Q2YHF0 · POLG_DEN4T
- ProteinGenome polyprotein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids3387 (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. 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 1
Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.
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.
Non-structural protein 4A
Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between RIGI and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity).
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. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).
May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity).
May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity).
Catalytic activity
Serine protease NS3
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.RNA-directed RNA polymerase NS5
a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 99-100 | Cleavage; by viral protease NS3 | ||||
Sequence: RS | ||||||
Site | 113-114 | Cleavage; by host signal peptidase | ||||
Sequence: AF | ||||||
Site | 204-205 | Cleavage; by host furin | ||||
Sequence: RS | ||||||
Site | 279-280 | Cleavage; by host signal peptidase | ||||
Sequence: GM | ||||||
Site | 774-775 | Cleavage; by host signal peptidase | ||||
Sequence: AD | ||||||
Site | 1126-1127 | Cleavage; by host | ||||
Sequence: AG | ||||||
Site | 1344-1345 | Cleavage; by viral protease NS3 | ||||
Sequence: RS | ||||||
Site | 1474-1475 | Cleavage; by autolysis | ||||
Sequence: RS | ||||||
Active site | 1525 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: H | ||||||
Active site | 1549 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: D | ||||||
Active site | 1609 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: S | ||||||
Binding site | 1667-1674 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LHPGAGKT | ||||||
Site | 1931 | Involved in NS3 ATPase and RTPase activities | ||||
Sequence: R | ||||||
Site | 1934 | Involved in NS3 ATPase and RTPase activities | ||||
Sequence: R | ||||||
Site | 2092-2093 | Cleavage; by autolysis | ||||
Sequence: KS | ||||||
Site | 2219-2220 | Cleavage; by viral protease NS3 | ||||
Sequence: RT | ||||||
Site | 2242-2243 | Cleavage; by host signal peptidase | ||||
Sequence: AN | ||||||
Site | 2487-2488 | Cleavage; by viral protease NS3 | ||||
Sequence: RG | ||||||
Site | 2501 | mRNA cap binding | ||||
Sequence: K | ||||||
Site | 2504 | mRNA cap binding; via carbonyl oxygen | ||||
Sequence: L | ||||||
Site | 2505 | mRNA cap binding | ||||
Sequence: N | ||||||
Site | 2507 | mRNA cap binding; via carbonyl oxygen | ||||
Sequence: L | ||||||
Site | 2512 | mRNA cap binding | ||||
Sequence: F | ||||||
Site | 2516 | mRNA cap binding | ||||
Sequence: K | ||||||
Binding site | 2543 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 2548 | For 2'-O-MTase activity | ||||
Sequence: K | ||||||
Site | 2548 | Essential for 2'-O-methyltransferase activity | ||||
Sequence: K | ||||||
Binding site | 2573 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 2574 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 2591 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 2592 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2618 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 2619 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Active site | 2633 | For 2'-O-MTase activity | ||||
Sequence: D | ||||||
Site | 2633 | Essential for 2'-O-methyltransferase and N-7 methyltransferase activity | ||||
Sequence: D | ||||||
Binding site | 2634 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Site | 2637 | mRNA cap binding | ||||
Sequence: S | ||||||
Active site | 2668 | For 2'-O-MTase activity | ||||
Sequence: K | ||||||
Site | 2668 | Essential for 2'-O-methyltransferase activity | ||||
Sequence: K | ||||||
Site | 2699 | mRNA cap binding | ||||
Sequence: R | ||||||
Site | 2701 | mRNA cap binding | ||||
Sequence: S | ||||||
Active site | 2704 | For 2'-O-MTase activity | ||||
Sequence: E | ||||||
Site | 2704 | Essential for 2'-O-methyltransferase activity | ||||
Sequence: E | ||||||
Binding site | 2706 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 2925 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2929 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2934 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2937 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3200 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 3216 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3335 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
- Cleaved into 13 chains
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Flasuviricetes > Amarillovirales > Flaviviridae > Orthoflavivirus > Orthoflavivirus denguei > Dengue virus
- Virus hosts
Accessions
- Primary accessionQ2YHF0
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
Envelope protein E
Virion membrane ; Multi-pass membrane protein
Host endoplasmic reticulum membrane ; Multi-pass membrane protein
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 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-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes.
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, especially in the DENV 2, 3, 4 serotypes.
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-100 | Cytoplasmic | ||||
Sequence: MNQRKKVARPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKILTGFRKEIGRMLNILNGRKRS | ||||||
Transmembrane | 101-117 | Helical | ||||
Sequence: TITLLCLIPTVMAFHLS | ||||||
Topological domain | 118-237 | Extracellular | ||||
Sequence: TRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCEDTVTYKCPLLVNTEPEDIDCWCNLTSAWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVE | ||||||
Transmembrane | 238-258 | Helical | ||||
Sequence: SWILRNPGFALLAGFMAYMIG | ||||||
Topological domain | 259-265 | Cytoplasmic | ||||
Sequence: QTGIQRT | ||||||
Transmembrane | 266-279 | Helical | ||||
Sequence: VFFILMMLVAPSYG | ||||||
Topological domain | 280-725 | Extracellular | ||||
Sequence: MRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTLDFELIKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDMVDRGWGNGCGLFGKGGVVTCAKFSCSGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTATITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKMKTKTWLVHKQWFLDLPLPWTAGADTLEVHWNHKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAGHLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGTGAPCKVPIEIRDVNKEKVVGRIISSTPFAENTNSVTNIELEPPFGDSYIVIGVGDSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLLTSLGKAVHQVFGSVYTT | ||||||
Transmembrane | 726-746 | Helical | ||||
Sequence: MFGGVSWMVRILIGLLVLWIG | ||||||
Topological domain | 747-753 | Cytoplasmic | ||||
Sequence: TNSRNTS | ||||||
Transmembrane | 754-774 | Helical | ||||
Sequence: MAMSCIAVGGITLFLGFTVHA | ||||||
Topological domain | 775-1194 | Extracellular | ||||
Sequence: DMGCAVSWSGKELKCGSGIFVIDNVHTWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLSKGKRALAPPVNDLKYSWKTWGKAKIFTPETRNSTFLVDGPDTSECPNERRAWNFLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSAAIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKAYAGPISQHNYRQGYATQTVGPWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLNEKEENMVKSQVSAGQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVTTLCAIILGGLTWMDLLRALIMLGDTMSGRM | ||||||
Transmembrane | 1195-1218 | Helical | ||||
Sequence: GGQIHLAIMAVFKMSPGYVLGIFL | ||||||
Topological domain | 1219-1224 | Lumenal | ||||
Sequence: RKLTSR | ||||||
Transmembrane | 1225-1243 | Helical | ||||
Sequence: ETALMVIGMAMTTVLSIPH | ||||||
Topological domain | 1244-1267 | Cytoplasmic | ||||
Sequence: DLMEFIDGISLGLILLKMVTHFDN | ||||||
Transmembrane | 1268-1288 | Helical | ||||
Sequence: TQVGTLALSLTFIKSTMPLVM | ||||||
Topological domain | 1289 | Lumenal | ||||
Sequence: A | ||||||
Transmembrane | 1290-1308 | Helical | ||||
Sequence: WRTIMAVLFVVTLIPLCRT | ||||||
Topological domain | 1309-1316 | Lumenal | ||||
Sequence: SCLQKQSH | ||||||
Transmembrane | 1317-1337 | Helical | ||||
Sequence: WVEITALILGAQALPVYLMTL | ||||||
Topological domain | 1338-1345 | Cytoplasmic | ||||
Sequence: MKGASKRS | ||||||
Transmembrane | 1346-1366 | Helical | ||||
Sequence: WPLNEGIMAVGLVSLLGSALL | ||||||
Topological domain | 1367-1369 | Lumenal | ||||
Sequence: KND | ||||||
Transmembrane | 1370-1390 | Helical | ||||
Sequence: VPLAGPMVAGGLLLAAYVMSG | ||||||
Topological domain | 1391-1437 | Cytoplasmic | ||||
Sequence: SSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETN | ||||||
Intramembrane | 1438-1458 | Helical | ||||
Sequence: MITLLVKLALITVSGLYPLAI | ||||||
Topological domain | 1459-2143 | Cytoplasmic | ||||
Sequence: PVTMTLWYMWQVKTQRSGALWDVPSPAAAQKATLTEGVYRIMQRGLFGKTQVGVGIHMEGVFHTMWHVTRGSVICHESGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAVTLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPSIVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEAHFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGTTDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIKAGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILTDGPERVILAGPIPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLRNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLRGEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMALKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGKAYQHALNELPES | ||||||
Transmembrane | 2144-2164 | Helical | ||||
Sequence: LETLMLVALLGAMTAGIFLFF | ||||||
Topological domain | 2165-2169 | Lumenal | ||||
Sequence: MQGKG | ||||||
Intramembrane | 2170-2190 | Helical | ||||
Sequence: IGKLSMGLIAIAVASGLLWVA | ||||||
Topological domain | 2191 | Lumenal | ||||
Sequence: E | ||||||
Transmembrane | 2192-2212 | Helical | ||||
Sequence: IQPQWIAASIILEFFLMVLLV | ||||||
Topological domain | 2213-2225 | Cytoplasmic | ||||
Sequence: PEPEKQRTPQDNQ | ||||||
Transmembrane | 2226-2246 | Helical; Note=Signal for NS4B | ||||
Sequence: LIYVILTILTIIALVAANEMG | ||||||
Topological domain | 2247-2270 | Lumenal | ||||
Sequence: LIEKTKTDFGFYQAKTETTILDVD | ||||||
Intramembrane | 2271-2291 | Helical | ||||
Sequence: LRPASAWTLYAVATTILTPML | ||||||
Topological domain | 2292-2301 | Lumenal | ||||
Sequence: RHTIENTSAN | ||||||
Intramembrane | 2302-2322 | Helical | ||||
Sequence: LSLAAIANQAAVLMGLGKGWP | ||||||
Topological domain | 2323-2343 | Lumenal | ||||
Sequence: LHRMDLGVPLLAMGCYSQVNP | ||||||
Transmembrane | 2344-2364 | Helical | ||||
Sequence: TTLTASLVMLLVHYAIIGPGL | ||||||
Topological domain | 2365-2409 | Cytoplasmic | ||||
Sequence: QAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYDPKFEKQLGQ | ||||||
Transmembrane | 2410-2430 | Helical | ||||
Sequence: VMLLVLCAGQLLLMRTTWAFC | ||||||
Topological domain | 2431-2455 | Lumenal | ||||
Sequence: EVLTLATGPILTLWEGNPGRFWNTT | ||||||
Transmembrane | 2456-2476 | Helical | ||||
Sequence: IAVSTANIFRGSYLAGAGLAF | ||||||
Topological domain | 2477-3387 | Cytoplasmic | ||||
Sequence: SLIKNAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKYAVSRGTSKIRWIVERGMVKPKGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSNPTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLVRCPLSRNSTHEMYWVSGVSGNIVSSVNTTSKMLLNRFTTRHRKPTYEKDADLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDHENPYRTWAYHGSYEAPSTGSASSMVNGVVKLLTKPWDVVPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRVVMTTTANWLWALLGRKKNPRLCTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDKKDGDLIYADDTAGWDTRITEDDLLNEELITEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITRDDMHNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHHFHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSRTTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMIDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIQTAITQVRNLIGKEEYVDYMPVMKRYSAHFESEGVL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, propeptide, glycosylation, disulfide bond, modified residue, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000268131 | 1-99 | Capsid protein C | |||
Sequence: MNQRKKVARPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKILTGFRKEIGRMLNILNGRKR | ||||||
Chain | PRO_0000405229 | 1-3387 | Genome polyprotein | |||
Sequence: MNQRKKVARPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKILTGFRKEIGRMLNILNGRKRSTITLLCLIPTVMAFHLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCEDTVTYKCPLLVNTEPEDIDCWCNLTSAWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWILRNPGFALLAGFMAYMIGQTGIQRTVFFILMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTLDFELIKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDMVDRGWGNGCGLFGKGGVVTCAKFSCSGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTATITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKMKTKTWLVHKQWFLDLPLPWTAGADTLEVHWNHKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAGHLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGTGAPCKVPIEIRDVNKEKVVGRIISSTPFAENTNSVTNIELEPPFGDSYIVIGVGDSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLLTSLGKAVHQVFGSVYTTMFGGVSWMVRILIGLLVLWIGTNSRNTSMAMSCIAVGGITLFLGFTVHADMGCAVSWSGKELKCGSGIFVIDNVHTWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLSKGKRALAPPVNDLKYSWKTWGKAKIFTPETRNSTFLVDGPDTSECPNERRAWNFLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSAAIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKAYAGPISQHNYRQGYATQTVGPWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLNEKEENMVKSQVSAGQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVTTLCAIILGGLTWMDLLRALIMLGDTMSGRMGGQIHLAIMAVFKMSPGYVLGIFLRKLTSRETALMVIGMAMTTVLSIPHDLMEFIDGISLGLILLKMVTHFDNTQVGTLALSLTFIKSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASKRSWPLNEGIMAVGLVSLLGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMITLLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQRSGALWDVPSPAAAQKATLTEGVYRIMQRGLFGKTQVGVGIHMEGVFHTMWHVTRGSVICHESGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAVTLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPSIVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEAHFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGTTDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIKAGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILTDGPERVILAGPIPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLRNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLRGEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMALKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGKAYQHALNELPESLETLMLVALLGAMTAGIFLFFMQGKGIGKLSMGLIAIAVASGLLWVAEIQPQWIAASIILEFFLMVLLVPEPEKQRTPQDNQLIYVILTILTIIALVAANEMGLIEKTKTDFGFYQAKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKGWPLHRMDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYDPKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPILTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIKNAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKYAVSRGTSKIRWIVERGMVKPKGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSNPTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLVRCPLSRNSTHEMYWVSGVSGNIVSSVNTTSKMLLNRFTTRHRKPTYEKDADLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDHENPYRTWAYHGSYEAPSTGSASSMVNGVVKLLTKPWDVVPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRVVMTTTANWLWALLGRKKNPRLCTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDKKDGDLIYADDTAGWDTRITEDDLLNEELITEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITRDDMHNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHHFHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSRTTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMIDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIQTAITQVRNLIGKEEYVDYMPVMKRYSAHFESEGVL | ||||||
Propeptide | PRO_0000268132 | 100-113 | ER anchor for the capsid protein C, removed in mature form by serine protease NS3 | |||
Sequence: STITLLCLIPTVMA | ||||||
Chain | PRO_0000268134 | 114-204 | Peptide pr | |||
Sequence: FHLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCEDTVTYKCPLLVNTEPEDIDCWCNLTSAWVMYGTCTQSGERRREKR | ||||||
Chain | PRO_0000268133 | 114-279 | Protein prM | |||
Sequence: FHLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCEDTVTYKCPLLVNTEPEDIDCWCNLTSAWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWILRNPGFALLAGFMAYMIGQTGIQRTVFFILMMLVAPSYG | ||||||
Glycosylation | 182 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000268135 | 205-279 | Small envelope protein M | |||
Sequence: SVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWILRNPGFALLAGFMAYMIGQTGIQRTVFFILMMLVAPSYG | ||||||
Chain | PRO_0000268136 | 280-774 | Envelope protein E | |||
Sequence: MRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTLDFELIKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDMVDRGWGNGCGLFGKGGVVTCAKFSCSGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTATITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKMKTKTWLVHKQWFLDLPLPWTAGADTLEVHWNHKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAGHLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGTGAPCKVPIEIRDVNKEKVVGRIISSTPFAENTNSVTNIELEPPFGDSYIVIGVGDSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLLTSLGKAVHQVFGSVYTTMFGGVSWMVRILIGLLVLWIGTNSRNTSMAMSCIAVGGITLFLGFTVHA | ||||||
Disulfide bond | 282↔309 | |||||
Sequence: CVGVGNRDFVEGVSGGAWVDLVLEHGGC | ||||||
Disulfide bond | 339↔400 | |||||
Sequence: CIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDMVDRGWGNGCGLFGKGGVVTCAKFSC | ||||||
Glycosylation | 346 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 353↔384 | |||||
Sequence: CPTQGEPYLKEEQDQQYICRRDMVDRGWGNGC | ||||||
Disulfide bond | 371↔395 | |||||
Sequence: CRRDMVDRGWGNGCGLFGKGGVVTC | ||||||
Glycosylation | 432 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 464↔564 | |||||
Sequence: CEPRSGIDFNEMILMKMKTKTWLVHKQWFLDLPLPWTAGADTLEVHWNHKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAGHLKC | ||||||
Disulfide bond | 581↔612 | |||||
Sequence: CSGKFSIDKEMAETQHGTTVVKVKYEGTGAPC | ||||||
Chain | PRO_0000268137 | 775-1126 | Non-structural protein 1 | |||
Sequence: DMGCAVSWSGKELKCGSGIFVIDNVHTWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLSKGKRALAPPVNDLKYSWKTWGKAKIFTPETRNSTFLVDGPDTSECPNERRAWNFLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSAAIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKAYAGPISQHNYRQGYATQTVGPWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLNEKEENMVKSQVSA | ||||||
Disulfide bond | 778↔789 | |||||
Sequence: CAVSWSGKELKC | ||||||
Disulfide bond | 829↔917 | |||||
Sequence: CGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLSKGKRALAPPVNDLKYSWKTWGKAKIFTPETRNSTFLVDGPDTSEC | ||||||
Glycosylation | 904 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 953↔997 | |||||
Sequence: CDHRLMSAAIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTC | ||||||
Glycosylation | 981 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 1054↔1103 | |||||
Sequence: CPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGC | ||||||
Disulfide bond | 1065↔1087 | |||||
Sequence: CDHRGPSLRTTTASGKLVTQWCC | ||||||
Disulfide bond | 1086↔1090 | |||||
Sequence: CCRSC | ||||||
Chain | PRO_0000268138 | 1127-1344 | Non-structural protein 2A | |||
Sequence: GQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVTTLCAIILGGLTWMDLLRALIMLGDTMSGRMGGQIHLAIMAVFKMSPGYVLGIFLRKLTSRETALMVIGMAMTTVLSIPHDLMEFIDGISLGLILLKMVTHFDNTQVGTLALSLTFIKSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASKR | ||||||
Chain | PRO_0000268139 | 1345-1474 | Serine protease subunit NS2B | |||
Sequence: SWPLNEGIMAVGLVSLLGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMITLLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQR | ||||||
Chain | PRO_0000268140 | 1475-2092 | Serine protease NS3 | |||
Sequence: SGALWDVPSPAAAQKATLTEGVYRIMQRGLFGKTQVGVGIHMEGVFHTMWHVTRGSVICHESGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAVTLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPSIVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEAHFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGTTDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIKAGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILTDGPERVILAGPIPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLRNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLRGEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMALKDFKEFASGRK | ||||||
Modified residue | 1862 | N6-acetyllysine; by host | ||||
Sequence: K | ||||||
Chain | PRO_0000268141 | 2093-2219 | Non-structural protein 4A | |||
Sequence: SITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGKAYQHALNELPESLETLMLVALLGAMTAGIFLFFMQGKGIGKLSMGLIAIAVASGLLWVAEIQPQWIAASIILEFFLMVLLVPEPEKQR | ||||||
Peptide | PRO_0000268142 | 2220-2242 | Peptide 2k | |||
Sequence: TPQDNQLIYVILTILTIIALVAA | ||||||
Chain | PRO_0000268143 | 2243-2487 | Non-structural protein 4B | |||
Sequence: NEMGLIEKTKTDFGFYQAKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKGWPLHRMDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYDPKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPILTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIKNAQTPRR | ||||||
Glycosylation | 2297 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 2301 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 2453 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000268144 | 2488-3387 | RNA-directed RNA polymerase NS5 | |||
Sequence: GTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKYAVSRGTSKIRWIVERGMVKPKGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSNPTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLVRCPLSRNSTHEMYWVSGVSGNIVSSVNTTSKMLLNRFTTRHRKPTYEKDADLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDHENPYRTWAYHGSYEAPSTGSASSMVNGVVKLLTKPWDVVPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRVVMTTTANWLWALLGRKKNPRLCTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDKKDGDLIYADDTAGWDTRITEDDLLNEELITEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITRDDMHNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHHFHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSRTTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMIDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIQTAITQVRNLIGKEEYVDYMPVMKRYSAHFESEGVL | ||||||
Modified residue | 2543 | Phosphoserine | ||||
Sequence: S |
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. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.
Serine protease 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
Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication.
RNA-directed RNA polymerase NS5
Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.
Keywords
- PTM
Interaction
Subunit
Capsid protein C
Homodimer. Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway.
Protein prM
Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi.
Envelope protein E
Homodimer; in the endoplasmic reticulum and Golgi. Interacts with protein prM. Interacts with non-structural protein 1.
Non-structural protein 1
Homodimer; Homohexamer when secreted. Interacts with envelope protein E.
Non-structural protein 2A
Interacts (via N-terminus) with serine protease NS3.
Serine protease subunit NS2B
Forms a heterodimer with serine protease NS3. May form homooligomers.
Serine protease NS3
Forms a heterodimer with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. Interacts with host SHFL.
Non-structural protein 4A
Interacts with host MAVS; this interaction inhibits the synthesis of IFN-beta. Interacts with host SHFL. Interacts with host AUP1; the interaction occurs in the presence of Dengue virus NS4B and induces lipophagy which facilitates production of virus progeny particles (By similarity).
Non-structural protein 4B
Interacts with serine protease NS3.
RNA-directed RNA polymerase NS5
Homodimer. Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation. Interacts with serine protease NS3 (By similarity).
Interacts with host PAF1 complex; the interaction may prevent the recruitment of the PAF1 complex to interferon-responsive genes, and thus reduces the immune response (By similarity).
Interacts with host PAF1 complex; the interaction may prevent the recruitment of the PAF1 complex to interferon-responsive genes, and thus reduces the immune response (By similarity).
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 36-71 | Hydrophobic; homodimerization of capsid protein C | ||||
Sequence: LFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQL | ||||||
Region | 377-390 | Fusion peptide | ||||
Sequence: DRGWGNGCGLFGKG | ||||||
Region | 1397-1436 | Interacts with and activates NS3 protease | ||||
Sequence: LEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEET | ||||||
Domain | 1475-1652 | Peptidase S7 | ||||
Sequence: SGALWDVPSPAAAQKATLTEGVYRIMQRGLFGKTQVGVGIHMEGVFHTMWHVTRGSVICHESGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAVTLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEV | ||||||
Domain | 1654-1810 | Helicase ATP-binding | ||||
Sequence: EDIFRKKRLTIMDLHPGAGKTKRILPSIVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEAHFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGTTDPFPQSNSPIEDIE | ||||||
Region | 1658-1661 | Important for RNA-binding | ||||
Sequence: RKKR | ||||||
Motif | 1758-1761 | DEAH box | ||||
Sequence: DEAH | ||||||
Domain | 1820-1987 | Helicase C-terminal | ||||
Sequence: TGFDWITDYQGKTVWFVPSIKAGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILTDGPERVILAGPIPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLRNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPER | ||||||
Domain | 2489-2751 | mRNA cap 0-1 NS5-type MT | ||||
Sequence: TGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKYAVSRGTSKIRWIVERGMVKPKGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSNPTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLVRCPLSRNSTHEMYWVSGVSGNIVSSVNTTSKMLLNRFTTRHRKPTYEKDADLGAGTRS | ||||||
Motif | 2564-2567 | SUMO-interacting motif | ||||
Sequence: VVDL | ||||||
Domain | 3016-3166 | RdRp catalytic | ||||
Sequence: LIYADDTAGWDTRITEDDLLNEELITEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITRDDMHNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSL |
Domain
The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.
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
- Length3,387
- Mass (Da)378,438
- Last updated2005-12-20 v1
- Checksum1FEDC2D663A0F945
Keywords
- Technical term