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P27915

- POLG_DEN3P

UniProt

P27915 - POLG_DEN3P

Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 3 (strain Philippines/H87/1956) (DENV-3)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA By similarity.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.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.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.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.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
    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
    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
    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
    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

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. double-stranded RNA binding Source: InterPro
    4. metal ion binding Source: UniProtKB-KW
    5. mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-EC
    6. mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB-EC
    7. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    8. RNA helicase activity Source: InterPro
    9. serine-type endopeptidase activity Source: InterPro
    10. serine-type exopeptidase activity Source: InterPro
    11. structural molecule activity Source: InterPro

    GO - Biological processi

    1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    3. induction by virus of host autophagy Source: UniProtKB-KW
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. suppression by virus of host STAT2 activity Source: UniProtKB-KW
    6. suppression by virus of host TYK2 activity Source: UniProtKB-KW
    7. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
    8. transcription, DNA-templated Source: UniProtKB-KW
    9. viral RNA genome replication Source: InterPro
    10. virion attachment to host cell Source: UniProtKB-KW

    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 Philippines/H87/1956) (DENV-3)
    Taxonomic identifieri408870 [NCBI]
    Taxonomic lineageiVirusesssRNA 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]
    ProteomesiUP000007200: Genome

    Subcellular locationi

    Chain Peptide pr : Secreted By similarity
    Chain Small envelope protein M : Virion membrane By similarity; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain Envelope protein E : Virion membrane By similarity; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain Non-structural protein 1 : Secreted. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Lumenal side By similarity
    Chain Non-structural protein 2A : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein Curated
    Chain Serine protease subunit NS2B : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein Curated
    Chain 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
    Chain Non-structural protein 4A : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Note: Located in RE-associated vesicles hosting the replication complex.
    Chain Non-structural protein 4B : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain 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.

    GO - Cellular componenti

    1. host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. viral capsid Source: UniProtKB-KW
    5. viral envelope Source: UniProtKB-KW
    6. virion membrane Source: UniProtKB-SubCell

    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_0000405221Add
    BLAST
    Chaini1 – 100100Capsid protein CBy similarityPRO_0000037989Add
    BLAST
    Propeptidei101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000037990Add
    BLAST
    Chaini115 – 280166prMBy similarityPRO_0000308293Add
    BLAST
    Chaini115 – 20591Peptide prBy similarityPRO_0000308294Add
    BLAST
    Chaini206 – 28075Small envelope protein MBy similarityPRO_0000037991Add
    BLAST
    Chaini281 – 773493Envelope protein EBy similarityPRO_0000037992Add
    BLAST
    Chaini774 – 1125352Non-structural protein 1By similarityPRO_0000037993Add
    BLAST
    Chaini1126 – 1343218Non-structural protein 2ABy similarityPRO_0000037994Add
    BLAST
    Chaini1126 – 1313188Non-structural protein 2A-alphaBy similarityPRO_0000308295Add
    BLAST
    Chaini1344 – 1473130Serine protease subunit NS2BBy similarityPRO_0000037995Add
    BLAST
    Chaini1474 – 2092619Serine protease NS3By similarityPRO_0000037996Add
    BLAST
    Chaini2093 – 2219127Non-structural protein 4ABy similarityPRO_0000037997Add
    BLAST
    Peptidei2220 – 224223Peptide 2kBy similarityPRO_0000308296Add
    BLAST
    Chaini2243 – 2490248Non-structural protein 4BBy similarityPRO_0000037998Add
    BLAST
    Chaini2491 – 3390900RNA-directed RNA polymerase NS5By similarityPRO_0000037999Add
    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
    Glycosylationi903 – 9031N-linked (GlcNAc...); by hostSequence Analysis
    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.By similarity

    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.By similarity

    Structurei

    Secondary structure

    1
    3390
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni282 – 2854
    Beta strandi287 – 2937
    Beta strandi301 – 3055
    Beta strandi310 – 3156
    Beta strandi318 – 32710
    Beta strandi334 – 3374
    Beta strandi343 – 3519
    Helixi363 – 3664
    Beta strandi368 – 37912
    Turni381 – 3844
    Beta strandi389 – 40416
    Beta strandi406 – 4094
    Beta strandi415 – 4239
    Beta strandi434 – 4363
    Beta strandi438 – 4436
    Beta strandi448 – 4536
    Turni454 – 4563
    Beta strandi457 – 4626
    Beta strandi473 – 4797
    Beta strandi482 – 4876
    Helixi488 – 4936
    Beta strandi503 – 5053
    Helixi512 – 5143
    Beta strandi517 – 5193
    Beta strandi521 – 5244
    Beta strandi527 – 5293
    Helixi535 – 5417
    Beta strandi543 – 5453
    Beta strandi561 – 5666
    Beta strandi577 – 5793
    Beta strandi584 – 5863
    Beta strandi594 – 5963
    Beta strandi598 – 6047
    Beta strandi610 – 6123
    Beta strandi615 – 6184
    Beta strandi628 – 6314
    Beta strandi635 – 6373
    Beta strandi643 – 6486
    Beta strandi651 – 66111
    Beta strandi665 – 6717
    Helixi2499 – 250911
    Helixi2512 – 25198
    Turni2520 – 25223
    Beta strandi2524 – 25274
    Helixi2529 – 25368
    Helixi2548 – 255710
    Beta strandi2565 – 25717
    Helixi2576 – 25827
    Beta strandi2587 – 25937
    Turni2609 – 26124
    Beta strandi2613 – 26175
    Helixi2622 – 26243
    Beta strandi2631 – 26355
    Helixi2644 – 265815
    Helixi2659 – 26613
    Beta strandi2666 – 26727
    Helixi2677 – 269014
    Beta strandi2693 – 26953
    Beta strandi2707 – 27126
    Helixi2717 – 273014
    Beta strandi2733 – 27353
    Beta strandi2740 – 27434

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UZGX-ray3.60A/B281-672[»]
    2J7UX-ray1.85A2762-3390[»]
    2J7WX-ray2.60A2762-3390[»]
    3P8ZX-ray1.70A/C2491-2752[»]
    3P97X-ray1.70A/C2491-2752[»]
    3UZEX-ray2.04C/D573-673[»]
    3VTTX-ray1.70A/B574-678[»]
    ProteinModelPortaliP27915.
    SMRiP27915. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27915.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 100100CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini119 – 243125ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini265 – 2651CytoplasmicSequence Analysis
    Topological domaini281 – 723443ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini745 – 7506ExtracellularSequence Analysis
    Topological domaini772 – 1123352ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1145 – 115410CytoplasmicSequence Analysis
    Topological domaini1176 – 119621LumenalSequence AnalysisAdd
    BLAST
    Topological domaini1218 – 128265CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1304 – 131512LumenalSequence AnalysisAdd
    BLAST
    Topological domaini1337 – 13448CytoplasmicSequence Analysis
    Topological domaini1366 – 13683LumenalSequence Analysis
    Topological domaini1390 – 144354CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1465 – 2146682CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2168 – 21692LumenalSequence Analysis
    Topological domaini2191 – 21911LumenalSequence Analysis
    Topological domaini2213 – 222715CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2249 – 227325LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2295 – 230511LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2327 – 234620LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2368 – 241245CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2434 – 245825LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2480 – 3390911CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei724 – 74421HelicalSequence AnalysisAdd
    BLAST
    Intramembranei751 – 77121HelicalSequence AnalysisAdd
    BLAST
    Intramembranei1444 – 146421HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2170 – 219021HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2274 – 229421HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2306 – 232621HelicalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei101 – 11818HelicalSequence AnalysisAdd
    BLAST
    Transmembranei244 – 26421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei266 – 28015HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1124 – 114421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1155 – 117521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1197 – 121721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1283 – 130321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1316 – 133621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1345 – 136521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1369 – 138921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2147 – 216721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2192 – 221221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2228 – 224821Helical; Note=Signal for NS4BSequence AnalysisAdd
    BLAST
    Transmembranei2347 – 236721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2413 – 243321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2459 – 247921HelicalSequence AnalysisAdd
    BLAST

    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

    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.
    IPR000208. RNA-dir_pol_flavivirus.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    [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.
    PF00271. Helicase_C. 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.

    P27915-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSRGLLNG QGPMKLVMAF     50
    IAFLRFLAIP PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK 100
    TSLCLMMMLP ATLAFHLTSR DGEPRMIVGK NERGKSLLFK TASGINMCTL 150
    IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC WCNLTSTWVT YGTCNQAGEH 200
    RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW ALRHPGFTIL 250
    ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW 300
    VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT 350
    DSRCPTQGEA ILPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ 400
    CLESIEGKVV QHENLKYTVI ITVHTGDQHQ VGNETQGVTA EITSQASTAE 450
    AILPEYGTLG LECSPRTGLD FNEMILLTMK NKAWMVHRQW FFDLPLPWTS 500
    GATTKTPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT ALTGATEIQT 550
    SGGTSIFAGH LKCRLKMDKL KLKGMSYAMC LNTFVLKKEV SETQHGTILI 600
    KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP 650
    FGESNIVIGI GDKALKINWY RKGSSIGKMF EATARGARRM AILGDTAWDF 700
    GSVGGVLNSL GKMVHQIFGS AYTALFSGVS WIMKIGIGVL LTWIGLNSKN 750
    TSMSFSCIAI GIITLYLGVV VQADMGCVIN WKGKELKCGS GIFVTNEVHT 800
    WTEQYKFQAD SPKRVATAIA GAWENGVCGI RSTTRMENLL WKQIANELNY 850
    ILWENDIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGLAKIVTAE 900
    TQNSSFIIDG PSTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ 950
    LCDHRLMSAA VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK 1000
    SHTLWSNGVL ESDMIIPKSL AGPISQHNHR PGYHTQTAGP WHLGKLELDF 1050
    NYCEGTTVVI SENCGTRGPS LRTTTVSGKL IHEWCCRSCT LPPLRYMGED 1100
    GCWYGMEIRP INEKEENMVK SLASAGSGKV DNFTMGVLCL AILFEEVMRG 1150
    KFGKKHMIAG VLFTFVLLLS GQITWRGMAH TLIMIGSNAS DRMGMGVTYL 1200
    ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMAATLR LPEDIEQMAN 1250
    GIALGLMALK LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGI 1300
    SLLPVCQSSS MRKTDWLPMT VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG 1350
    VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL LIACYVITGT SADLTVEKAA 1400
    DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV LLKTALLIVS 1450
    GIFPYSIPAT MLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ 1500
    QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI 1550
    SYGGGWRLSA QWQKGEEVQV IAVEPGKNPK NFQTMPGIFQ TTTGEIGAIA 1600
    LDFKPGTSGS PIINREGKVV GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP 1650
    ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA IVREAIKRRL RTLILAPTRV 1700
    VAAEMEEAMK GLPIRYQTTA TKSEHTGREI VDLMCHATFT MRLLSPVRVP 1750
    NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP 1800
    QSNAPIQDEE RDIPERSWNS GNEWITDFVG KTVWFVPSIK AGNVIANCLR 1850
    KNGKKVIQLS RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FIADRVIDPR 1900
    RCLKPVILTD GPERVILAGP MPVTVASAAQ RRGRVGRNPQ KENDQYIFMG 1950
    QPLNKDEDHA HWTEAKMLLD NINTPEGIIP ALFEPEREKS AAIDGEYRLK 2000
    GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG ERNNQILEEN 2050
    MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT 2100
    EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL 2150
    GLMILLTGGA MLFLISGKGI GKTSIGLICV IASSGMLWMA DVPLQWIASA 2200
    IVLEFFMMVL LIPEPEKQRT PQDNQLAYVV IGILTLAAIV AANEMGLLET 2250
    TKRDLGMSKE PGVVSPTSYL DVDLHPASAW TLYAVATTVI TPMLRHTIEN 2300
    STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC YSQVNPLTLI 2350
    AAVLLLVTHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV 2400
    IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEVLTLAT GPITTLWEGS 2450
    PGKFWNTTIA VSMANIFRGS YLAGAGLALS IMKSVGTGKR GTGSQGETLG 2500
    EKWKKKLNQL SRKEFDLYKK SGITEVDRTE AKEGLKRGEI THHAVSRGSA 2550
    KLQWFVERNM VIPEGRVIDL GCGRGGWSYY CAGLKKVTEV RGYTKGGPGH 2600
    EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES SPSPTVEESR 2650
    TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS 2700
    RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG 2750
    TRHVNAEPET PNMDVIGERI KRIKEEHSST WHYDDENPYK TWAYHGSYEV 2800
    KATGSASSMI NGVVKLLTKP WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT 2850
    RTPRPMPGTR KVMEITAEWL WRTLGRNKRP RLCTREEFTK KVRTNAAMGA 2900
    VFTEENQWDS ARAAVEDEEF WKLVDREREL HKLGKCGSCV YNMMGKREKK 2950
    LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG 3000
    LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH 3050
    RQLANAIFKL TYQNKVVKVQ RPTPKGTVMD IISRKDQRGS GQVGTYGLNT 3100
    FTNMEAQLIR QMEGEGVLSK ADLENPHPLE KKITQWLETK GVERLKRMAI 3150
    SGDDCVVKPI DDRFANALLA LNDMGKVRKD IPQWQPSKGW HDWQQVPFCS 3200
    HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE TACLGKAYAQ 3250
    MWTLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML 3300
    TVWNRVWIED NPWMEDKTPV TTWEDVPYLG KREDQWCGSL IGLTSRATWA 3350
    QNILTAIQQV RSLIGNEEFL DYMPSMKRFR KEEESEGAIW 3390
    Length:3,390
    Mass (Da):378,063
    Last modified:August 1, 1992 - v1
    Checksum:i666E8F70F1E1756E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93130 Genomic RNA. Translation: AAA99437.1.
    PIRiA34774. GNWVD3.

    Cross-referencesi

    Web resourcesi

    Virus Pathogen Resource

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93130 Genomic RNA. Translation: AAA99437.1 .
    PIRi A34774. GNWVD3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UZG X-ray 3.60 A/B 281-672 [» ]
    2J7U X-ray 1.85 A 2762-3390 [» ]
    2J7W X-ray 2.60 A 2762-3390 [» ]
    3P8Z X-ray 1.70 A/C 2491-2752 [» ]
    3P97 X-ray 1.70 A/C 2491-2752 [» ]
    3UZE X-ray 2.04 C/D 573-673 [» ]
    3VTT X-ray 1.70 A/B 574-678 [» ]
    ProteinModelPortali P27915.
    SMRi P27915. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S07.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P27915.
    PROi P27915.

    Family and domain databases

    Gene3Di 2.60.40.350. 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.
    InterProi IPR011492. 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.
    IPR000208. RNA-dir_pol_flavivirus.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF01003. Flavi_capsid. 1 hit.
    PF07652. Flavi_DEAD. 1 hit.
    PF02832. Flavi_glycop_C. 1 hit.
    PF00869. Flavi_glycoprot. 1 hit.
    PF01004. Flavi_M. 1 hit.
    PF00948. Flavi_NS1. 1 hit.
    PF01005. Flavi_NS2A. 1 hit.
    PF01002. Flavi_NS2B. 1 hit.
    PF01350. Flavi_NS4A. 1 hit.
    PF01349. Flavi_NS4B. 1 hit.
    PF00972. Flavi_NS5. 1 hit.
    PF01570. Flavi_propep. 1 hit.
    PF01728. FtsJ. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00949. Peptidase_S7. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003817. Gen_Poly_FLV. 1 hit.
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF53335. SSF53335. 1 hit.
    SSF56983. SSF56983. 1 hit.
    SSF81296. SSF81296. 1 hit.
    TIGRFAMsi TIGR04240. flavi_E_stem. 1 hit.
    PROSITEi PS51527. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of dengue type 3 virus genome RNA."
      Osatomi K., Sumiyoshi H.
      Virology 176:643-647(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], PARTIAL PROTEIN SEQUENCE.
    2. "Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein."
      Modis Y., Ogata S., Clements D., Harrison S.C.
      J. Virol. 79:1223-1231(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 281-672.

    Entry informationi

    Entry nameiPOLG_DEN3P
    AccessioniPrimary (citable) accession number: P27915
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 135 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, Direct protein sequencing, 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

    External Data

    Dasty 3