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P27915

- POLG_DEN3P

UniProt

P27915 - POLG_DEN3P

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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

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
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 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 Source: UniProtKB-KW
  2. host cell membrane Source: UniProtKB-KW
  3. host cell nucleus Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
  5. viral capsid Source: UniProtKB-KW
  6. viral envelope Source: UniProtKB-KW
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_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

        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
TSLCLMMMLP ATLAFHLTSR DGEPRMIVGK NERGKSLLFK TASGINMCTL
160 170 180 190 200
IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC 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
CLESIEGKVV QHENLKYTVI ITVHTGDQHQ VGNETQGVTA EITSQASTAE
460 470 480 490 500
AILPEYGTLG LECSPRTGLD FNEMILLTMK NKAWMVHRQW FFDLPLPWTS
510 520 530 540 550
GATTKTPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT ALTGATEIQT
560 570 580 590 600
SGGTSIFAGH LKCRLKMDKL KLKGMSYAMC LNTFVLKKEV SETQHGTILI
610 620 630 640 650
KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP
660 670 680 690 700
FGESNIVIGI GDKALKINWY RKGSSIGKMF EATARGARRM AILGDTAWDF
710 720 730 740 750
GSVGGVLNSL GKMVHQIFGS AYTALFSGVS WIMKIGIGVL LTWIGLNSKN
760 770 780 790 800
TSMSFSCIAI GIITLYLGVV VQADMGCVIN WKGKELKCGS GIFVTNEVHT
810 820 830 840 850
WTEQYKFQAD SPKRVATAIA GAWENGVCGI RSTTRMENLL WKQIANELNY
860 870 880 890 900
ILWENDIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGLAKIVTAE
910 920 930 940 950
TQNSSFIIDG PSTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ
960 970 980 990 1000
LCDHRLMSAA VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK
1010 1020 1030 1040 1050
SHTLWSNGVL ESDMIIPKSL AGPISQHNHR PGYHTQTAGP WHLGKLELDF
1060 1070 1080 1090 1100
NYCEGTTVVI SENCGTRGPS LRTTTVSGKL IHEWCCRSCT LPPLRYMGED
1110 1120 1130 1140 1150
GCWYGMEIRP INEKEENMVK SLASAGSGKV DNFTMGVLCL AILFEEVMRG
1160 1170 1180 1190 1200
KFGKKHMIAG VLFTFVLLLS GQITWRGMAH TLIMIGSNAS DRMGMGVTYL
1210 1220 1230 1240 1250
ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMAATLR LPEDIEQMAN
1260 1270 1280 1290 1300
GIALGLMALK LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGI
1310 1320 1330 1340 1350
SLLPVCQSSS MRKTDWLPMT VAAMGVPPLP LFIFSLKDTL 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 MLVWHTWQKQ 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
VAAEMEEAMK GLPIRYQTTA TKSEHTGREI VDLMCHATFT MRLLSPVRVP
1760 1770 1780 1790 1800
NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP
1810 1820 1830 1840 1850
QSNAPIQDEE RDIPERSWNS GNEWITDFVG KTVWFVPSIK AGNVIANCLR
1860 1870 1880 1890 1900
KNGKKVIQLS RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FIADRVIDPR
1910 1920 1930 1940 1950
RCLKPVILTD GPERVILAGP MPVTVASAAQ RRGRVGRNPQ KENDQYIFMG
1960 1970 1980 1990 2000
QPLNKDEDHA HWTEAKMLLD NINTPEGIIP ALFEPEREKS AAIDGEYRLK
2010 2020 2030 2040 2050
GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG ERNNQILEEN
2060 2070 2080 2090 2100
MDVEIWTKEG EKKKLRPRWL 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
TKRDLGMSKE PGVVSPTSYL DVDLHPASAW TLYAVATTVI TPMLRHTIEN
2310 2320 2330 2340 2350
STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC YSQVNPLTLI
2360 2370 2380 2390 2400
AAVLLLVTHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV
2410 2420 2430 2440 2450
IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEVLTLAT GPITTLWEGS
2460 2470 2480 2490 2500
PGKFWNTTIA VSMANIFRGS YLAGAGLALS 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
FTNMEAQLIR QMEGEGVLSK ADLENPHPLE KKITQWLETK GVERLKRMAI
3160 3170 3180 3190 3200
SGDDCVVKPI DDRFANALLA LNDMGKVRKD IPQWQPSKGW HDWQQVPFCS
3210 3220 3230 3240 3250
HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE TACLGKAYAQ
3260 3270 3280 3290 3300
MWTLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML
3310 3320 3330 3340 3350
TVWNRVWIED NPWMEDKTPV TTWEDVPYLG KREDQWCGSL IGLTSRATWA
3360 3370 3380 3390
QNILTAIQQV RSLIGNEEFL DYMPSMKRFR KEEESEGAIW
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 29, 2014
This is version 136 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