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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 4 (strain Dominica/814669/1981) (DENV-4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein C: Plays a role in virus budding by binding to membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration in host cytoplasm after hemifusion induced by surface proteins. Can migrate tot cell nucleus where it modulates host functions.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. Presumably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Small envelope protein M: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M extodomain. May display a viroporin activity.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 particule is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.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. May plays a role in viral genome replication. Assist membrane bending and envelopment of genomic RNA at the endoplasmic reticulum. Excreted as a hexameric lipoparticle that plays a role against host immune responce.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
Non-structural protein 2B: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane-destabilizing activity and form viroporins (By similarity).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: Induces host endoplasmic regulate the ATPase activity of the NS3 helicase.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: 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 (-) 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 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'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

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
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
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
Sitei2633Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2634S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2637mRNA capPROSITE-ProRule annotation1
Sitei2668Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2699mRNA capPROSITE-ProRule annotation1
Binding sitei2701mRNA capPROSITE-ProRule annotation1
Sitei2704Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2706S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation 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 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

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 14 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Non-structural protein 2A-alpha
Short name:
NS2A-alpha
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Alternative name(s):
Non-structural protein 5
OrganismiDengue virus type 4 (strain Dominica/814669/1981) (DENV-4)
Taxonomic identifieri408871 [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
  • UP000000274 Componenti: Genome

Subcellular locationi

Protein C :
  • Virion By similarity
  • Host nucleus By similarity
Peptide pr :
  • Secreted By similarity
Small envelope protein M :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotationBy similarity; Multi-pass membrane protein By similarity
Envelope protein E :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotationBy similarity; Multi-pass membrane protein By similarity
Non-structural protein 1 :
  • Secreted By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Lumenal side By similarity
Non-structural protein 2A-alpha :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
Non-structural protein 2A :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
Serine protease subunit NS2B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotationBy similarity
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 NS3 protease.PROSITE-ProRule annotation
Non-structural protein 4A :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.By similarity
Non-structural protein 4B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Host nucleus By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.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
Intramembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 751ExtracellularSequence analysis5
Intramembranei752 – 772HelicalSequence analysisAdd BLAST21
Topological domaini773 – 1156ExtracellularSequence analysisAdd BLAST384
Transmembranei1157 – 1177HelicalSequence analysisAdd BLAST21
Topological domaini1178 – 1197CytoplasmicSequence analysisAdd BLAST20
Transmembranei1198 – 1218HelicalSequence analysisAdd BLAST21
Topological domaini1219 – 1244LumenalSequence analysisAdd BLAST26
Transmembranei1245 – 1265HelicalSequence analysisAdd BLAST21
Topological domaini1266 – 1285CytoplasmicSequence analysisAdd BLAST20
Transmembranei1286 – 1306HelicalSequence analysisAdd BLAST21
Topological domaini1307 – 1316LumenalSequence analysis10
Transmembranei1317 – 1337HelicalSequence analysisAdd BLAST21
Topological domaini1338 – 1345CytoplasmicSequence analysis8
Transmembranei1346 – 1366HelicalSequence analysisAdd BLAST21
Topological domaini1367 – 1369LumenalSequence analysis3
Transmembranei1370 – 1390HelicalSequence analysisAdd BLAST21
Topological domaini1391 – 1437CytoplasmicSequence analysisAdd BLAST47
Intramembranei1438 – 1458HelicalSequence analysisAdd 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 – 2273LumenalSequence analysisAdd BLAST27
Intramembranei2274 – 2291HelicalSequence analysisAdd BLAST18
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

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004052261 – 3386Genome polyproteinAdd BLAST3386
ChainiPRO_00000380001 – 99Protein CBy similarityAdd BLAST99
PropeptideiPRO_0000038001100 – 113ER anchor for the protein C, removed in mature form by serine protease NS3By similarityAdd BLAST14
ChainiPRO_0000308297114 – 279prMBy similarityAdd BLAST166
ChainiPRO_0000308298114 – 204Peptide prBy similarityAdd BLAST91
ChainiPRO_0000038002205 – 279Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000038003280 – 774Envelope protein EBy similarityAdd BLAST495
ChainiPRO_0000038004775 – 1126Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000380051127 – 1344Non-structural protein 2ABy similarityAdd BLAST218
ChainiPRO_00004379911127 – 1313Non-structural protein 2A-alphaBy similarityAdd BLAST187
ChainiPRO_00003082991127 – ?Non-structural protein 2A-alphaBy similarity
ChainiPRO_00000380061345 – 1474Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00000380071475 – 2092Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00000380082093 – 2219Non-structural protein 4ABy similarityAdd BLAST127
PeptideiPRO_00003083002220 – 2242Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000380092243 – 2487Non-structural protein 4BBy similarityAdd BLAST245
ChainiPRO_00000380102488 – 3387RNA-directed RNA polymerase NS5By similarityAdd BLAST900

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi182N-linked (GlcNAc...); by host1
Disulfide bondi282 ↔ 309By similarity
Disulfide bondi339 ↔ 400By similarity
Glycosylationi346N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi353 ↔ 384By similarity
Disulfide bondi371 ↔ 395By similarity
Glycosylationi432N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi464 ↔ 564By similarity
Disulfide bondi581 ↔ 612By similarity
Disulfide bondi778 ↔ 789By similarity
Disulfide bondi829 ↔ 917By similarity
Glycosylationi904N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi953 ↔ 997By similarity
Glycosylationi981N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi1054 ↔ 1103By similarity
Disulfide bondi1065 ↔ 1087By similarity
Disulfide bondi1086 ↔ 1090By similarity
Glycosylationi2297N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2301N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2453N-linked (GlcNAc...); by hostSequence analysis1

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, wereas cleavages in the cytoplasmic side are performed by the Serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Non-structural protein 2A-alpha: A C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3.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
Non-structural protein 1: 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: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei99 – 100Cleavage; by viral protease NS3Sequence analysis2
Sitei113 – 114Cleavage; by host signal peptidaseBy similarity2
Sitei204 – 205Cleavage; by host furinSequence analysis2
Sitei279 – 280Cleavage; by host signal peptidaseSequence analysis2
Sitei774 – 775Cleavage; by host signal peptidaseSequence analysis2
Sitei1126 – 1127Cleavage; by hostBy similarity2
Sitei1344 – 1345Cleavage; by viral protease NS3Sequence analysis2
Sitei1474 – 1475Cleavage; by autolysisSequence analysis2
Sitei2092 – 2093Cleavage; by autolysisSequence analysis2
Sitei2219 – 2220Cleavage; by viral protease NS3Sequence analysis2
Sitei2242 – 2243Cleavage; by host signal peptidaseSequence analysis2
Sitei2487 – 2488Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

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

Proteomic databases

PRIDEiP09866.

Interactioni

Subunit structurei

Protein C: Homodimerizes. Protein prM: Forms homodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Forms homodimers with envelope protein E in the endoplasmic reticulum and Golgi. Non-structural protein 1: Forms homodimers as well as homohexamers. NS1 may interact with NS4A. Non-structural protein 2B: Forms a heterodimer with Non-structural protein 3. May form homooligomers. Non-structural protein 3: Forms a heterodimer with Non-structural protein 2B. Interacts with Non-structural protein 4B. Interacts with unphosphorylated Non-structural protein 5; this interaction stimulates Non-structural protein 5 guanylyltransferase activity. Non-structural protein 4B: Interacts with non-structural protein 3. Non-structural protein 5: 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

Protein-protein interaction databases

MINTiMINT-8373716.

Structurei

Secondary structure

13387
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi283 – 286Combined sources4
Turni292 – 294Combined sources3
Beta strandi295 – 297Combined sources3
Beta strandi300 – 306Combined sources7
Beta strandi309 – 314Combined sources6
Beta strandi317 – 327Combined sources11
Beta strandi333 – 351Combined sources19
Helixi362 – 364Combined sources3
Beta strandi369 – 379Combined sources11
Turni380 – 383Combined sources4
Beta strandi388 – 408Combined sources21
Beta strandi411 – 413Combined sources3
Beta strandi416 – 422Combined sources7
Beta strandi439 – 443Combined sources5
Beta strandi449 – 454Combined sources6
Turni455 – 457Combined sources3
Beta strandi458 – 465Combined sources8
Helixi472 – 474Combined sources3
Beta strandi475 – 480Combined sources6
Beta strandi483 – 488Combined sources6
Helixi489 – 493Combined sources5
Helixi513 – 515Combined sources3
Beta strandi517 – 519Combined sources3
Beta strandi529 – 531Combined sources3
Helixi536 – 542Combined sources7
Beta strandi544 – 546Combined sources3
Beta strandi548 – 550Combined sources3
Beta strandi552 – 554Combined sources3
Beta strandi560 – 567Combined sources8
Beta strandi570 – 572Combined sources3
Turni574 – 577Combined sources4
Beta strandi585 – 593Combined sources9
Beta strandi595 – 597Combined sources3
Beta strandi599 – 605Combined sources7
Beta strandi607 – 609Combined sources3
Beta strandi611 – 613Combined sources3
Beta strandi616 – 619Combined sources4
Beta strandi621 – 623Combined sources3
Beta strandi632 – 634Combined sources3
Beta strandi636 – 639Combined sources4
Beta strandi643 – 648Combined sources6
Beta strandi652 – 661Combined sources10
Helixi662 – 664Combined sources3
Beta strandi666 – 672Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H0PNMR-A568-679[»]
3UAJX-ray3.23A/B280-674[»]
3UC0X-ray2.71A/B280-329[»]
A/B414-469[»]
A/B560-577[»]
3WE1X-ray2.28A/B575-679[»]
4X42X-ray2.78A/B/C/D/E/F575-679[»]
5B1CX-ray2.00A/B/C575-679[»]
ProteinModelPortaliP09866.
SMRiP09866.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09866.

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
Regioni32 – 73Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST42
Regioni1397 – 1436Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1758 – 1761DEAH box4

Domaini

Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals.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
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.Curated
Contains 1 mRNA cap 0-1 NS5-type MT domain.PROSITE-ProRule annotation
Contains 1 peptidase S7 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR027287. Flavi_E_Ig-like.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
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.
[Graphical view]
PfamiPF01003. 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.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. 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.
PROSITEiPS51527. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09866-1 [UniParc]FASTAAdd to basket

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MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI
60 70 80 90 100
TFLRVLSIPP TAGILKRWGQ LKKNKAIKIL IGFRKEIGRM LNILNGRKRS
110 120 130 140 150
TITLLCLIPT VMAFSLSTRD GEPLMIVAKH ERGRPLLFKT TEGINKCTLI
160 170 180 190 200
AMDLGEMCED TVTYKCPLLV NTEPEDIDCW CNLTSTWVMY GTCTQSGERR
210 220 230 240 250
REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI LRNPGFALLA
260 270 280 290 300
GFMAYMIGQT GIQRTVFFVL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV
310 320 330 340 350
DLVLEHGGCV TTMAQGKPTL DFELTKTTAK EVALLRTYCI EASISNITTA
360 370 380 390 400
TRCPTQGEPY LKEEQDQQYI CRRDVVDRGW GNGCGLFGKG GVVTCAKFSC
410 420 430 440 450
SGKITGNLVQ IENLEYTVVV TVHNGDTHAV GNDTSNHGVT AMITPRSPSV
460 470 480 490 500
EVKLPDYGEL TLDCEPRSGI DFNEMILMKM KKKTWLVHKQ WFLDLPLPWT
510 520 530 540 550
AGADTSEVHW NYKERMVTFK VPHAKRQDVT VLGSQEGAMH SALAGATEVD
560 570 580 590 600
SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV
610 620 630 640 650
VKVKYEGAGA PCKVPIEIRD VNKEKVVGRI ISSTPLAENT NSVTNIELEP
660 670 680 690 700
PFGDSYIVIG VGNSALTLHW FRKGSSIGKM FESTYRGAKR MAILGETAWD
710 720 730 740 750
FGSVGGLFTS LGKAVHQVFG SVYTTMFGGV SWMIRILIGF LVLWIGTNSR
760 770 780 790 800
NTSMAMTCIA VGGITLFLGF TVQADMGCVA SWSGKELKCG SGIFVVDNVH
810 820 830 840 850
TWTEQYKFQP ESPARLASAI LNAHKDGVCG IRSTTRLENV MWKQITNELN
860 870 880 890 900
YVLWEGGHDL TVVAGDVKGV LTKGKRALTP PVSDLKYSWK TWGKAKIFTP
910 920 930 940 950
EARNSTFLID GPDTSECPNE RRAWNSLEVE DYGFGMFTTN IWMKFREGSS
960 970 980 990 1000
EVCDHRLMSA AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP
1010 1020 1030 1040 1050
KTHTLWSNGV LESQMLIPKS YAGPFSQHNY RQGYATQTVG PWHLGKLEID
1060 1070 1080 1090 1100
FGECPGTTVT IQEDCDHRGP SLRTTTASGK LVTQWCCRSC TMPPLRFLGE
1110 1120 1130 1140 1150
DGCWYGMEIR PLSEKEENMV KSQVTAGQGT SETFSMGLLC LTLFVEECLR
1160 1170 1180 1190 1200
RRVTRKHMIL VVVITLCAII LGGLTWMDLL RALIMLGDTM SGRIGGQIHL
1210 1220 1230 1240 1250
AIMAVFKMSP GYVLGVFLRK LTSRETALMV IGMAMTTVLS IPHDLMELID
1260 1270 1280 1290 1300
GISLGLILLK IVTQFDNTQV GTLALSLTFI RSTMPLVMAW RTIMAVLFVV
1310 1320 1330 1340 1350
TLIPLCRTSC LQKQSHWVEI TALILGAQAL PVYLMTLMKG ASRRSWPLNE
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 VPSPAATKKA ALSEGVYRIM
1510 1520 1530 1540 1550
QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHETGRLE 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 TPPGATDPFP
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
RCLKPVILPD GPERVILAGP IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG
1960 1970 1980 1990 2000
DPLKNDEDHA HWTEAKMLLD NIYTPEGIIP TLFGPEREKT QAIDGEFRLR
2010 2020 2030 2040 2050
GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG ERNNQILEEN
2060 2070 2080 2090 2100
MEVEIWTREG EKKKLRPRWL DARVYADPMA LKDFKEFASG RKSITLDILT
2110 2120 2130 2140 2150
EIASLPTYLS SRAKLALDNI VMLHTTERGG RAYQHALNEL PESLETLMLV
2160 2170 2180 2190 2200
ALLGAMTAGI FLFFMQGKGI GKLSMGLITI AVASGLLWVA EIQPQWIAAS
2210 2220 2230 2240 2250
IILEFFLMVL LIPEPEKQRT PQDNQLIYVI LTILTIIGLI AANEMGLIEK
2260 2270 2280 2290 2300
TKTDFGFYQV 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 ALKDGSKIKH AVSRGSSKIR
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 NLVRCPLSRN
2710 2720 2730 2740 2750
STHEMYWVSG ASGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDVDLGAGTR
2760 2770 2780 2790 2800
SVSTETEKPD MTIIGRRLQR LQEEHKETWH YDQENPYRTW AYHGSYEAPS
2810 2820 2830 2840 2850
TGSASSMVNG VVKLLTKPWD VIPMVTQLAM TDTTPFGQQR VFKEKVDTRT
2860 2870 2880 2890 2900
PQPKPGTRMV MTTTANWLWA LLGKKKNPRL 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
RLGYILEEID KKDGDLMYAD DTAGWDTRIT EDDLQNEELI TEQMAPHHKI
3060 3070 3080 3090 3100
LAKAIFKLTY QNKVVKVLRP TPRGAVMDII SRKDQRGSGQ VGTYGLNTFT
3110 3120 3130 3140 3150
NMEVQLIRQM EAEGVITQDD MQNPKGLKER VEKWLKECGV DRLKRMAISG
3160 3170 3180 3190 3200
DDCVVKPLDE RFGTSLLFLN 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 NMTDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN
3360 3370 3380
IHTAITQVRN LIGKEEYVDY MPVMKRYSAP SESEGVL
Length:3,387
Mass (Da):378,385
Last modified:January 16, 2004 - v2
Checksum:i0CE81B6E7DEFDB5E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti780A → V in AAG45436 (Ref. 2) Curated1
Sequence conflicti780A → V in AAK01233 (Ref. 2) Curated1
Sequence conflicti1418I → V in AAG45435 (Ref. 2) Curated1
Sequence conflicti1909P → T in AAK01233 (Ref. 2) Curated1
Sequence conflicti2032K → E in AAG45435 (Ref. 2) Curated1
Sequence conflicti2351V → A in AAG45436 (Ref. 2) Curated1
Sequence conflicti2354L → F in AAG45437 (Ref. 2) Curated1
Sequence conflicti2510K → R in AAK01233 (Ref. 2) Curated1
Sequence conflicti2736K → R in AAG45436 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14931 Genomic RNA. Translation: AAA42964.2.
AF326825 Genomic RNA. Translation: AAG45435.1.
AF326826 Genomic RNA. Translation: AAG45436.1.
AF326827 Genomic RNA. Translation: AAG45437.1.
AF326573 Genomic RNA. Translation: AAK01233.1.
RefSeqiNP_073286.1. NC_002640.1.

Genome annotation databases

GeneIDi5075729.
KEGGivg:5075729.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14931 Genomic RNA. Translation: AAA42964.2.
AF326825 Genomic RNA. Translation: AAG45435.1.
AF326826 Genomic RNA. Translation: AAG45436.1.
AF326827 Genomic RNA. Translation: AAG45437.1.
AF326573 Genomic RNA. Translation: AAK01233.1.
RefSeqiNP_073286.1. NC_002640.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H0PNMR-A568-679[»]
3UAJX-ray3.23A/B280-674[»]
3UC0X-ray2.71A/B280-329[»]
A/B414-469[»]
A/B560-577[»]
3WE1X-ray2.28A/B575-679[»]
4X42X-ray2.78A/B/C/D/E/F575-679[»]
5B1CX-ray2.00A/B/C575-679[»]
ProteinModelPortaliP09866.
SMRiP09866.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8373716.

Proteomic databases

PRIDEiP09866.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5075729.
KEGGivg:5075729.

Miscellaneous databases

EvolutionaryTraceiP09866.
PROiP09866.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR027287. Flavi_E_Ig-like.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
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.
[Graphical view]
PfamiPF01003. 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.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. 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.
PROSITEiPS51527. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_DEN4D
AccessioniPrimary (citable) accession number: P09866
Secondary accession number(s): Q88661
, Q88662, Q88663, Q88664, Q88665, Q88666, Q88667, Q88668, Q88669, Q88670, Q88671, Q99BK4, Q9DKQ5, Q9DKQ6, Q9DKQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 16, 2004
Last modified: November 30, 2016
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.