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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 4 (strain Thailand/0348/1991) (DENV-4)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.By similarity
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.By similarity
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.By similarity
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.By similarity
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.By similarity
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.By similarity
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).By similarity
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.By similarity
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy 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.PROSITE-ProRule annotation
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 DDX58 and MAVS. In turn, IFN-beta production is impaired.By similarity
Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
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.By similarity
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

Catalytic activityi

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.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1525Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1549Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1609Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1931Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1934Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2501mRNA capPROSITE-ProRule annotation1
Binding sitei2504mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2505mRNA capPROSITE-ProRule annotation1
Binding sitei2507mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2512mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2516mRNA capPROSITE-ProRule annotation1
Binding sitei2543S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2548For 2'-O-MTase activityBy similarity1
Sitei2548Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2573S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2574S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2591S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2592S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2618S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2619S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2633For 2'-O-MTase activityBy similarity1
Sitei2633Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2634S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2637mRNA capPROSITE-ProRule annotation1
Active sitei2668For 2'-O-MTase activityBy similarity1
Sitei2668Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2699mRNA capPROSITE-ProRule annotation1
Binding sitei2701mRNA capPROSITE-ProRule annotation1
Active sitei2704For 2'-O-MTase activityBy similarity1
Sitei2704Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2706S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2925Zinc 1By similarity1
Metal bindingi2929Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2934Zinc 1By similarity1
Metal bindingi2937Zinc 1By similarity1
Metal bindingi3200Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3216Zinc 2By similarity1
Metal bindingi3335Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1667 – 1674ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase, Viral ion channel
Biological processActivation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT2 by virus, Inhibition of host TYK2 by virus, Ion transport, mRNA capping, mRNA processing, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDAi3.4.21.91 9641

Protein family/group databases

MEROPSiS07.001

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 5
OrganismiDengue virus type 4 (strain Thailand/0348/1991) (DENV-4)
Taxonomic identifieri408688 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000000273 Componenti: Genome

Subcellular locationi

Capsid protein C :
  • Virion By similarity
  • Host nucleus By similarity
  • Host cytoplasm By similarity
  • host perinuclear region By similarity
Peptide pr :
  • Secreted By similarity
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
  • Secreted By similarity
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
Non-structural protein 2A :
Serine protease subunit NS2B :
Serine protease NS3 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Note: Remains non-covalently associated to serine protease subunit NS2B.PROSITE-ProRule annotation
Non-structural protein 4A :
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Host mitochondrion By similarity
  • Note: Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes.By similarity
Non-structural protein 4B :
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Host nucleus By similarity
  • 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.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 100CytoplasmicSequence analysisAdd BLAST100
Transmembranei101 – 117HelicalSequence analysisAdd BLAST17
Topological domaini118 – 237ExtracellularSequence analysisAdd BLAST120
Transmembranei238 – 258HelicalSequence analysisAdd BLAST21
Topological domaini259 – 265CytoplasmicSequence analysis7
Transmembranei266 – 279HelicalSequence analysisAdd BLAST14
Topological domaini280 – 725ExtracellularSequence analysisAdd BLAST446
Transmembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 753CytoplasmicSequence analysis7
Transmembranei754 – 774HelicalSequence analysisAdd BLAST21
Topological domaini775 – 1194ExtracellularSequence analysisAdd BLAST420
Transmembranei1195 – 1218HelicalSequence analysisAdd BLAST24
Topological domaini1219 – 1224LumenalSequence analysis6
Transmembranei1225 – 1243HelicalSequence analysisAdd BLAST19
Topological domaini1244 – 1267CytoplasmicSequence analysisAdd BLAST24
Transmembranei1268 – 1288HelicalSequence analysisAdd BLAST21
Topological domaini1289LumenalSequence analysis1
Transmembranei1290 – 1308HelicalSequence analysisAdd BLAST19
Topological domaini1309 – 1316LumenalSequence analysis8
Transmembranei1317 – 1337HelicalSequence analysisAdd BLAST21
Topological domaini1338 – 1345CytoplasmicSequence analysis8
Transmembranei1346 – 1366Helical1 PublicationAdd BLAST21
Topological domaini1367 – 1369Lumenal1 Publication3
Transmembranei1370 – 1390Helical1 PublicationAdd BLAST21
Topological domaini1391 – 1437Cytoplasmic1 PublicationAdd BLAST47
Intramembranei1438 – 1458Helical1 PublicationAdd BLAST21
Topological domaini1459 – 2143CytoplasmicSequence analysisAdd BLAST685
Transmembranei2144 – 2164HelicalSequence analysisAdd BLAST21
Topological domaini2165 – 2169LumenalSequence analysis5
Intramembranei2170 – 2190HelicalSequence analysisAdd BLAST21
Topological domaini2191LumenalSequence analysis1
Transmembranei2192 – 2212HelicalSequence analysisAdd BLAST21
Topological domaini2213 – 2225CytoplasmicSequence analysisAdd BLAST13
Transmembranei2226 – 2246Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2247 – 2270LumenalSequence analysisAdd BLAST24
Intramembranei2271 – 2291HelicalSequence analysisAdd BLAST21
Topological domaini2292 – 2301LumenalSequence analysis10
Intramembranei2302 – 2322HelicalSequence analysisAdd BLAST21
Topological domaini2323 – 2343LumenalSequence analysisAdd BLAST21
Transmembranei2344 – 2364HelicalSequence analysisAdd BLAST21
Topological domaini2365 – 2409CytoplasmicSequence analysisAdd BLAST45
Transmembranei2410 – 2430HelicalSequence analysisAdd BLAST21
Topological domaini2431 – 2455LumenalSequence analysisAdd BLAST25
Transmembranei2456 – 2476HelicalSequence analysisAdd BLAST21
Topological domaini2477 – 3387CytoplasmicSequence analysisAdd BLAST911

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host endoplasmic reticulum, Host membrane, Host mitochondrion, Host nucleus, Membrane, Secreted, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004052291 – 3387Genome polyproteinAdd BLAST3387
ChainiPRO_00002681311 – 99Capsid protein CBy similarityAdd BLAST99
PropeptideiPRO_0000268132100 – 113ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST14
ChainiPRO_0000268133114 – 279Protein prMBy similarityAdd BLAST166
ChainiPRO_0000268134114 – 204Peptide prBy similarityAdd BLAST91
ChainiPRO_0000268135205 – 279Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000268136280 – 774Envelope protein EBy similarityAdd BLAST495
ChainiPRO_0000268137775 – 1126Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00002681381127 – 1344Non-structural protein 2ABy similarityAdd BLAST218
ChainiPRO_00002681391345 – 1474Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00002681401475 – 2092Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00002681412093 – 2219Non-structural protein 4ABy similarityAdd BLAST127
PeptideiPRO_00002681422220 – 2242Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00002681432243 – 2487Non-structural protein 4BBy similarityAdd BLAST245
ChainiPRO_00002681442488 – 3387RNA-directed RNA polymerase NS5By similarityAdd BLAST900

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi182N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi282 ↔ 309By similarity
Disulfide bondi339 ↔ 400By similarity
Glycosylationi346N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi353 ↔ 384By similarity
Disulfide bondi371 ↔ 395By similarity
Glycosylationi432N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi464 ↔ 564By similarity
Disulfide bondi581 ↔ 612By similarity
Disulfide bondi778 ↔ 789By similarity
Disulfide bondi829 ↔ 917By similarity
Glycosylationi904N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi953 ↔ 997By similarity
Glycosylationi981N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi1054 ↔ 1103By similarity
Disulfide bondi1065 ↔ 1087By similarity
Disulfide bondi1086 ↔ 1090By similarity
Glycosylationi2297N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2301N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2453N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Modified residuei2543PhosphoserineBy similarity1

Post-translational modificationi

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.By similarity
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.By similarity
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
RNA-directed RNA polymerase NS5: Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei99 – 100Cleavage; by viral protease NS3By similarity2
Sitei113 – 114Cleavage; by host signal peptidaseBy similarity2
Sitei204 – 205Cleavage; by host furinSequence analysisBy similarity2
Sitei279 – 280Cleavage; by host signal peptidaseBy similarity2
Sitei774 – 775Cleavage; by host signal peptidaseBy similarity2
Sitei1126 – 1127Cleavage; by hostBy similarity2
Sitei1344 – 1345Cleavage; by viral protease NS3By similarity2
Sitei1474 – 1475Cleavage; by autolysisBy similarity2
Sitei2092 – 2093Cleavage; by autolysisBy similarity2
Sitei2219 – 2220Cleavage; by viral protease NS3By similarity2
Sitei2242 – 2243Cleavage; by host signal peptidaseBy similarity2
Sitei2487 – 2488Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ2YHF0

Interactioni

Subunit structurei

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. Non-structural protein 2B: 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. Non-structural protein 4A: Interacts with host MAVS; this interaction inhibits the synthesis of IFN-beta. 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

GO - Molecular functioni

Structurei

Secondary structure

13387
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi585 – 589Combined sources5
Beta strandi599 – 605Combined sources7
Beta strandi607 – 609Combined sources3
Beta strandi611 – 613Combined sources3
Beta strandi616 – 619Combined sources4
Beta strandi625 – 630Combined sources6
Beta strandi632 – 634Combined sources3
Beta strandi639 – 642Combined sources4
Beta strandi644 – 649Combined sources6
Beta strandi652 – 661Combined sources10
Helixi662 – 664Combined sources3
Beta strandi665 – 672Combined sources8
Beta strandi1395 – 1401Combined sources7
Beta strandi1496 – 1502Combined sources7
Beta strandi1507 – 1514Combined sources8
Beta strandi1516 – 1518Combined sources3
Beta strandi1520 – 1522Combined sources3
Helixi1524 – 1527Combined sources4
Beta strandi1541 – 1545Combined sources5
Turni1546 – 1549Combined sources4
Beta strandi1550 – 1556Combined sources7
Beta strandi1565 – 1567Combined sources3
Beta strandi1569 – 1573Combined sources5
Beta strandi1581 – 1585Combined sources5
Beta strandi1598 – 1600Combined sources3
Beta strandi1612 – 1614Combined sources3
Beta strandi1616 – 1618Combined sources3
Beta strandi1620 – 1623Combined sources4
Beta strandi1637 – 1640Combined sources4
Beta strandi1645 – 1647Combined sources3
Helixi1654 – 1657Combined sources4
Beta strandi1662 – 1665Combined sources4
Beta strandi1669 – 1671Combined sources3
Turni1673 – 1676Combined sources4
Helixi1677 – 1687Combined sources11
Beta strandi1692 – 1698Combined sources7
Helixi1699 – 1708Combined sources10
Turni1709 – 1711Combined sources3
Beta strandi1714 – 1716Combined sources3
Beta strandi1727 – 1729Combined sources3
Beta strandi1731 – 1735Combined sources5
Helixi1736 – 1745Combined sources10
Beta strandi1753 – 1758Combined sources6
Turni1759 – 1761Combined sources3
Helixi1765 – 1779Combined sources15
Beta strandi1784 – 1788Combined sources5
Beta strandi1806 – 1810Combined sources5
Beta strandi1819 – 1821Combined sources3
Helixi1823 – 1827Combined sources5
Beta strandi1832 – 1835Combined sources4
Helixi1839 – 1850Combined sources12
Turni1851 – 1853Combined sources3
Beta strandi1856 – 1859Combined sources4
Turni1861 – 1863Combined sources3
Helixi1864 – 1867Combined sources4
Helixi1868 – 1872Combined sources5
Beta strandi1877 – 1881Combined sources5
Helixi1883 – 1886Combined sources4
Beta strandi1894 – 1898Combined sources5
Beta strandi1901 – 1908Combined sources8
Beta strandi1910 – 1912Combined sources3
Beta strandi1914 – 1922Combined sources9
Helixi1925 – 1932Combined sources8
Beta strandi1935 – 1938Combined sources4
Beta strandi1944 – 1948Combined sources5
Helixi1960 – 1969Combined sources10
Helixi1984 – 1989Combined sources6
Turni1994 – 1997Combined sources4
Helixi2001 – 2012Combined sources12
Helixi2018 – 2026Combined sources9
Helixi2035 – 2037Combined sources3
Helixi2042 – 2044Combined sources3
Beta strandi2047 – 2052Combined sources6
Beta strandi2054 – 2056Combined sources3
Beta strandi2062 – 2064Combined sources3
Helixi2072 – 2074Combined sources3
Helixi2078 – 2088Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JLQX-ray1.67A1646-2092[»]
2JLRX-ray2.00A1646-2092[»]
2JLSX-ray2.23A1646-2092[»]
2JLUX-ray2.04A/B1646-2092[»]
2JLVX-ray2.30A/B1646-2092[»]
2JLWX-ray2.60A/B1646-2092[»]
2JLXX-ray2.20A/B1646-2092[»]
2JLYX-ray2.40A/B1646-2092[»]
2JLZX-ray2.20A/B1646-2092[»]
2WHXX-ray2.20A1475-2092[»]
C1393-1406[»]
2WZQX-ray2.80A1475-2092[»]
C1393-1410[»]
3UYPX-ray2.00B575-679[»]
ProteinModelPortaliQ2YHF0
SMRiQ2YHF0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2YHF0

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1475 – 1652Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1654 – 1810Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1820 – 1987Helicase C-terminalAdd BLAST168
Domaini2489 – 2751mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST263
Domaini3016 – 3166RdRp catalyticPROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 71Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni377 – 390Fusion peptideBy similarityAdd BLAST14
Regioni1397 – 1436Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1658 – 1661Important for RNA-bindingBy similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1758 – 1761DEAH boxPROSITE-ProRule annotation4
Motifi2564 – 2567SUMO-interacting motifBy similarity4

Domaini

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.By similarity

Sequence similaritiesi

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG090000PI

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 3 hits
3.30.387.10, 2 hits
3.30.67.10, 4 hits
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR000208 RNA-dir_pol_flavivirus
IPR007094 RNA-dir_pol_PSvirus
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF01003 Flavi_capsid, 1 hit
PF07652 Flavi_DEAD, 1 hit
PF02832 Flavi_glycop_C, 1 hit
PF00869 Flavi_glycoprot, 1 hit
PF01004 Flavi_M, 1 hit
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 1 hit
PF01002 Flavi_NS2B, 1 hit
PF01350 Flavi_NS4A, 1 hit
PF01349 Flavi_NS4B, 1 hit
PF00972 Flavi_NS5, 1 hit
PF01570 Flavi_propep, 1 hit
PF01728 FtsJ, 1 hit
PF00949 Peptidase_S7, 1 hit
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF101257 SSF101257, 1 hit
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit
TIGRFAMsiTIGR04240 flavi_E_stem, 1 hit
PROSITEiView protein in PROSITE
PS51527 FLAVIVIRUS_NS2B, 1 hit
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2YHF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQRKKVARP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI
60 70 80 90 100
TFLRVLSIPP TAGILKRWGQ LKKNKAIKIL TGFRKEIGRM LNILNGRKRS
110 120 130 140 150
TITLLCLIPT VMAFHLSTRD GEPLMIVAKH ERGRPLLFKT TEGINKCTLI
160 170 180 190 200
AMDLGEMCED TVTYKCPLLV NTEPEDIDCW CNLTSAWVMY GTCTQSGERR
210 220 230 240 250
REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI LRNPGFALLA
260 270 280 290 300
GFMAYMIGQT GIQRTVFFIL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV
310 320 330 340 350
DLVLEHGGCV TTMAQGKPTL DFELIKTTAK EVALLRTYCI EASISNITTA
360 370 380 390 400
TRCPTQGEPY LKEEQDQQYI CRRDMVDRGW GNGCGLFGKG GVVTCAKFSC
410 420 430 440 450
SGKITGNLVQ IENLEYTVVV TVHNGDTHAV GNDTSNHGVT ATITPRSPSV
460 470 480 490 500
EVKLPDYGEL TLDCEPRSGI DFNEMILMKM KTKTWLVHKQ WFLDLPLPWT
510 520 530 540 550
AGADTLEVHW NHKERMVTFK VPHAKRQDVT VLGSQEGAMH SALAGATEVD
560 570 580 590 600
SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV
610 620 630 640 650
VKVKYEGTGA PCKVPIEIRD VNKEKVVGRI ISSTPFAENT NSVTNIELEP
660 670 680 690 700
PFGDSYIVIG VGDSALTLHW FRKGSSIGKM FESTYRGAKR MAILGETAWD
710 720 730 740 750
FGSVGGLLTS LGKAVHQVFG SVYTTMFGGV SWMVRILIGL LVLWIGTNSR
760 770 780 790 800
NTSMAMSCIA VGGITLFLGF TVHADMGCAV SWSGKELKCG SGIFVIDNVH
810 820 830 840 850
TWTEQYKFQP ESPARLASAI LNAHKDGVCG IRSTTRLENV MWKQITNELN
860 870 880 890 900
YVLWEGGHDL TVVAGDVKGV LSKGKRALAP PVNDLKYSWK TWGKAKIFTP
910 920 930 940 950
ETRNSTFLVD GPDTSECPNE RRAWNFLEVE DYGFGMFTTN IWMKFREGSS
960 970 980 990 1000
EVCDHRLMSA AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP
1010 1020 1030 1040 1050
KTHTLWSNGV LESQMLIPKA YAGPISQHNY RQGYATQTVG PWHLGKLEID
1060 1070 1080 1090 1100
FGECPGTTVT IQEDCDHRGP SLRTTTASGK LVTQWCCRSC TMPPLRFLGE
1110 1120 1130 1140 1150
DGCWYGMEIR PLNEKEENMV KSQVSAGQGT SETFSMGLLC LTLFVEECLR
1160 1170 1180 1190 1200
RRVTRKHMIL VVVTTLCAII LGGLTWMDLL RALIMLGDTM SGRMGGQIHL
1210 1220 1230 1240 1250
AIMAVFKMSP GYVLGIFLRK LTSRETALMV IGMAMTTVLS IPHDLMEFID
1260 1270 1280 1290 1300
GISLGLILLK MVTHFDNTQV GTLALSLTFI KSTMPLVMAW RTIMAVLFVV
1310 1320 1330 1340 1350
TLIPLCRTSC LQKQSHWVEI TALILGAQAL PVYLMTLMKG ASKRSWPLNE
1360 1370 1380 1390 1400
GIMAVGLVSL LGSALLKNDV PLAGPMVAGG LLLAAYVMSG SSADLSLEKA
1410 1420 1430 1440 1450
ANVQWDEMAD ITGSSPIIEV KQDEDGSFSI RDVEETNMIT LLVKLALITV
1460 1470 1480 1490 1500
SGLYPLAIPV TMTLWYMWQV KTQRSGALWD VPSPAAAQKA TLTEGVYRIM
1510 1520 1530 1540 1550
QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHESGRLE PSWADVRNDM
1560 1570 1580 1590 1600
ISYGGGWRLG DKWDKEEDVQ VLAIEPGKNP KHVQTKPGLF KTLTGEIGAV
1610 1620 1630 1640 1650
TLDFKPGTSG SPIINRKGKV IGLYGNGVVT KSGDYVSAIT QAERIGEPDY
1660 1670 1680 1690 1700
EVDEDIFRKK RLTIMDLHPG AGKTKRILPS IVREALKRRL RTLILAPTRV
1710 1720 1730 1740 1750
VAAEMEEALR GLPIRYQTPA VKSEHTGREI VDLMCHATFT TRLLSSTRVP
1760 1770 1780 1790 1800
NYNLIVMDEA HFTDPSSVAA RGYISTRVEM GEAAAIFMTA TPPGTTDPFP
1810 1820 1830 1840 1850
QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR
1860 1870 1880 1890 1900
KSGKKVIQLS RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR
1910 1920 1930 1940 1950
RCLKPVILTD GPERVILAGP IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG
1960 1970 1980 1990 2000
DPLRNDEDHA HWTEAKMLLD NIYTPEGIIP TLFGPEREKT QAIDGEFRLR
2010 2020 2030 2040 2050
GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG ERNNQILEEN
2060 2070 2080 2090 2100
MEVEIWTREG EKKKLRPKWL DARVYADPMA LKDFKEFASG RKSITLDILT
2110 2120 2130 2140 2150
EIASLPTYLS SRAKLALDNI VMLHTTERGG KAYQHALNEL PESLETLMLV
2160 2170 2180 2190 2200
ALLGAMTAGI FLFFMQGKGI GKLSMGLIAI AVASGLLWVA EIQPQWIAAS
2210 2220 2230 2240 2250
IILEFFLMVL LVPEPEKQRT PQDNQLIYVI LTILTIIALV AANEMGLIEK
2260 2270 2280 2290 2300
TKTDFGFYQA KTETTILDVD LRPASAWTLY AVATTILTPM LRHTIENTSA
2310 2320 2330 2340 2350
NLSLAAIANQ AAVLMGLGKG WPLHRMDLGV PLLAMGCYSQ VNPTTLTASL
2360 2370 2380 2390 2400
VMLLVHYAII GPGLQAKATR EAQKRTAAGI MKNPTVDGIT VIDLEPISYD
2410 2420 2430 2440 2450
PKFEKQLGQV MLLVLCAGQL LLMRTTWAFC EVLTLATGPI LTLWEGNPGR
2460 2470 2480 2490 2500
FWNTTIAVST ANIFRGSYLA GAGLAFSLIK NAQTPRRGTG TTGETLGEKW
2510 2520 2530 2540 2550
KRQLNSLDRK EFEEYKRSGI LEVDRTEAKS ALKDGSKIKY AVSRGTSKIR
2560 2570 2580 2590 2600
WIVERGMVKP KGKVVDLGCG RGGWSYYMAT LKNVTEVKGY TKGGPGHEEP
2610 2620 2630 2640 2650
IPMATYGWNL VKLHSGVDVF YKPTEQVDTL LCDIGESSSN PTIEEGRTLR
2660 2670 2680 2690 2700
VLKMVEPWLS SKPEFCIKVL NPYMPTVIEE LEKLQRKHGG SLVRCPLSRN
2710 2720 2730 2740 2750
STHEMYWVSG VSGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDADLGAGTR
2760 2770 2780 2790 2800
SVSTETEKPD MTIIGRRLQR LQEEHKETWH YDHENPYRTW AYHGSYEAPS
2810 2820 2830 2840 2850
TGSASSMVNG VVKLLTKPWD VVPMVTQLAM TDTTPFGQQR VFKEKVDTRT
2860 2870 2880 2890 2900
PQPKPGTRVV MTTTANWLWA LLGRKKNPRL CTREEFISKV RSNAAIGAVF
2910 2920 2930 2940 2950
QEEQGWTSAS EAVNDSRFWE LVDKERALHQ EGKCESCVYN MMGKREKKLG
2960 2970 2980 2990 3000
EFGRAKGSRA IWYMWLGARF LEFEALGFLN EDHWFGRENS WSGVEGEGLH
3010 3020 3030 3040 3050
RLGYILEDID KKDGDLIYAD DTAGWDTRIT EDDLLNEELI TEQMAPHHKI
3060 3070 3080 3090 3100
LAKAIFKLTY QNKVVKVLRP TPKGAVMDII SRKDQRGSGQ VGTYGLNTFT
3110 3120 3130 3140 3150
NMEVQLIRQM EAEGVITRDD MHNPKGLKER VEKWLKECGV DRLKRMAISG
3160 3170 3180 3190 3200
DDCVVKPLDE RFSTSLLFLN DMGKVRKDIP QWEPSKGWKN WQEVPFCSHH
3210 3220 3230 3240 3250
FHKIFMKDGR SLVVPCRNQD ELIGRARISQ GAGWSLRETA CLGKAYAQMW
3260 3270 3280 3290 3300
SLMYFHRRDL RLASMAICSA VPTEWFPTSR TTWSIHAHHQ WMTTEDMLKV
3310 3320 3330 3340 3350
WNRVWIEDNP NMIDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN
3360 3370 3380
IQTAITQVRN LIGKEEYVDY MPVMKRYSAH FESEGVL
Length:3,387
Mass (Da):378,438
Last modified:December 20, 2005 - v1
Checksum:i1FEDC2D663A0F945
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY618990 Genomic RNA Translation: AAU89377.1

Similar proteinsi

Entry informationi

Entry nameiPOLG_DEN4T
AccessioniPrimary (citable) accession number: Q2YHF0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 20, 2005
Last modified: May 23, 2018
This is version 111 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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