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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 3 (strain Singapore/8120/1995) (DENV-3)
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 sitei1524 – 15241Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1548 – 15481Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1608 – 16081Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Binding sitei2504 – 25041mRNA capPROSITE-ProRule annotation
Binding sitei2507 – 25071mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2508 – 25081mRNA capPROSITE-ProRule annotation
Binding sitei2510 – 25101mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2515 – 25151mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2519 – 25191mRNA capPROSITE-ProRule annotation
Binding sitei2546 – 25461S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2551 – 25511Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2576 – 25761S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2577 – 25771S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2594 – 25941S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2595 – 25951S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2621 – 26211S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2622 – 26221S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2636 – 26361Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2637 – 26371S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2640 – 26401mRNA capPROSITE-ProRule annotation
Sitei2670 – 26701Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2701 – 27011mRNA capPROSITE-ProRule annotation
Binding sitei2703 – 27031mRNA capPROSITE-ProRule annotation
Sitei2706 – 27061Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2708 – 27081S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1667 – 16748ATPPROSITE-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

Protein family/group databases

MEROPSiS07.001.

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 3 (strain Singapore/8120/1995) (DENV-3)
Taxonomic identifieri408693 [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
  • UP000002479 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 – 100100CytoplasmicSequence analysisAdd
BLAST
Transmembranei101 – 11818HelicalSequence analysisAdd
BLAST
Topological domaini119 – 243125ExtracellularSequence analysisAdd
BLAST
Transmembranei244 – 26421HelicalSequence analysisAdd
BLAST
Topological domaini265 – 2651CytoplasmicSequence analysis
Transmembranei266 – 28015HelicalSequence analysisAdd
BLAST
Topological domaini281 – 723443ExtracellularSequence analysisAdd
BLAST
Intramembranei724 – 74421HelicalSequence analysisAdd
BLAST
Topological domaini745 – 7506ExtracellularSequence analysis
Intramembranei751 – 77121HelicalSequence analysisAdd
BLAST
Topological domaini772 – 1123352ExtracellularSequence analysisAdd
BLAST
Transmembranei1124 – 114421HelicalSequence analysisAdd
BLAST
Topological domaini1145 – 115410CytoplasmicSequence analysis
Transmembranei1155 – 117521HelicalSequence analysisAdd
BLAST
Topological domaini1176 – 119621LumenalSequence analysisAdd
BLAST
Transmembranei1197 – 121721HelicalSequence analysisAdd
BLAST
Topological domaini1218 – 128265CytoplasmicSequence analysisAdd
BLAST
Transmembranei1283 – 130321HelicalSequence analysisAdd
BLAST
Topological domaini1304 – 131512LumenalSequence analysisAdd
BLAST
Transmembranei1316 – 133621HelicalSequence analysisAdd
BLAST
Topological domaini1337 – 13448CytoplasmicSequence analysis
Transmembranei1345 – 136521HelicalSequence analysisAdd
BLAST
Topological domaini1366 – 13683LumenalSequence analysis
Transmembranei1369 – 138921HelicalSequence analysisAdd
BLAST
Topological domaini1390 – 144354CytoplasmicSequence analysisAdd
BLAST
Intramembranei1444 – 146421HelicalSequence analysisAdd
BLAST
Topological domaini1465 – 2146682CytoplasmicSequence analysisAdd
BLAST
Transmembranei2147 – 216721HelicalSequence analysisAdd
BLAST
Topological domaini2168 – 21692LumenalSequence analysis
Intramembranei2170 – 219021HelicalSequence analysisAdd
BLAST
Topological domaini2191 – 21911LumenalSequence analysis
Transmembranei2192 – 221221HelicalSequence analysisAdd
BLAST
Topological domaini2213 – 222715CytoplasmicSequence analysisAdd
BLAST
Transmembranei2228 – 224821Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2249 – 227325LumenalSequence analysisAdd
BLAST
Intramembranei2274 – 229421HelicalSequence analysisAdd
BLAST
Topological domaini2295 – 230511LumenalSequence analysisAdd
BLAST
Intramembranei2306 – 232621HelicalSequence analysisAdd
BLAST
Topological domaini2327 – 234620LumenalSequence analysisAdd
BLAST
Transmembranei2347 – 236721HelicalSequence analysisAdd
BLAST
Topological domaini2368 – 241245CytoplasmicSequence analysisAdd
BLAST
Transmembranei2413 – 243321HelicalSequence analysisAdd
BLAST
Topological domaini2434 – 245825LumenalSequence analysisAdd
BLAST
Transmembranei2459 – 247921HelicalSequence analysisAdd
BLAST
Topological domaini2480 – 3390911CytoplasmicSequence 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 – 33903390Genome polyproteinPRO_0000405223Add
BLAST
Chaini1 – 100100Capsid protein CBy similarityPRO_0000268058Add
BLAST
Propeptidei101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3PRO_0000268059Add
BLAST
Chaini115 – 280166prMBy similarityPRO_0000268060Add
BLAST
Chaini115 – 20591Peptide prBy similarityPRO_0000268061Add
BLAST
Chaini206 – 28075Small envelope protein MBy similarityPRO_0000268062Add
BLAST
Chaini281 – 773493Envelope protein EBy similarityPRO_0000268063Add
BLAST
Chaini774 – 1125352Non-structural protein 1By similarityPRO_0000268064Add
BLAST
Chaini1126 – 1343218Non-structural protein 2ABy similarityPRO_0000268065Add
BLAST
Chaini1126 – 1313188Non-structural protein 2A-alphaBy similarityPRO_0000268066Add
BLAST
Chaini1344 – 1473130Serine protease subunit NS2BBy similarityPRO_0000268067Add
BLAST
Chaini1474 – 2092619Serine protease NS3By similarityPRO_0000268068Add
BLAST
Chaini2093 – 2219127Non-structural protein 4ABy similarityPRO_0000268069Add
BLAST
Peptidei2220 – 224223Peptide 2kPRO_0000268070Add
BLAST
Chaini2243 – 2490248Non-structural protein 4BBy similarityPRO_0000268071Add
BLAST
Chaini2491 – 3390900RNA-directed RNA polymerase NS5By similarityPRO_0000268072Add
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 bondi463 ↔ 563By similarity
Disulfide bondi580 ↔ 611By similarity
Glycosylationi980 – 9801N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2300 – 23001N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2304 – 23041N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2456 – 24561N-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
Sitei773 – 7742Cleavage; by host signal peptidaseSequence analysis
Sitei1125 – 11262Cleavage; by hostBy similarity
Sitei1343 – 13442Cleavage; by viral protease NS3Sequence analysis
Sitei1473 – 14742Cleavage; by autolysisSequence analysis
Sitei2092 – 20932Cleavage; by autolysisSequence analysis
Sitei2219 – 22202Cleavage; by viral protease NS3Sequence analysis
Sitei2242 – 22432Cleavage; by host signal peptidaseSequence analysis
Sitei2490 – 24912Cleavage; 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
3390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1394 – 14007Combined sources
Beta strandi1409 – 14124Combined sources
Beta strandi1416 – 14216Combined sources
Beta strandi1427 – 14293Combined sources
Beta strandi1476 – 14783Combined sources
Beta strandi1493 – 150210Combined sources
Beta strandi1505 – 151511Combined sources
Beta strandi1518 – 15225Combined sources
Helixi1523 – 15264Combined sources
Beta strandi1531 – 15333Combined sources
Beta strandi1536 – 15383Combined sources
Beta strandi1540 – 15445Combined sources
Turni1545 – 15484Combined sources
Beta strandi1549 – 15557Combined sources
Beta strandi1568 – 15725Combined sources
Beta strandi1580 – 15845Combined sources
Beta strandi1587 – 15904Combined sources
Beta strandi1595 – 15995Combined sources
Beta strandi1611 – 16133Combined sources
Beta strandi1619 – 16224Combined sources
Beta strandi1625 – 16284Combined sources
Beta strandi1634 – 16374Combined sources
Helixi2499 – 25079Combined sources
Helixi2512 – 25187Combined sources
Turni2519 – 25224Combined sources
Beta strandi2524 – 25263Combined sources
Helixi2529 – 25368Combined sources
Beta strandi2541 – 25433Combined sources
Helixi2548 – 255710Combined sources
Beta strandi2565 – 25706Combined sources
Helixi2576 – 25816Combined sources
Beta strandi2587 – 25937Combined sources
Helixi2611 – 26133Combined sources
Beta strandi2614 – 26174Combined sources
Helixi2622 – 26243Combined sources
Beta strandi2631 – 26355Combined sources
Helixi2644 – 265815Combined sources
Helixi2659 – 26613Combined sources
Beta strandi2663 – 267210Combined sources
Helixi2677 – 269014Combined sources
Beta strandi2693 – 26953Combined sources
Beta strandi2707 – 27126Combined sources
Helixi2717 – 273317Combined sources
Beta strandi2740 – 27423Combined sources
Helixi2754 – 27563Combined sources
Helixi2763 – 277614Combined sources
Turni2777 – 27804Combined sources
Beta strandi2790 – 279910Combined sources
Helixi2812 – 28154Combined sources
Helixi2819 – 28213Combined sources
Beta strandi2822 – 28243Combined sources
Helixi2825 – 28284Combined sources
Helixi2837 – 284711Combined sources
Helixi2857 – 287418Combined sources
Helixi2885 – 28939Combined sources
Helixi2909 – 29146Combined sources
Helixi2918 – 293215Combined sources
Helixi2961 – 297818Combined sources
Helixi2980 – 29834Combined sources
Turni2984 – 29874Combined sources
Helixi2989 – 29924Combined sources
Beta strandi2993 – 29953Combined sources
Turni2997 – 29993Combined sources
Helixi3001 – 301212Combined sources
Helixi3027 – 30304Combined sources
Helixi3033 – 30397Combined sources
Helixi3040 – 30456Combined sources
Helixi3048 – 306013Combined sources
Beta strandi3063 – 307311Combined sources
Beta strandi3076 – 308712Combined sources
Beta strandi3090 – 30923Combined sources
Helixi3095 – 311420Combined sources
Helixi3120 – 31245Combined sources
Helixi3131 – 314515Combined sources
Beta strandi3148 – 31514Combined sources
Beta strandi3154 – 31574Combined sources
Helixi3162 – 31665Combined sources
Helixi3169 – 31735Combined sources
Beta strandi3178 – 31814Combined sources
Beta strandi3190 – 31923Combined sources
Helixi3193 – 31953Combined sources
Beta strandi3201 – 32077Combined sources
Beta strandi3213 – 32186Combined sources
Helixi3221 – 32288Combined sources
Beta strandi3233 – 32353Combined sources
Helixi3239 – 325517Combined sources
Helixi3260 – 327112Combined sources
Beta strandi3294 – 32974Combined sources
Helixi3299 – 33079Combined sources
Helixi3323 – 33253Combined sources
Helixi3331 – 33366Combined sources
Helixi3344 – 33518Combined sources
Helixi3353 – 336412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U1IX-ray2.30A/C1393-1438[»]
B/D1474-1655[»]
3U1JX-ray1.80A1393-1438[»]
B1474-1655[»]
4CTJX-ray1.47A/C2491-2766[»]
4CTKX-ray1.53A/C2491-2766[»]
4V0QX-ray2.30A2496-3385[»]
4V0RX-ray2.40A2496-3385[»]
ProteinModelPortaliQ5UB51.
SMRiQ5UB51. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1474 – 1651178Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1654 – 1810157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1821 – 1986166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2492 – 2753262mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3018 – 3168151RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni1396 – 143540Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1758 – 17614DEAH box

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.

Q5UB51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSRGLLNG QGPMKLVMAF
60 70 80 90 100
IAFLRFLAIP PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK
110 120 130 140 150
TSLCLMMILP ATLAFHLTSR DGEPRMIVGK NERGKSLLFK TASGINMCTL
160 170 180 190 200
IAMDLGEMCD DTVTYKCPLI AEVEPEDIDC WCNLTSTWVT YGTCNQAGEH
210 220 230 240 250
RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW ALRHPGFTIL
260 270 280 290 300
ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW
310 320 330 340 350
VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT
360 370 380 390 400
DSRCPTQGEA ILPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ
410 420 430 440 450
CLEPIEGKVV QHENLKYTVI ITVHTGDQHQ VGNDTQGVTV EITPQASTVE
460 470 480 490 500
AILPEYGTLG LECSPRTGLD FNEMILLTMK NKAWMVHRQW FFDLPLPWTS
510 520 530 540 550
GATTEAPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT ALTGATEIQN
560 570 580 590 600
SGGTSIFAGH LKCRLKMDKL ELKGMSYAMC LNTFVLKKEV SETQHGTILI
610 620 630 640 650
KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP
660 670 680 690 700
FGESNIVIGI GDKALKINWY KKGSSIGKMF EATARGARRM AILGDTAWDF
710 720 730 740 750
GSVGGVLNSL GKMVHQIFGS AYTALFSGVS WIMKIGIGVL LTWIGLNSKN
760 770 780 790 800
TSMSFSCIAI GIITLYLGAV VQADMGCVIN WKGKELKCGS GIFVTNEVHT
810 820 830 840 850
WTEQYKFQAD SPKRLATAIA GAWENGVCGI RSTTRMENLL WKQIANELNY
860 870 880 890 900
ILWENNIKLT VVVGDIIGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE
910 920 930 940 950
TQNSSFIIDG PNTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ
960 970 980 990 1000
SCDHRLMSAA IKDERAVHAD MGYWIESQKN GSWKLEKASF IEVKTCTWPK
1010 1020 1030 1040 1050
SHTLWSNGVL ESDMIIPKSL AGPISQHNHR PGYHTQTAGP WHLGKLELDF
1060 1070 1080 1090 1100
NYCEGTTVVI TENCGTRGPS LRATTVSGKL IHEWCCRSCT LPPLRYMGED
1110 1120 1130 1140 1150
GCWYGMEIRP VNEKEENMVK SLVSAGSGKV DNFTMGVLCL AILFEEVMRG
1160 1170 1180 1190 1200
KFGKKHMIAG VLFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTCL
1210 1220 1230 1240 1250
ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN
1260 1270 1280 1290 1300
GIALGLMTLK LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGV
1310 1320 1330 1340 1350
SLLPVCQSSS MRKTDWLPMT VAAMGVPPLP LFIFSLKDAL KRRSWPLNEG
1360 1370 1380 1390 1400
VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL LIACYVITGT SADLTVEKAA
1410 1420 1430 1440 1450
DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV LLKTALLIVS
1460 1470 1480 1490 1500
GIFPYSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ
1510 1520 1530 1540 1550
QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI
1560 1570 1580 1590 1600
SYGGGWRLSA QWQKGEEVQV IAVEPGKNPK NFQTMPGIFQ TTTGEIGAIA
1610 1620 1630 1640 1650
LDFKPGTSGS PIINREGKVV GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP
1660 1670 1680 1690 1700
ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA IVREAIKRRL RTLILAPTRV
1710 1720 1730 1740 1750
VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT MRLLSPVRVP
1760 1770 1780 1790 1800
NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTAEAFP
1810 1820 1830 1840 1850
QSNAPIQDEE RDIPERSWNS GNEWITDFVG KTVWFVPSIK AGNDIANCLR
1860 1870 1880 1890 1900
KNGKKVIQLS RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FKADRVIDPR
1910 1920 1930 1940 1950
RCLKPVILTD GPERVILAGP MPVTAASAAQ RRGRVGRNPQ KENDQYIFTG
1960 1970 1980 1990 2000
QPLNNDEDHA HWTEAKMLLD NINTPEGIIP ALFEPEREKS AAIDGEYRLK
2010 2020 2030 2040 2050
GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG ERNNQILEEN
2060 2070 2080 2090 2100
MDVEIWTKEG ERKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT
2110 2120 2130 2140 2150
EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL
2160 2170 2180 2190 2200
GLMILLTGGA MLFLISGKGI GKTSIGLICV IASSGMLWMA DVPLQWIASA
2210 2220 2230 2240 2250
IVLEFFMMVL LIPEPEKQRT PQDNQLAYVV IGILTLAAIV AANEMGLLET
2260 2270 2280 2290 2300
TKRNLGMSKE PGVVSPTSYL DVDLHPASAW TLYAVATTVI TPMLRHTIEN
2310 2320 2330 2340 2350
STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC YSQVNPLTLT
2360 2370 2380 2390 2400
AAVLLLVTHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV
2410 2420 2430 2440 2450
IYDSKFEKQL GQVMLLVLCA VQLLLMKTSW ALCEVLTLAT GPITTLWEGS
2460 2470 2480 2490 2500
PGKFWNTTIA VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG
2510 2520 2530 2540 2550
EKWKKKLNQL SRKEFDLYKK SGITEVDRTE AKEGLKRGEI THHAVSRGSA
2560 2570 2580 2590 2600
KLQWFVERNM VIPEGRVIDL GCGRGGWSYY CAGLKKVTEV RGYTKGGPGH
2610 2620 2630 2640 2650
EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES SPSPTVEESR
2660 2670 2680 2690 2700
TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS
2710 2720 2730 2740 2750
RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG
2760 2770 2780 2790 2800
TRHVNAEPET PNMDVIGERI KRIKEEHSST WHYDDENPYK TWAYHGSYEV
2810 2820 2830 2840 2850
KATGSASSMI NGVVKLLTKP WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT
2860 2870 2880 2890 2900
RTPRPMPGTR KVMEITAEWL WRTLGRNKRP RLCTREEFTK KVRTNAAMGA
2910 2920 2930 2940 2950
VFTEENQWDS ARAAVEDEEF WKLVDREREL HKLGKCGSCV YNMMGKREKK
2960 2970 2980 2990 3000
LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG
3010 3020 3030 3040 3050
LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH
3060 3070 3080 3090 3100
RQLANAIFKL TYQNKVVKVQ RPTPKGTVMD IISRKDQRGS GQVGTYGLNT
3110 3120 3130 3140 3150
FTNMEAQLVR QMEGEGVLSK ADLENPHPLE KKITQWLETK GVERLKRMAI
3160 3170 3180 3190 3200
SGDDCVVKPI DDRFANALLA LNDMGKVRKD IPQWQPSKGW HDWQQVPFCS
3210 3220 3230 3240 3250
HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLKE TACLGKAYAQ
3260 3270 3280 3290 3300
MWSLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML
3310 3320 3330 3340 3350
TVWNRVWIED NPWMEDKTPV TTWEDVPYLG KREDQWCGSL IGLTSRATWA
3360 3370 3380 3390
QNILIAIQQV RSLIGDEEFL DYMPSMKRFR KEEESEGAIW
Length:3,390
Mass (Da):377,970
Last modified:December 7, 2004 - v1
Checksum:i3E1ADA87637EB6E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY766104 Genomic RNA. Translation: AAV34603.1.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY766104 Genomic RNA. Translation: AAV34603.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U1IX-ray2.30A/C1393-1438[»]
B/D1474-1655[»]
3U1JX-ray1.80A1393-1438[»]
B1474-1655[»]
4CTJX-ray1.47A/C2491-2766[»]
4CTKX-ray1.53A/C2491-2766[»]
4V0QX-ray2.30A2496-3385[»]
4V0RX-ray2.40A2496-3385[»]
ProteinModelPortaliQ5UB51.
SMRiQ5UB51. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

PROiQ5UB51.

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. "Dengue Virus type, strain Singapore 8120/95."
    Yoong L.F., Tan T., Anwar A., August T.J., Too H.P.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLG_DEN3I
AccessioniPrimary (citable) accession number: Q5UB51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 7, 2004
Last modified: May 11, 2016
This is version 101 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.