an optimal viral replication.
Sequence similarities
In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,433
- Mass (Da)381,176
- Last updated2001-03-01 v2
- MD5 ChecksumEFF65EEF6616F54D651EDCB674659A4C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF196835 EMBL· GenBank· DDBJ | AAF20092.2 EMBL· GenBank· DDBJ | Genomic RNA | ||
AF404755 EMBL· GenBank· DDBJ | AAM81751.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
HM488125 EMBL· GenBank· DDBJ | ADL27936.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
HM488126 EMBL· GenBank· DDBJ | ADL27937.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
HM488127 EMBL· GenBank· DDBJ | ADL27938.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
HM488128 EMBL· GenBank· DDBJ | ADL27939.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
KC407666 EMBL· GenBank· DDBJ | AGI15883.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
KM083619 EMBL· GenBank· DDBJ | AIO10814.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
KX547386 EMBL· GenBank· DDBJ | ANW69091.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
KX547393 EMBL· GenBank· DDBJ | ANW69112.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
AB185914 EMBL· GenBank· DDBJ | BAD34488.1 EMBL· GenBank· DDBJ | Genomic RNA |