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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969) (DENV-2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA.By similarity
prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated.By similarity
Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes.By similarity
Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome.By similarity
Non-structural protein 2A may be involved viral RNA replication and capsid assembly.Curated
Non-structural protein 2B is a required cofactor for the serine protease function of NS3.PROSITE-ProRule annotation
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 (By similarity).PROSITE-ProRule annotation
Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also 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).PROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1526 – 15261Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1550 – 15501Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1610 – 16101Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Binding sitei2502 – 25021mRNA capPROSITE-ProRule annotation
Binding sitei2505 – 25051mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2506 – 25061mRNA capPROSITE-ProRule annotation
Binding sitei2508 – 25081mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2513 – 25131mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2517 – 25171mRNA capPROSITE-ProRule annotation
Binding sitei2544 – 25441S-adenosyl-L-methionine
Sitei2549 – 25491Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2574 – 25741S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei2575 – 25751S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei2592 – 25921S-adenosyl-L-methionine
Binding sitei2593 – 25931S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei2619 – 26191S-adenosyl-L-methionine
Binding sitei2620 – 26201S-adenosyl-L-methionine; via carbonyl oxygen
Sitei2634 – 26341Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2635 – 26351S-adenosyl-L-methionine binding
Binding sitei2638 – 26381mRNA capPROSITE-ProRule annotation
Sitei2669 – 26691Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2700 – 27001mRNA capPROSITE-ProRule annotation
Binding sitei2702 – 27021mRNA capPROSITE-ProRule annotation
Sitei2705 – 27051Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2707 – 27071S-adenosyl-L-methionine

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1668 – 16758ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase

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, mRNA capping, mRNA processing, Transcription, Transcription regulation, 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

Enzyme and pathway databases

BRENDAi2.1.1.57. 1867.

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 2 (strain Puerto Rico/PR159-S1/1969) (DENV-2)
Taxonomic identifieri11066 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostiAedimorphus [TaxID: 53540]
Diceromyia [TaxID: 53539]
Erythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
Stegomyia [TaxID: 53541]
Proteomesi
  • UP000007197 Componenti: Genome

Subcellular locationi

Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A-alpha :
Non-structural protein 2A :
Serine protease subunit NS2B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
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 :
Non-structural protein 4B :
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 101101CytoplasmicSequence analysisAdd
BLAST
Transmembranei102 – 12221HelicalSequence analysisAdd
BLAST
Topological domaini123 – 238116ExtracellularSequence analysisAdd
BLAST
Transmembranei239 – 25921HelicalSequence analysisAdd
BLAST
Topological domaini260 – 2656CytoplasmicSequence analysis
Transmembranei266 – 28015HelicalSequence analysisAdd
BLAST
Topological domaini281 – 725445ExtracellularSequence analysisAdd
BLAST
Intramembranei726 – 74621HelicalSequence analysisAdd
BLAST
Topological domaini747 – 7526ExtracellularSequence analysis
Intramembranei753 – 77321HelicalSequence analysisAdd
BLAST
Topological domaini774 – 1124351ExtracellularSequence analysisAdd
BLAST
Transmembranei1125 – 114521HelicalSequence analysisAdd
BLAST
Topological domaini1146 – 115611CytoplasmicSequence analysisAdd
BLAST
Transmembranei1157 – 117721HelicalSequence analysisAdd
BLAST
Topological domaini1178 – 11847LumenalSequence analysis
Transmembranei1185 – 120521HelicalSequence analysisAdd
BLAST
Topological domaini1206 – 127166CytoplasmicSequence analysisAdd
BLAST
Transmembranei1272 – 129221HelicalSequence analysisAdd
BLAST
Topological domaini1293 – 131725LumenalSequence analysisAdd
BLAST
Transmembranei1318 – 133821HelicalSequence analysisAdd
BLAST
Topological domaini1339 – 13468CytoplasmicSequence analysis
Transmembranei1347 – 136721HelicalSequence analysisAdd
BLAST
Topological domaini1368 – 13703LumenalSequence analysis
Transmembranei1371 – 139121HelicalSequence analysisAdd
BLAST
Topological domaini1392 – 144756CytoplasmicSequence analysisAdd
BLAST
Intramembranei1448 – 146821HelicalSequence analysisAdd
BLAST
Topological domaini1469 – 2144676CytoplasmicSequence analysisAdd
BLAST
Transmembranei2145 – 216521HelicalSequence analysisAdd
BLAST
Topological domaini2166 – 21672LumenalSequence analysis
Intramembranei2168 – 218821HelicalSequence analysisAdd
BLAST
Topological domaini2189 – 21891LumenalSequence analysis
Transmembranei2190 – 221021HelicalSequence analysisAdd
BLAST
Topological domaini2211 – 222515CytoplasmicSequence analysisAdd
BLAST
Transmembranei2226 – 224621Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2247 – 227428LumenalSequence analysisAdd
BLAST
Intramembranei2275 – 229218HelicalSequence analysisAdd
BLAST
Topological domaini2293 – 231321LumenalSequence analysisAdd
BLAST
Intramembranei2314 – 233421HelicalSequence analysisAdd
BLAST
Topological domaini2335 – 234410LumenalSequence analysis
Transmembranei2345 – 236521HelicalSequence analysisAdd
BLAST
Topological domaini2366 – 241045CytoplasmicSequence analysisAdd
BLAST
Transmembranei2411 – 243121HelicalSequence analysisAdd
BLAST
Topological domaini2432 – 245625LumenalSequence analysisAdd
BLAST
Transmembranei2457 – 247721HelicalSequence analysisAdd
BLAST
Topological domaini2478 – 3388911CytoplasmicSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 33883388Genome polyproteinPRO_0000405217Add
BLAST
Chaini1 – 100100Capsid protein CBy similarityPRO_0000037969Add
BLAST
Propeptidei101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000037970Add
BLAST
Chaini115 – 280166prMBy similarityPRO_0000308286Add
BLAST
Chaini115 – 20591Peptide prBy similarityPRO_0000308287Add
BLAST
Chaini206 – 28075Small envelope protein MBy similarityPRO_0000037971Add
BLAST
Chaini281 – 775495Envelope protein EBy similarityPRO_0000037972Add
BLAST
Chaini776 – 1127352Non-structural protein 1By similarityPRO_0000037973Add
BLAST
Chaini1128 – 1345218Non-structural protein 2ABy similarityPRO_0000037974Add
BLAST
Chaini1128 – 1315188Non-structural protein 2A-alphaBy similarityPRO_0000308288Add
BLAST
Chaini1346 – 1475130Serine protease subunit NS2BBy similarityPRO_0000037975Add
BLAST
Chaini1476 – 2090615Serine protease NS3By similarityPRO_0000037976Add
BLAST
Chaini2091 – 2217127Non-structural protein 4ABy similarityPRO_0000037977Add
BLAST
Peptidei2218 – 224023Peptide 2kBy similarityPRO_0000308289Add
BLAST
Chaini2241 – 2488248Non-structural protein 4BBy similarityPRO_0000037978Add
BLAST
Chaini2489 – 3388900RNA-directed RNA polymerase NS5By similarityPRO_0000037979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi283 ↔ 3101 Publication
Disulfide bondi340 ↔ 4011 Publication
Glycosylationi347 – 3471N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi354 ↔ 3851 Publication
Disulfide bondi372 ↔ 3961 Publication
Glycosylationi433 – 4331N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi465 ↔ 5651 Publication
Disulfide bondi582 ↔ 6131 Publication
Glycosylationi905 – 9051N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi982 – 9821N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2298 – 22981N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2302 – 23021N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity
Envelope protein E and non-structural protein 1 are N-glycosylated.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei100 – 1012Cleavage; by viral protease NS3Sequence analysis
Sitei114 – 1152Cleavage; by host signal peptidaseBy similarity
Sitei205 – 2062Cleavage; by host furinSequence analysis
Sitei280 – 2812Cleavage; by host signal peptidaseSequence analysis
Sitei775 – 7762Cleavage; by host signal peptidaseSequence analysis
Sitei1127 – 11282Cleavage; by hostBy similarity
Sitei1345 – 13462Cleavage; by viral protease NS3Sequence analysis
Sitei1475 – 14762Cleavage; by autolysisSequence analysis
Sitei2090 – 20912Cleavage; by autolysisSequence analysis
Sitei2217 – 22182Cleavage; by viral protease NS3Sequence analysis
Sitei2240 – 22412Cleavage; by host signal peptidaseSequence analysis
Sitei2488 – 24892Cleavage; by viral protease NS3Sequence analysis

Keywords - PTMi

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

Interactioni

Subunit structurei

Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity. NS5 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

Structurei

Secondary structure

1
3388
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253Combined sources
Helixi27 – 326Combined sources
Beta strandi34 – 363Combined sources
Helixi45 – 5713Combined sources
Helixi63 – 697Combined sources
Helixi75 – 9521Combined sources
Turni282 – 2854Combined sources
Helixi288 – 2903Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi295 – 30612Combined sources
Beta strandi311 – 3155Combined sources
Beta strandi320 – 33213Combined sources
Beta strandi334 – 35219Combined sources
Helixi363 – 3664Combined sources
Beta strandi370 – 37910Combined sources
Helixi381 – 3833Combined sources
Beta strandi389 – 40921Combined sources
Helixi412 – 4143Combined sources
Beta strandi415 – 42410Combined sources
Turni428 – 4325Combined sources
Beta strandi440 – 4445Combined sources
Beta strandi450 – 4556Combined sources
Turni456 – 4583Combined sources
Beta strandi459 – 4679Combined sources
Turni473 – 4753Combined sources
Beta strandi476 – 4816Combined sources
Beta strandi484 – 4896Combined sources
Helixi490 – 4956Combined sources
Beta strandi500 – 5023Combined sources
Helixi514 – 5163Combined sources
Beta strandi518 – 5203Combined sources
Beta strandi523 – 5264Combined sources
Beta strandi530 – 5323Combined sources
Helixi537 – 5437Combined sources
Turni544 – 5463Combined sources
Beta strandi547 – 5504Combined sources
Beta strandi552 – 5598Combined sources
Beta strandi562 – 57110Combined sources
Beta strandi586 – 5949Combined sources
Beta strandi600 – 6067Combined sources
Beta strandi608 – 6103Combined sources
Beta strandi612 – 6143Combined sources
Beta strandi617 – 6248Combined sources
Beta strandi631 – 6333Combined sources
Beta strandi645 – 6495Combined sources
Beta strandi653 – 6619Combined sources
Beta strandi667 – 6737Combined sources
Helixi2497 – 250711Combined sources
Helixi2510 – 25178Combined sources
Turni2518 – 25203Combined sources
Beta strandi2522 – 25254Combined sources
Helixi2527 – 25359Combined sources
Beta strandi2543 – 25453Combined sources
Helixi2546 – 25549Combined sources
Turni2555 – 25573Combined sources
Beta strandi2563 – 25686Combined sources
Turni2571 – 25733Combined sources
Helixi2574 – 25796Combined sources
Beta strandi2585 – 25917Combined sources
Helixi2609 – 26113Combined sources
Beta strandi2612 – 26154Combined sources
Helixi2620 – 26223Combined sources
Beta strandi2629 – 26335Combined sources
Helixi2642 – 265716Combined sources
Beta strandi2665 – 26717Combined sources
Helixi2676 – 268813Combined sources
Beta strandi2692 – 26943Combined sources
Beta strandi2706 – 27094Combined sources
Helixi2716 – 272914Combined sources
Beta strandi2739 – 27424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9KX-ray2.40A2492-2784[»]
1OANX-ray2.75A/B281-674[»]
1OK8X-ray2.00A281-674[»]
1OKEX-ray2.40A/B281-674[»]
1P58electron microscopy9.50A/B/C281-775[»]
D/E/F206-280[»]
1R6AX-ray2.60A2492-2784[»]
1R6RNMR-A/B1-100[»]
1THDelectron microscopy9.50A/B/C281-675[»]
2P1DX-ray2.90A2492-2784[»]
2P3LX-ray2.20A2492-2784[»]
2P3OX-ray2.76A2492-2784[»]
2P3QX-ray2.75A2492-2784[»]
2P40X-ray2.70A2492-2784[»]
2P41X-ray1.80A2492-2784[»]
3J8Delectron microscopy26.00G/H/I281-674[»]
3ZKOelectron microscopy13.70A/B/C281-775[»]
ProteinModelPortaliP12823.
SMRiP12823. Positions 21-100, 115-195, 281-674, 1394-1440, 1495-2090, 2495-2756, 2762-3371.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12823.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1476 – 1653178Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1655 – 1811157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1821 – 1988168Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2490 – 2752263mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3017 – 3166150RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni1398 – 143740Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1759 – 17624DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi97 – 1004Poly-Arg
Compositional biasi1434 – 14374Poly-Glu
Compositional biasi2145 – 21517Poly-Leu
Compositional biasi2351 – 23544Poly-Leu
Compositional biasi3380 – 33834Poly-Glu

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.PROSITE-ProRule annotation
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

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.
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.
IPR027287. Flavovir_Ig-like.
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.
PS51194. HELICASE_CTER. 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.

P12823-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDQRKKARN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL
60 70 80 90 100
VAFLRFLTIP PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR
110 120 130 140 150
TAGMIIMLIP TVMAFHLTTR NGEPHMIVSR QEKGKSLLFK TKDGTNMCTL
160 170 180 190 200
MAMDLGELCE DTITYKCPFL KQNEPEDIDC WCNSTSTWVT YGTCTTTGEH
210 220 230 240 250
RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW ILRHPGFTIM
260 270 280 290 300
AAILAYTIGT THFQRVLIFI LLTAIAPSMT MRCIGISNRD FVEGVSGGSW
310 320 330 340 350
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT
360 370 380 390 400
DSRCPTQGEP TLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT
410 420 430 440 450
CKKNMEGKIV QPENLEYTVV ITPHSGEEHA VGNDTGKHGK EVKITPQSSI
460 470 480 490 500
TEAELTGYGT VTMECSPRTG LDFNEMVLLQ MKDKAWLVHR QWFLDLPLPW
510 520 530 540 550
LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM HTALTGATEI
560 570 580 590 600
QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI
610 620 630 640 650
VIRVQYEGDG SPCKTPFEIM DLEKRHVLGR LTTVNPIVTE KDSPVNIEAE
660 670 680 690 700
PPFGDSYIII GVEPGQLKLD WFKKGSSIGQ MFETTMRGAK RMAILGDTAW
710 720 730 740 750
DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS
760 770 780 790 800
RSTSLSVSLV LVGIVTLYLG VMVQADSGCV VSWKNKELKC GSGIFVTDNV
810 820 830 840 850
HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN LMWKQITSEL
860 870 880 890 900
NHILSENEVK LTIMTGDIKG IMQVGKRSLR PQPTELRYSW KTWGKAKMLS
910 920 930 940 950
TELHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLRLREKQ
960 970 980 990 1000
DAFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW
1010 1020 1030 1040 1050
PKSHTLWSNG VLESEMVIPK NFAGPVSQHN NRPGYHTQTA GPWHLGKLEM
1060 1070 1080 1090 1100
DFDFCEGTTV VVTEDCGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG
1110 1120 1130 1140 1150
EDGCWYGMEI RPLKEKEENL VSSLVTAGHG QIDNFSLGIL GMALFLEEML
1160 1170 1180 1190 1200
RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT
1210 1220 1230 1240 1250
YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ SSIPETILEL
1260 1270 1280 1290 1300
TDALALGMMV LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA
1310 1320 1330 1340 1350
VVSVSPLFLT SSQQKADWIP LALTIKGLNP TAIFLTTLSR TSKKRSWPLN
1360 1370 1380 1390 1400
EAIMAVGMVS ILASSLLKND TPMTGPLVAG GLLTVCYVLT GRSADLELER
1410 1420 1430 1440 1450
ATDVKWDDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL TILIRTGLLV
1460 1470 1480 1490 1500
ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPVGK AELEDGAYRI
1510 1520 1530 1540 1550
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD
1560 1570 1580 1590 1600
LISYGGGWKL EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FRTNTGTIGA
1610 1620 1630 1640 1650
VSLDFSPGTS GSPIVDKKGK VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN
1660 1670 1680 1690 1700
PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP AIVREAIKRG LRTLILAPTR
1710 1720 1730 1740 1750
VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF TMRLLSPIRV
1760 1770 1780 1790 1800
PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
1810 1820 1830 1840 1850
PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KTGNDIAACL
1860 1870 1880 1890 1900
RKNGKRVIQL SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP
1910 1920 1930 1940 1950
RRCMKPVILT DGEERVILAG PMPVTHSSAA QRRGRIGRNP RNENDQYIYM
1960 1970 1980 1990 2000
GEPLENDEDC AHWKEAKMLL DNINTPEGII PSMFEPEREK VDAIDGEYRL
2010 2020 2030 2040 2050
RGEARKTFVD LMRRGDLPVW LAYKVAAEGI NYADRRWCFD GTRNNQILEE
2060 2070 2080 2090 2100
NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFAAGRK SLTLNLITEM
2110 2120 2130 2140 2150
GRLPTFMTQK ARDALDNLAV LHTAEAGGKA YNHALSELPE TLETLLLLTL
2160 2170 2180 2190 2200
LATVTGGIFL FLMSGRGIGK MTLGMCCIIT ASILLWYAQI QPHWIAASII
2210 2220 2230 2240 2250
LEFFLIVLLI PEPEKQRTPQ DNQLTYVIIA ILTVVAATMA NEMGFLEKTK
2260 2270 2280 2290 2300
KDLGLGNIAT QQPESNILDI DLRPASAWTL YAVATTFITP MLRHSIENSS
2310 2320 2330 2340 2350
VNVSLTAIAN QATVLMGLGK GWPLSKMDIG VPLLAIGCYS QVNPITLTAA
2360 2370 2380 2390 2400
LLLLVAHYAI IGPGLQAKAT REAQKRAAAG IMKNPTVDGI TVIDLDPIPY
2410 2420 2430 2440 2450
DPKFEKQLGQ VMLLVLCVTQ VLMMRTTWAL CEALTLATGP VSTLWEGNPG
2460 2470 2480 2490 2500
RFWNTTIAVS MANIFRGSYL AGAGLLFSIM KNTTSTRRGT GNIGETLGEK
2510 2520 2530 2540 2550
WKSRLNALGK SEFQIYKKSG IQEVDRTLAK EGIKRGETDH HAVSRGSAKL
2560 2570 2580 2590 2600
RWFVERNLVT PEGKVVDLGC GRGGWSYYCG GLKNVREVKG LTKGGPGHEE
2610 2620 2630 2640 2650
PIPMSTYGWN LVRLQSGVDV FFVPPEKCDT LLCDIGESSP NPTVEAGRTL
2660 2670 2680 2690 2700
RVLNLVENWL NNNTQFCVKV LNPYMPSVIE RMETLQRKYG GALVRNPLSR
2710 2720 2730 2740 2750
NSTHEMYWVS NASGNIVSSV NMISRMLINR FTMRHKKATY EPDVDLGSGT
2760 2770 2780 2790 2800
RNIGIESETP NLDIIGKRIE KIKQEHETSW HYDQDHPYKT WAYHGSYETK
2810 2820 2830 2840 2850
QTGSASSMVN GVVRLLTKPW DVVPMVTQMA MTDTTPFGQQ RVFKEKVDTR
2860 2870 2880 2890 2900
TQEPKEGTKK LMKITAEWLW KELGKKKTPR MCTREEFTKK VRSNAALGAI
2910 2920 2930 2940 2950
FTDENKWKSA REAVEDSRFW ELVDKERNLH LEGKCETCVY NMMGKREKKL
2960 2970 2980 2990 3000
GEFGKAKGSR AIWYMWLGAR FLEFEALGFL NEDHWFSREN SLSGVEGEGL
3010 3020 3030 3040 3050
HKLGYILREV SKKEGGAMYA DDTAGWDTRI TIEDLKNEEM ITNHMAGEHK
3060 3070 3080 3090 3100
KLAEAIFKLT YQNKVVRVQR PTPRGTVMDI ISRRDQRGSG QVGTYGLNTF
3110 3120 3130 3140 3150
TNMEAQLIRQ MEGEGIFKSI QHLTASEEIA VQDWLARVGR ERLSRMAISG
3160 3170 3180 3190 3200
DDCVVKPLDD RFARALTALN DMGKVRKDIQ QWEPSRGWND WTQVPFCSHH
3210 3220 3230 3240 3250
FHELIMKDGR TLVVPCRNQD ELIGRARISQ GAGWSLRETA CLGKSYAQMW
3260 3270 3280 3290 3300
SLMYFHRRDL RLAANAICSA VPSHWVPTSR TTWSIHASHE WMTTEDMLTV
3310 3320 3330 3340 3350
WNKVWILENP WMEDKTPVES WEEIPYLGKR EDQWCGSLIG LTSRATWAKN
3360 3370 3380
IQTAINQVRS LIGNEEYTDY MPSMKRFRRE EEEAGVLW
Length:3,388
Mass (Da):379,219
Last modified:October 1, 1989 - v1
Checksum:i79B7C87BE64D2D8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti351 – 3511D → E (PubMed:12759475).Curated
Sequence conflicti615 – 6151T → I (PubMed:12759475).Curated
Sequence conflicti632 – 6321T → I (PubMed:12759475).Curated
Sequence conflicti670 – 6701D → N (PubMed:12759475).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19197 Genomic RNA. Translation: AAA42962.1.
PIRiA29972. GNWVDP.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19197 Genomic RNA. Translation: AAA42962.1.
PIRiA29972. GNWVDP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9KX-ray2.40A2492-2784[»]
1OANX-ray2.75A/B281-674[»]
1OK8X-ray2.00A281-674[»]
1OKEX-ray2.40A/B281-674[»]
1P58electron microscopy9.50A/B/C281-775[»]
D/E/F206-280[»]
1R6AX-ray2.60A2492-2784[»]
1R6RNMR-A/B1-100[»]
1THDelectron microscopy9.50A/B/C281-675[»]
2P1DX-ray2.90A2492-2784[»]
2P3LX-ray2.20A2492-2784[»]
2P3OX-ray2.76A2492-2784[»]
2P3QX-ray2.75A2492-2784[»]
2P40X-ray2.70A2492-2784[»]
2P41X-ray1.80A2492-2784[»]
3J8Delectron microscopy26.00G/H/I281-674[»]
3ZKOelectron microscopy13.70A/B/C281-775[»]
ProteinModelPortaliP12823.
SMRiP12823. Positions 21-100, 115-195, 281-674, 1394-1440, 1495-2090, 2495-2756, 2762-3371.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.1.1.57. 1867.

Miscellaneous databases

EvolutionaryTraceiP12823.
PROiP12823.

Family and domain databases

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.
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.
IPR027287. Flavovir_Ig-like.
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.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of dengue 2 RNA and comparison of the encoded proteins with those of other flaviviruses."
    Hahn Y.S., Galler R., Hunkapiller T., Dalrymple J.M., Strauss J.H., Strauss E.G.
    Virology 162:167-180(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Definition of the carboxy termini of the three glycoproteins specified by dengue virus type 2."
    Wright P.J., Cauchi M.R., Ng M.L.
    Virology 171:61-67(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: C-TERMINUS OF M; E AND NS1.
    Strain: New-Guinea.
  3. "An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization."
    Egloff M.P., Benarroch D., Selisko B., Romette J.L., Canard B.
    EMBO J. 21:2757-2768(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2494-2783 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, CHARACTERIZATION OF METHYLTRANSFERASE ACTIVITY.
  4. "A ligand-binding pocket in the dengue virus envelope glycoprotein."
    Modis Y., Ogata S., Clements D., Harrison S.C.
    Proc. Natl. Acad. Sci. U.S.A. 100:6986-6991(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 281-674, DISULFIDE BONDS.
  5. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (16 ANGSTROMS) OF IMMATURE PARTICLES.

Entry informationi

Entry nameiPOLG_DEN2P
AccessioniPrimary (citable) accession number: P12823
Secondary accession number(s): Q88646
, Q88647, Q88648, Q88649, Q88650, Q88651, Q88652, Q88653, Q88654, Q88655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 9, 2015
This is version 166 of the entry and version 1 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.