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P27915 (POLG_DEN3P) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 14 chains:

  1. Capsid protein C
    Alternative name(s):
    Core protein
  2. prM
  3. Peptide pr
  4. Small envelope protein M
    Alternative name(s):
    Matrix protein
  5. Envelope protein E
  6. Non-structural protein 1
    Short name=NS1
  7. Non-structural protein 2A
    Short name=NS2A
  8. Non-structural protein 2A-alpha
    Short name=NS2A-alpha
  9. Serine protease subunit NS2B
    Alternative name(s):
    Flavivirin protease NS2B regulatory subunit
    Non-structural protein 2B
  10. Serine protease NS3
    EC=3.4.21.91
    EC=3.6.1.15
    EC=3.6.4.13
    Alternative name(s):
    Flavivirin protease NS3 catalytic subunit
    Non-structural protein 3
  11. Non-structural protein 4A
    Short name=NS4A
  12. Peptide 2k
  13. Non-structural protein 4B
    Short name=NS4B
  14. RNA-directed RNA polymerase NS5
    EC=2.1.1.56
    EC=2.1.1.57
    EC=2.7.7.48
    Alternative name(s):
    Non-structural protein 5
OrganismDengue virus type 3 (strain Philippines/H87/1956) (DENV-3) [Complete proteome]
Taxonomic identifier408870 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostAedimorphus [TaxID: 53540]
Diceromyia [TaxID: 53539]
Erythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
Stegomyia [TaxID: 53541]

Protein attributes

Sequence length3390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 Potential.

Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity.

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.

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.

Catalytic activity

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).

NTP + H2O = NDP + phosphate.

ATP + H2O = ADP + phosphate.

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

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).

Subunit structure

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.

Subcellular location

Capsid protein C: Virion Potential.

Peptide pr: Secreted By similarity.

Small envelope protein M: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Envelope protein E: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity.

Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Remains non-covalently associated to NS3 protease By similarity.

Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Located in RE-associated vesicles hosting the replication complex.

Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Host nucleus By similarity. Note: Located in RE-associated vesicles hosting the replication complex.

Post-translational modification

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.

Sequence similarities

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 mRNA cap 0-1 NS5-type MT domain.

Contains 1 peptidase S7 domain.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processActivation 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
   Cellular componentCapsid protein
Host endoplasmic reticulum
Host membrane
Host nucleus
Membrane
Secreted
Viral envelope protein
Virion
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
S-adenosyl-L-methionine
   Molecular functionHelicase
Hydrolase
Methyltransferase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Serine protease
Transferase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processclathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host STAT2 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host TYK2 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host type I interferon-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

double-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

mRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

mRNA (nucleoside-2'-O-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 33903390Genome polyprotein
PRO_0000405221
Chain1 – 100100Capsid protein C By similarity
PRO_0000037989
Propeptide101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000037990
Chain115 – 280166prM By similarity
PRO_0000308293
Chain115 – 20591Peptide pr By similarity
PRO_0000308294
Chain206 – 28075Small envelope protein M By similarity
PRO_0000037991
Chain281 – 773493Envelope protein E By similarity
PRO_0000037992
Chain774 – 1125352Non-structural protein 1 By similarity
PRO_0000037993
Chain1126 – 1343218Non-structural protein 2A By similarity
PRO_0000037994
Chain1126 – 1313188Non-structural protein 2A-alpha By similarity
PRO_0000308295
Chain1344 – 1473130Serine protease subunit NS2B By similarity
PRO_0000037995
Chain1474 – 2092619Serine protease NS3 By similarity
PRO_0000037996
Chain2093 – 2219127Non-structural protein 4A By similarity
PRO_0000037997
Peptide2220 – 224223Peptide 2k By similarity
PRO_0000308296
Chain2243 – 2490248Non-structural protein 4B By similarity
PRO_0000037998
Chain2491 – 3390900RNA-directed RNA polymerase NS5 By similarity
PRO_0000037999

Regions

Topological domain1 – 100100Cytoplasmic Potential
Transmembrane101 – 11818Helical; Potential
Topological domain119 – 243125Extracellular Potential
Transmembrane244 – 26421Helical; Potential
Topological domain2651Cytoplasmic Potential
Transmembrane266 – 28015Helical; Potential
Topological domain281 – 723443Extracellular Potential
Intramembrane724 – 74421Helical; Potential
Topological domain745 – 7506Extracellular Potential
Intramembrane751 – 77121Helical; Potential
Topological domain772 – 1123352Extracellular Potential
Transmembrane1124 – 114421Helical; Potential
Topological domain1145 – 115410Cytoplasmic Potential
Transmembrane1155 – 117521Helical; Potential
Topological domain1176 – 119621Lumenal Potential
Transmembrane1197 – 121721Helical; Potential
Topological domain1218 – 128265Cytoplasmic Potential
Transmembrane1283 – 130321Helical; Potential
Topological domain1304 – 131512Lumenal Potential
Transmembrane1316 – 133621Helical; Potential
Topological domain1337 – 13448Cytoplasmic Potential
Transmembrane1345 – 136521Helical; Potential
Topological domain1366 – 13683Lumenal Potential
Transmembrane1369 – 138921Helical; Potential
Topological domain1390 – 144354Cytoplasmic Potential
Intramembrane1444 – 146421Helical; Potential
Topological domain1465 – 2146682Cytoplasmic Potential
Transmembrane2147 – 216721Helical; Potential
Topological domain2168 – 21692Lumenal Potential
Intramembrane2170 – 219021Helical; Potential
Topological domain21911Lumenal Potential
Transmembrane2192 – 221221Helical; Potential
Topological domain2213 – 222715Cytoplasmic Potential
Transmembrane2228 – 224821Helical; Note=Signal for NS4B; Potential
Topological domain2249 – 227325Lumenal Potential
Intramembrane2274 – 229421Helical; Potential
Topological domain2295 – 230511Lumenal Potential
Intramembrane2306 – 232621Helical; Potential
Topological domain2327 – 234620Lumenal Potential
Transmembrane2347 – 236721Helical; Potential
Topological domain2368 – 241245Cytoplasmic Potential
Transmembrane2413 – 243321Helical; Potential
Topological domain2434 – 245825Lumenal Potential
Transmembrane2459 – 247921Helical; Potential
Topological domain2480 – 3390911Cytoplasmic Potential
Domain1474 – 1651178Peptidase S7
Domain1654 – 1810157Helicase ATP-binding
Domain1821 – 1986166Helicase C-terminal
Domain2492 – 2753262mRNA cap 0-1 NS5-type MT
Domain3018 – 3168151RdRp catalytic
Nucleotide binding1667 – 16748ATP Potential
Region33 – 7442Hydrophobic; homodimerization of capsid protein C By similarity
Region1396 – 143540Interacts with and activates NS3 protease By similarity
Motif1758 – 17614DEAH box

Sites

Active site15241Charge relay system; for serine protease NS3 activity By similarity
Active site15481Charge relay system; for serine protease NS3 activity By similarity
Active site16081Charge relay system; for serine protease NS3 activity By similarity
Binding site25041mRNA cap By similarity
Binding site25071mRNA cap; via carbonyl oxygen By similarity
Binding site25081mRNA cap By similarity
Binding site25101mRNA cap; via carbonyl oxygen By similarity
Binding site25191mRNA cap By similarity
Binding site25461S-adenosyl-L-methionine By similarity
Binding site25761S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site25771S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site25941S-adenosyl-L-methionine By similarity
Binding site25951S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26211S-adenosyl-L-methionine By similarity
Binding site26221S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26401mRNA cap By similarity
Binding site27011mRNA cap By similarity
Binding site27031mRNA cap By similarity
Binding site27081S-adenosyl-L-methionine By similarity
Site100 – 1012Cleavage; by viral protease NS3 Potential
Site114 – 1152Cleavage; by host signal peptidase By similarity
Site205 – 2062Cleavage; by host furin Potential
Site280 – 2812Cleavage; by host signal peptidase Potential
Site773 – 7742Cleavage; by host signal peptidase Potential
Site1125 – 11262Cleavage; by host By similarity
Site1343 – 13442Cleavage; by viral protease NS3 Potential
Site1473 – 14742Cleavage; by autolysis Potential
Site2092 – 20932Cleavage; by autolysis Potential
Site2219 – 22202Cleavage; by viral protease NS3 Potential
Site2242 – 22432Cleavage; by host signal peptidase Potential
Site2490 – 24912Cleavage; by viral protease NS3 Potential
Site25151mRNA cap binding By similarity
Site25511Essential for 2'-O-methyltransferase activity By similarity
Site26361Essential for 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Site26371S-adenosyl-L-methionine binding By similarity
Site26701Essential for 2'-O-methyltransferase activity By similarity
Site27061Essential for 2'-O-methyltransferase activity By similarity

Amino acid modifications

Glycosylation1831N-linked (GlcNAc...); by host Potential
Glycosylation3471N-linked (GlcNAc...); by host Potential
Glycosylation4331N-linked (GlcNAc...); by host Potential
Glycosylation9031N-linked (GlcNAc...); by host Potential
Glycosylation9801N-linked (GlcNAc...); by host Potential
Glycosylation23001N-linked (GlcNAc...); by host Potential
Glycosylation23041N-linked (GlcNAc...); by host Potential
Glycosylation24561N-linked (GlcNAc...); by host Potential
Disulfide bond283 ↔ 310 By similarity
Disulfide bond340 ↔ 401 By similarity
Disulfide bond354 ↔ 385 By similarity
Disulfide bond372 ↔ 396 By similarity
Disulfide bond463 ↔ 563 By similarity
Disulfide bond580 ↔ 611 By similarity

Secondary structure

....................................................................................................................... 3390
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27915 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 666E8F70F1E1756E

FASTA3,390378,063
        10         20         30         40         50         60 
MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSRGLLNG QGPMKLVMAF IAFLRFLAIP 

        70         80         90        100        110        120 
PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK TSLCLMMMLP ATLAFHLTSR 

       130        140        150        160        170        180 
DGEPRMIVGK NERGKSLLFK TASGINMCTL IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC 

       190        200        210        220        230        240 
WCNLTSTWVT YGTCNQAGEH RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW 

       250        260        270        280        290        300 
ALRHPGFTIL ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW 

       310        320        330        340        350        360 
VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT DSRCPTQGEA 

       370        380        390        400        410        420 
ILPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ CLESIEGKVV QHENLKYTVI 

       430        440        450        460        470        480 
ITVHTGDQHQ VGNETQGVTA EITSQASTAE AILPEYGTLG LECSPRTGLD FNEMILLTMK 

       490        500        510        520        530        540 
NKAWMVHRQW FFDLPLPWTS GATTKTPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT 

       550        560        570        580        590        600 
ALTGATEIQT SGGTSIFAGH LKCRLKMDKL KLKGMSYAMC LNTFVLKKEV SETQHGTILI 

       610        620        630        640        650        660 
KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP FGESNIVIGI 

       670        680        690        700        710        720 
GDKALKINWY RKGSSIGKMF EATARGARRM AILGDTAWDF GSVGGVLNSL GKMVHQIFGS 

       730        740        750        760        770        780 
AYTALFSGVS WIMKIGIGVL LTWIGLNSKN TSMSFSCIAI GIITLYLGVV VQADMGCVIN 

       790        800        810        820        830        840 
WKGKELKCGS GIFVTNEVHT WTEQYKFQAD SPKRVATAIA GAWENGVCGI RSTTRMENLL 

       850        860        870        880        890        900 
WKQIANELNY ILWENDIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGLAKIVTAE 

       910        920        930        940        950        960 
TQNSSFIIDG PSTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ LCDHRLMSAA 

       970        980        990       1000       1010       1020 
VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWSNGVL ESDMIIPKSL 

      1030       1040       1050       1060       1070       1080 
AGPISQHNHR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI SENCGTRGPS LRTTTVSGKL 

      1090       1100       1110       1120       1130       1140 
IHEWCCRSCT LPPLRYMGED GCWYGMEIRP INEKEENMVK SLASAGSGKV DNFTMGVLCL 

      1150       1160       1170       1180       1190       1200 
AILFEEVMRG KFGKKHMIAG VLFTFVLLLS GQITWRGMAH TLIMIGSNAS DRMGMGVTYL 

      1210       1220       1230       1240       1250       1260 
ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMAATLR LPEDIEQMAN GIALGLMALK 

      1270       1280       1290       1300       1310       1320 
LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGI SLLPVCQSSS MRKTDWLPMT 

      1330       1340       1350       1360       1370       1380 
VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL 

      1390       1400       1410       1420       1430       1440 
LIACYVITGT SADLTVEKAA DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV 

      1450       1460       1470       1480       1490       1500 
LLKTALLIVS GIFPYSIPAT MLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ 

      1510       1520       1530       1540       1550       1560 
QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI SYGGGWRLSA 

      1570       1580       1590       1600       1610       1620 
QWQKGEEVQV IAVEPGKNPK NFQTMPGIFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV 

      1630       1640       1650       1660       1670       1680 
GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA 

      1690       1700       1710       1720       1730       1740 
IVREAIKRRL RTLILAPTRV VAAEMEEAMK GLPIRYQTTA TKSEHTGREI VDLMCHATFT 

      1750       1760       1770       1780       1790       1800 
MRLLSPVRVP NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP 

      1810       1820       1830       1840       1850       1860 
QSNAPIQDEE RDIPERSWNS GNEWITDFVG KTVWFVPSIK AGNVIANCLR KNGKKVIQLS 

      1870       1880       1890       1900       1910       1920 
RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FIADRVIDPR RCLKPVILTD GPERVILAGP 

      1930       1940       1950       1960       1970       1980 
MPVTVASAAQ RRGRVGRNPQ KENDQYIFMG QPLNKDEDHA HWTEAKMLLD NINTPEGIIP 

      1990       2000       2010       2020       2030       2040 
ALFEPEREKS AAIDGEYRLK GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG 

      2050       2060       2070       2080       2090       2100 
ERNNQILEEN MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT 

      2110       2120       2130       2140       2150       2160 
EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL GLMILLTGGA 

      2170       2180       2190       2200       2210       2220 
MLFLISGKGI GKTSIGLICV IASSGMLWMA DVPLQWIASA IVLEFFMMVL LIPEPEKQRT 

      2230       2240       2250       2260       2270       2280 
PQDNQLAYVV IGILTLAAIV AANEMGLLET TKRDLGMSKE PGVVSPTSYL DVDLHPASAW 

      2290       2300       2310       2320       2330       2340 
TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC 

      2350       2360       2370       2380       2390       2400 
YSQVNPLTLI AAVLLLVTHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV 

      2410       2420       2430       2440       2450       2460 
IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEVLTLAT GPITTLWEGS PGKFWNTTIA 

      2470       2480       2490       2500       2510       2520 
VSMANIFRGS YLAGAGLALS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK 

      2530       2540       2550       2560       2570       2580 
SGITEVDRTE AKEGLKRGEI THHAVSRGSA KLQWFVERNM VIPEGRVIDL GCGRGGWSYY 

      2590       2600       2610       2620       2630       2640 
CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES 

      2650       2660       2670       2680       2690       2700 
SPSPTVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS 

      2710       2720       2730       2740       2750       2760 
RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET 

      2770       2780       2790       2800       2810       2820 
PNMDVIGERI KRIKEEHSST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP 

      2830       2840       2850       2860       2870       2880 
WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRPMPGTR KVMEITAEWL WRTLGRNKRP 

      2890       2900       2910       2920       2930       2940 
RLCTREEFTK KVRTNAAMGA VFTEENQWDS ARAAVEDEEF WKLVDREREL HKLGKCGSCV 

      2950       2960       2970       2980       2990       3000 
YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG 

      3010       3020       3030       3040       3050       3060 
LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH RQLANAIFKL 

      3070       3080       3090       3100       3110       3120 
TYQNKVVKVQ RPTPKGTVMD IISRKDQRGS GQVGTYGLNT FTNMEAQLIR QMEGEGVLSK 

      3130       3140       3150       3160       3170       3180 
ADLENPHPLE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD 

      3190       3200       3210       3220       3230       3240 
IPQWQPSKGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE 

      3250       3260       3270       3280       3290       3300 
TACLGKAYAQ MWTLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML 

      3310       3320       3330       3340       3350       3360 
TVWNRVWIED NPWMEDKTPV TTWEDVPYLG KREDQWCGSL IGLTSRATWA QNILTAIQQV 

      3370       3380       3390 
RSLIGNEEFL DYMPSMKRFR KEEESEGAIW 

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References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93130 Genomic RNA. Translation: AAA99437.1.
PIRGNWVD3. A34774.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP27915.
SMRP27915. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS07.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR011492. 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.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF01003. 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]
PIRSFPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsTIGR04240. flavi_E_stem. 1 hit.
PROSITEPS51527. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP27915.
PROP27915.

Entry information

Entry namePOLG_DEN3P
AccessionPrimary (citable) accession number: P27915
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references