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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 2 (strain Thailand/16681/1984) (DENV-2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications
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
Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA.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)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 sitei2505 – 25051mRNA capPROSITE-ProRule annotation
Binding sitei2508 – 25081mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2509 – 25091mRNA capPROSITE-ProRule annotation
Binding sitei2511 – 25111mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2516 – 25161mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2520 – 25201mRNA capPROSITE-ProRule annotation
Binding sitei2547 – 25471S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2552 – 25521Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2577 – 25771S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2578 – 25781S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2595 – 25951S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2596 – 25961S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2622 – 26221S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2623 – 26231S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2637 – 26371Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2638 – 26381S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2641 – 26411mRNA capPROSITE-ProRule annotation
Sitei2672 – 26721Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2703 – 27031mRNA capPROSITE-ProRule annotation
Binding sitei2705 – 27051mRNA capPROSITE-ProRule annotation
Sitei2708 – 27081Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2710 – 27101S-adenosyl-L-methioninePROSITE-ProRule annotation

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

BRENDAi2.7.7.50. 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 Thailand/16681/1984) (DENV-2)
Taxonomic identifieri31634 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes furcifer (Mosquito) [TaxID: 299627]
Aedes taylori (Mosquito) [TaxID: 299628]
Erythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000002324 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

  • Note: Located in RE-associated vesicles hosting the replication complex.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 101101CytoplasmicSequence analysisAdd
BLAST
Transmembranei102 – 11918HelicalSequence analysisAdd
BLAST
Topological domaini120 – 242123ExtracellularSequence analysisAdd
BLAST
Transmembranei243 – 26018HelicalSequence analysisAdd
BLAST
Topological domaini261 – 2611CytoplasmicSequence analysis
Transmembranei262 – 28019HelicalSequence 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 – 2147679CytoplasmicSequence analysisAdd
BLAST
Transmembranei2148 – 216821HelicalSequence analysisAdd
BLAST
Topological domaini2169 – 21702LumenalSequence analysis
Intramembranei2171 – 219121HelicalSequence analysisAdd
BLAST
Topological domaini2192 – 21921LumenalSequence analysis
Transmembranei2193 – 221321HelicalSequence analysisAdd
BLAST
Topological domaini2214 – 222815CytoplasmicSequence analysisAdd
BLAST
Transmembranei2229 – 224921Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2250 – 227728LumenalSequence analysisAdd
BLAST
Intramembranei2278 – 229518HelicalSequence analysisAdd
BLAST
Topological domaini2296 – 231621LumenalSequence analysisAdd
BLAST
Intramembranei2317 – 233721HelicalSequence analysisAdd
BLAST
Topological domaini2338 – 234710LumenalSequence analysis
Transmembranei2348 – 236821HelicalSequence analysisAdd
BLAST
Topological domaini2369 – 241345CytoplasmicSequence analysisAdd
BLAST
Transmembranei2414 – 243421HelicalSequence analysisAdd
BLAST
Topological domaini2435 – 245925LumenalSequence analysisAdd
BLAST
Transmembranei2460 – 248021HelicalSequence analysisAdd
BLAST
Topological domaini2481 – 3391911CytoplasmicSequence 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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 33913391Genome polyproteinPRO_0000405213Add
BLAST
Chaini1 – 100100Capsid protein CPRO_0000037925Add
BLAST
Propeptidei101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3PRO_0000037926Add
BLAST
Chaini115 – 280166prMPRO_0000264673Add
BLAST
Chaini115 – 20591Peptide prPRO_0000264674Add
BLAST
Chaini206 – 28075Small envelope protein MPRO_0000037927Add
BLAST
Chaini281 – 775495Envelope protein EPRO_0000037928Add
BLAST
Chaini776 – 1127352Non-structural protein 1PRO_0000037929Add
BLAST
Chaini1128 – 1345218Non-structural protein 2APRO_0000037930Add
BLAST
Chaini1128 – 1315188Non-structural protein 2A-alphaPRO_0000264675Add
BLAST
Chaini1346 – 1475130Serine protease subunit NS2BPRO_0000037931Add
BLAST
Chaini1476 – 2093618Serine protease NS3PRO_0000037932Add
BLAST
Chaini2094 – 2220127Non-structural protein 4APRO_0000037933Add
BLAST
Peptidei2221 – 224323Peptide 2kPRO_0000264676Add
BLAST
Chaini2244 – 2491248Non-structural protein 4BPRO_0000037934Add
BLAST
Chaini2492 – 3391900RNA-directed RNA polymerase NS5PRO_0000037935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Glycosylationi347 – 3471N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 396By similarity
Glycosylationi433 – 4331N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi465 ↔ 565By similarity
Disulfide bondi582 ↔ 613By similarity
Glycosylationi982 – 9821N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2301 – 23011N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2305 – 23051N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2457 – 24571N-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 NS3
Sitei114 – 1152Cleavage; by host signal peptidase
Sitei205 – 2062Cleavage; by host furinSequence analysis
Sitei280 – 2812Cleavage; by host signal peptidase
Sitei775 – 7762Cleavage; by host signal peptidase
Sitei1127 – 11282Cleavage; by host
Sitei1345 – 13462Cleavage; by viral protease NS3
Sitei1475 – 14762Cleavage; by autolysis
Sitei2093 – 20942Cleavage; by autolysis
Sitei2220 – 22212Cleavage; by viral protease NS3
Sitei2243 – 22442Cleavage; by host signal peptidase
Sitei2491 – 24922Cleavage; by viral protease NS3

Keywords - PTMi

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

PTM databases

iPTMnetiP29990.

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 (By similarity). 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 similarity4 Publications

Protein-protein interaction databases

IntActiP29990. 1 interaction.

Chemistry

BindingDBiP29990.

Structurei

Secondary structure

1
3391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi776 – 7816Combined sources
Turni783 – 7853Combined sources
Beta strandi788 – 79710Combined sources
Helixi814 – 82613Combined sources
Helixi837 – 85620Combined sources
Beta strandi862 – 8654Combined sources
Beta strandi870 – 8723Combined sources
Beta strandi907 – 9137Combined sources
Beta strandi916 – 9183Combined sources
Helixi920 – 9223Combined sources
Beta strandi928 – 9325Combined sources
Beta strandi942 – 9465Combined sources
Turni956 – 9583Combined sources
Beta strandi960 – 9645Combined sources
Beta strandi967 – 9715Combined sources
Beta strandi973 – 99321Combined sources
Turni1013 – 10153Combined sources
Helixi1020 – 10223Combined sources
Helixi1043 – 10453Combined sources
Beta strandi1046 – 10538Combined sources
Beta strandi1059 – 10624Combined sources
Beta strandi1073 – 10764Combined sources
Beta strandi1085 – 10906Combined sources
Beta strandi1096 – 10994Combined sources
Beta strandi1104 – 11063Combined sources
Beta strandi1110 – 11156Combined sources
Helixi1117 – 11193Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R69X-ray3.80A578-674[»]
4O6BX-ray3.00A/B775-1127[»]
ProteinModelPortaliP29990.
SMRiP29990. Positions 21-100, 115-195, 281-674, 1394-1440, 1495-2093, 2498-2759, 2765-3374.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29990.

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-terminalAdd
BLAST
Domaini2493 – 2755263mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3020 – 3169150RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni37 – 7236Hydrophobic; homodimerization of capsid protein CAdd
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 biasi2148 – 21547Poly-Leu
Compositional biasi3383 – 33864Poly-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.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

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.
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.

P29990-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDQRKKAKN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLYMAL
60 70 80 90 100
VAFLRFLTIP PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR
110 120 130 140 150
SAGMIIMLIP TVMAFHLTTR NGEPHMIVSR QEKGKSLLFK TEDGVNMCTL
160 170 180 190 200
MAMDLGELCE DTITYKCPLL RQNEPEDIDC WCNSTSTWVT YGTCTTMGEH
210 220 230 240 250
RRQKRSVALV PHVGMGLETR TETWMSSEGA WKHVQRIETW ILRHPGFTMM
260 270 280 290 300
AAILAYTIGT THFQRALIFI LLTAVTPSMT MRCIGMSNRD FVEGVSGGSW
310 320 330 340 350
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT
360 370 380 390 400
ESRCPTQGEP SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFR
410 420 430 440 450
CKKNMEGKVV QPENLEYTIV ITPHSGEEHA VGNDTGKHGK EIKITPQSST
460 470 480 490 500
TEAELTGYGT VTMECSPRTG LDFNEMVLLQ MENKAWLVHR 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 SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE
660 670 680 690 700
PPFGDSYIII GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW
710 720 730 740 750
DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS
760 770 780 790 800
RSTSLSVTLV LVGIVTLYLG VMVQADSGCV VSWKNKELKC GSGIFITDNV
810 820 830 840 850
HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN LMWKQITPEL
860 870 880 890 900
NHILSENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS
910 920 930 940 950
TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLKEKQ
960 970 980 990 1000
DVFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKNCHW
1010 1020 1030 1040 1050
PKSHTLWSNG VLESEMIIPK NLAGPVSQHN YRPGYHTQIT GPWHLGKLEM
1060 1070 1080 1090 1100
DFDFCDGTTV VVTEDCGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG
1110 1120 1130 1140 1150
EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QVDNFSLGVL GMALFLEEML
1160 1170 1180 1190 1200
RTRVGTKHAI LLVAVSFVTL IIGNMSFRDL GRVMVMVGAT MTDDIGMGVT
1210 1220 1230 1240 1250
YLALLAAFKV RPTFAAGLLL RKLTSKALMM TTIGIVLSSQ STTPETILEL
1260 1270 1280 1290 1300
TDALALGMMV LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA
1310 1320 1330 1340 1350
VVSVSPLFLT SSQQKTDWIP LALTIKGLNP TAIFLTTLSR TSKKRSWPLN
1360 1370 1380 1390 1400
EAIMAVGMVS ILASSLLKND IPMTGPLVAG GPLTVCYVLT GRSADLELER
1410 1420 1430 1440 1450
AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL TILIRTGLLV
1460 1470 1480 1490 1500
ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPMGK AELEDGAYRI
1510 1520 1530 1540 1550
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD
1560 1570 1580 1590 1600
LISYGGGWKL EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FKTNAGTIGA
1610 1620 1630 1640 1650
VSLDFSPGTS GSPIIDKKGK VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN
1660 1670 1680 1690 1700
PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP AIVREAIKRG LRTLILAPTR
1710 1720 1730 1740 1750
VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF TMRLLSPVRV
1760 1770 1780 1790 1800
PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
1810 1820 1830 1840 1850
PQSNAPIIDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL
1860 1870 1880 1890 1900
SKNGKKVIQL SRKTFDSEYA KTRTNDWDFV VTTDISEMGA NFKAERVIDP
1910 1920 1930 1940 1950
RRCMKPVILT DGEERVILAG PMPVTHSSAA QRRGRIGRNP KNENDQYIYM
1960 1970 1980 1990 2000
GEPLENDEDC AHWKEAKMLL DNINTPEGII PSMFEPEREK VDAIDGEYRL
2010 2020 2030 2040 2050
RGEARTTFVD LMRRGDLPVW LAYRVAAEGI NYADRRWCFD GVKNNQILEE
2060 2070 2080 2090 2100
NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
2110 2120 2130 2140 2150
TEMGRLPTFM TQKARDALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL
2160 2170 2180 2190 2200
LTLLATVTGG ILLFLMSGRG IGKMTLGMCC IITASILLWY AQIQPHWIAA
2210 2220 2230 2240 2250
SIILEFFLIV LLIPEPEKQR TPQDNQLTYV VIAILTVVAA TMANEMGFLE
2260 2270 2280 2290 2300
KTKKDLGLGS IATQQPESNI LDIDLRPASA WTLYAVATTF VTPMLRHSIE
2310 2320 2330 2340 2350
NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG CYSQVNPTTL
2360 2370 2380 2390 2400
TAALFLLVAH YAIIGPALQA KASREAQKRA AAGIMKNPTV DGITVIDLDP
2410 2420 2430 2440 2450
IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEVLTLA TGPISTLWEG
2460 2470 2480 2490 2500
NPGRFWNTTI AVSMANIFRG SYLAGAGLLF SIMKNTTNAR RGTGNIGETL
2510 2520 2530 2540 2550
GEKWKSRLNA LGKSEFQIYK KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS
2560 2570 2580 2590 2600
AKLRWFVERN MVTPEGKVVD LGCGRGGWSY YCGGLKNVRE VKGLTKGGPG
2610 2620 2630 2640 2650
HEEPIPMSTY GWNLVRLQSG VDVFFIPPEK CDTLLCDIGE SSPNPTVEAG
2660 2670 2680 2690 2700
RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP
2710 2720 2730 2740 2750
LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRYKK ATYEPDVDLG
2760 2770 2780 2790 2800
SGTRNIGIES EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY
2810 2820 2830 2840 2850
ETKQTGSASS MVNGVFRLLT KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV
2860 2870 2880 2890 2900
DTRTQEPKEG TKKLMKITAE WLWKELGKKK TPRMCTREEF TRKVRSNAAL
2910 2920 2930 2940 2950
GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET CVYNIMGKRE
2960 2970 2980 2990 3000
KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG
3010 3020 3030 3040 3050
EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EAMVTNHMEG
3060 3070 3080 3090 3100
EHKKLAEAIF KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL
3110 3120 3130 3140 3150
NTFTNMEAQL IRQMEGEGVF KSIQHLTITE EIAVQNWLAR VGRERLSRMA
3160 3170 3180 3190 3200
ISGDDCVVKP LDDRLPSALT ALNDTGKIRK DIQQWEPSRG WNDWTQVPFC
3210 3220 3230 3240 3250
SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR ETACLGKSYD
3260 3270 3280 3290 3300
QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
3310 3320 3330 3340 3350
LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW
3360 3370 3380 3390
AKNIQAAINQ VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W
Length:3,391
Mass (Da):379,547
Last modified:April 1, 1993 - v1
Checksum:i2E20AD0D6C978ECC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84727 Genomic RNA. Translation: AAA73185.1.
PIRiA42451. GNWV16.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84727 Genomic RNA. Translation: AAA73185.1.
PIRiA42451. GNWV16.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R69X-ray3.80A578-674[»]
4O6BX-ray3.00A/B775-1127[»]
ProteinModelPortaliP29990.
SMRiP29990. Positions 21-100, 115-195, 281-674, 1394-1440, 1495-2093, 2498-2759, 2765-3374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29990. 1 interaction.

Chemistry

BindingDBiP29990.
ChEMBLiCHEMBL5980.

PTM databases

iPTMnetiP29990.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.7.7.50. 1867.

Miscellaneous databases

EvolutionaryTraceiP29990.
PROiP29990.

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.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparison of a dengue-2 virus and its candidate vaccine derivative: sequence relationships with the flaviviruses and other viruses."
    Blok J., McWilliam S.M., Butler H.C., Gibbs A.J., Weiller G., Herring B.L., Hemsley A.C., Aaskov J.G., Yoksan S., Bhamarapravati N.
    Virology 187:573-590(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Flavivirus capsid is a dimeric alpha-helical protein."
    Jones C.T., Ma L., Burgner J.W., Groesch T.D., Post C.B., Kuhn R.J.
    J. Virol. 77:7143-7149(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  3. "Alterations of pr-M cleavage and virus export in pr-M junction chimeric dengue viruses."
    Keelapang P., Sriburi R., Supasa S., Panyadee N., Songjaeng A., Jairungsri A., Puttikhunt C., Kasinrerk W., Malasit P., Sittisombut N.
    J. Virol. 78:2367-2381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  4. "Identification of the homotypic interaction domain of the core protein of dengue virus type 2."
    Wang S.H., Syu W.J., Hu S.T.
    J. Gen. Virol. 85:2307-2314(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, REGION OF HOMODIMERIZATION OF CAPSID PROTEIN C.
  5. "Inhibition of alpha/beta interferon signaling by the NS4B protein of flaviviruses."
    Munoz-Jordan J.L., Laurent-Rolle M., Ashour J., Martinez-Sobrido L., Ashok M., Lipkin W.I., Garcia-Sastre A.
    J. Virol. 79:8004-8013(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF NON-STRUCTURAL PROTEIN 4B, FUNCTION OF PEPTIDE 2K.
  6. Cited for: FUNCTION OF NS1.
  7. "Nuclear localization of flavivirus RNA synthesis in infected cells."
    Uchil P.D., Kumar A.V., Satchidanandam V.
    J. Virol. 80:5451-5464(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF SERINE PROTEASE NS3, SUBCELLULAR LOCATION OF RNA-DIRECTED RNA POLYMERASE NS5.
    Strain: TR 1751.
  8. "Cleavage preference distinguishes the two-component NS2B-NS3 serine proteinases of Dengue and West Nile viruses."
    Shiryaev S.A., Kozlov I.A., Ratnikov B.I., Smith J.W., Lebl M., Strongin A.Y.
    Biochem. J. 401:743-752(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  9. "Dengue virus type 2 antagonizes IFN-alpha but not IFN-gamma antiviral effect via down-regulating Tyk2-STAT signaling in the human dendritic cell."
    Ho L.J., Hung L.F., Weng C.Y., Wu W.L., Chou P., Lin Y.L., Chang D.M., Tai T.Y., Lai J.H.
    J. Immunol. 174:8163-8172(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
  10. Cited for: CHARACTERIZATION OF NS1.
  11. "The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure."
    Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S., Mayette J., Hobdey S.E., Bisaillon M.
    RNA 15:2340-2350(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5, INTERACTION OF NS5 WITH NS3.
  12. "Dengue virus NS5 inhibits interferon-alpha signaling by blocking signal transducer and activator of transcription 2 phosphorylation."
    Mazzon M., Jones M., Davidson A., Chain B., Jacobs M.
    J. Infect. Dis. 200:1261-1270(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5, INTERACTION OF NS5 WITH HUMAN STAT2.
  13. "Characterization of dengue virus entry into HepG2 cells."
    Suksanpaisan L., Susantad T., Smith D.R.
    J. Biomed. Sci. 16:17-17(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF ENVELOPE PROTEIN E.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 578-674.

Entry informationi

Entry nameiPOLG_DEN26
AccessioniPrimary (citable) accession number: P29990
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: January 20, 2016
This is version 148 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.