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P09866 (POLG_DEN4D) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 123. 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
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 4 (strain Dominica/814669/1981) (DENV-4) [Complete proteome]
Taxonomic identifier408871 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Dengue virus group
Virus hostAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Culex albopictus) [TaxID: 7160]
Homo sapiens (Human) [TaxID: 9606]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]

Protein attributes

Sequence length3387 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 an 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, functionning 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 + m7G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA.

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-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

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

Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

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.

Domain

Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals By similarity.

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. Ref.5

RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization By similarity.

Envelope protein E and non-structural protein 1 are N-glycosylated By similarity.

Sequence similarities

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 peptidase S7 domain.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processClathrin-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 STAT2 by virus
Inhibition of host TYK2 by virus
Inhibition of host innate immune response by virus
Inhibition of host interferon signaling pathway by virus
Initiation of viral infection
RNA replication
Transcription
Transcription regulation
Viral attachment to host cell
Viral immunoevasion
Viral penetration into host cytoplasm
Virus endocytosis by host
   Cellular componentHost endoplasmic reticulum
Host membrane
Host nucleus
Membrane
Secreted
Viral envelope protein
Virion
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionCapsid protein
Helicase
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
Multifunctional enzyme
Gene Ontology (GO)
   Biological processevasion by virus of host immune response

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular componenthost cell endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: InterPro

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: EC

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

Inferred from electronic annotation. Source: 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 – 33863386Genome polyprotein
PRO_0000405226
Chain1 – 9999Capsid protein C By similarity
PRO_0000038000
Propeptide100 – 11314ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000038001
Chain114 – 279166prM By similarity
PRO_0000308297
Chain114 – 20491Peptide pr By similarity
PRO_0000308298
Chain205 – 27975Small envelope protein M By similarity
PRO_0000038002
Chain280 – 774495Envelope protein E By similarity
PRO_0000038003
Chain775 – 1126352Non-structural protein 1 By similarity
PRO_0000038004
Chain1127 – 1344218Non-structural protein 2A By similarity
PRO_0000038005
Chain1127 – ?Non-structural protein 2A-alpha By similarityPRO_0000308299
Chain1345 – 1474130Serine protease subunit NS2B By similarity
PRO_0000038006
Chain1475 – 2092618Serine protease NS3 By similarity
PRO_0000038007
Chain2093 – 2219127Non-structural protein 4A By similarity
PRO_0000038008
Peptide2220 – 224223Peptide 2k By similarity
PRO_0000308300
Chain2243 – 2487245Non-structural protein 4B By similarity
PRO_0000038009
Chain2488 – 3387900RNA-directed RNA polymerase NS5 By similarity
PRO_0000038010

Regions

Topological domain1 – 100100Cytoplasmic Potential
Transmembrane101 – 11717Helical; Potential
Topological domain118 – 237120Extracellular Potential
Transmembrane238 – 25821Helical; Potential
Topological domain259 – 2657Cytoplasmic Potential
Transmembrane266 – 27914Helical; Potential
Topological domain280 – 725446Extracellular Potential
Intramembrane726 – 74621Helical; Potential
Topological domain747 – 7515Extracellular Potential
Intramembrane752 – 77221Helical; Potential
Topological domain773 – 1156384Extracellular Potential
Transmembrane1157 – 117721Helical; Potential
Topological domain1178 – 119720Cytoplasmic Potential
Transmembrane1198 – 121821Helical; Potential
Topological domain1219 – 124426Lumenal Potential
Transmembrane1245 – 126521Helical; Potential
Topological domain1266 – 128520Cytoplasmic Potential
Transmembrane1286 – 130621Helical; Potential
Topological domain1307 – 131610Lumenal Potential
Transmembrane1317 – 133721Helical; Potential
Topological domain1338 – 13458Cytoplasmic Potential
Transmembrane1346 – 136621Helical; Potential
Topological domain1367 – 13693Lumenal Potential
Transmembrane1370 – 139021Helical; Potential
Topological domain1391 – 143747Cytoplasmic Potential
Intramembrane1438 – 145821Helical; Potential
Topological domain1459 – 2143685Cytoplasmic Potential
Transmembrane2144 – 216421Helical; Potential
Topological domain2165 – 21695Lumenal Potential
Intramembrane2170 – 219021Helical; Potential
Topological domain21911Lumenal Potential
Transmembrane2192 – 221221Helical; Potential
Topological domain2213 – 222513Cytoplasmic Potential
Transmembrane2226 – 224621Helical; Note=Signal for NS4B; Potential
Topological domain2247 – 227327Lumenal Potential
Intramembrane2274 – 229118Helical; Potential
Topological domain2292 – 230110Lumenal Potential
Intramembrane2302 – 232221Helical; Potential
Topological domain2323 – 234321Lumenal Potential
Transmembrane2344 – 236421Helical; Potential
Topological domain2365 – 240945Cytoplasmic Potential
Transmembrane2410 – 243021Helical; Potential
Topological domain2431 – 245525Lumenal Potential
Transmembrane2456 – 247621Helical; Potential
Topological domain2477 – 3387911Cytoplasmic Potential
Domain1475 – 1652178Peptidase S7
Domain1654 – 1810157Helicase ATP-binding
Domain1820 – 1987168Helicase C-terminal
Domain3016 – 3166151RdRp catalytic
Nucleotide binding1667 – 16748ATP Potential
Region32 – 7342Hydrophobic; homodimerization of capsid protein C By similarity
Region1397 – 143640Interacts with and activates NS3 protease By similarity
Motif1758 – 17614DEAH box

Sites

Active site15251Charge relay system; for serine protease NS3 activity By similarity
Active site15491Charge relay system; for serine protease NS3 activity By similarity
Active site16091Charge relay system; for serine protease NS3 activity By similarity
Active site25481For 2'-O-methyltransferase activity By similarity
Active site26331For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Active site26681For 2'-O-methyltransferase activity By similarity
Active site27041For 2'-O-methyltransferase activity By similarity
Site99 – 1002Cleavage; by viral protease NS3 Potential
Site113 – 1142Cleavage; by host signal peptidase By similarity
Site204 – 2052Cleavage; by host furin Potential
Site279 – 2802Cleavage; by host signal peptidase Potential
Site774 – 7752Cleavage; by host signal peptidase Potential
Site1126 – 11272Cleavage; by host By similarity
Site1344 – 13452Cleavage; by viral protease NS3 Potential
Site1474 – 14752Cleavage; by autolysis Potential
Site2092 – 20932Cleavage; by autolysis Potential
Site2219 – 22202Cleavage; by viral protease NS3 Potential
Site2242 – 22432Cleavage; by host signal peptidase Potential
Site2487 – 24882Cleavage; by viral protease NS3 Potential

Amino acid modifications

Glycosylation1821N-linked (GlcNAc...); by host
Glycosylation3461N-linked (GlcNAc...); by host Potential
Glycosylation4321N-linked (GlcNAc...); by host Potential
Glycosylation9041N-linked (GlcNAc...); by host Potential
Glycosylation9811N-linked (GlcNAc...); by host Potential
Glycosylation22971N-linked (GlcNAc...); by host Potential
Glycosylation23011N-linked (GlcNAc...); by host Potential
Glycosylation24531N-linked (GlcNAc...); by host Potential
Disulfide bond282 ↔ 309 By similarity
Disulfide bond339 ↔ 400 By similarity
Disulfide bond353 ↔ 384 By similarity
Disulfide bond371 ↔ 395 By similarity
Disulfide bond464 ↔ 564 By similarity
Disulfide bond581 ↔ 612 By similarity

Experimental info

Sequence conflict7801A → V in AAG45436. Ref.2
Sequence conflict7801A → V in AAK01233. Ref.2
Sequence conflict14181I → V in AAG45435. Ref.2
Sequence conflict19091P → T in AAK01233. Ref.2
Sequence conflict20321K → E in AAG45435. Ref.2
Sequence conflict23511V → A in AAG45436. Ref.2
Sequence conflict23541L → F in AAG45437. Ref.2
Sequence conflict25101K → R in AAK01233. Ref.2
Sequence conflict27361K → R in AAG45436. Ref.2

Secondary structure

1 ..................... 3387
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09866 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: 0CE81B6E7DEFDB5E

FASTA3,387378,385
        10         20         30         40         50         60 
MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI TFLRVLSIPP 

        70         80         90        100        110        120 
TAGILKRWGQ LKKNKAIKIL IGFRKEIGRM LNILNGRKRS TITLLCLIPT VMAFSLSTRD 

       130        140        150        160        170        180 
GEPLMIVAKH ERGRPLLFKT TEGINKCTLI AMDLGEMCED TVTYKCPLLV NTEPEDIDCW 

       190        200        210        220        230        240 
CNLTSTWVMY GTCTQSGERR REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI 

       250        260        270        280        290        300 
LRNPGFALLA GFMAYMIGQT GIQRTVFFVL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV 

       310        320        330        340        350        360 
DLVLEHGGCV TTMAQGKPTL DFELTKTTAK EVALLRTYCI EASISNITTA TRCPTQGEPY 

       370        380        390        400        410        420 
LKEEQDQQYI CRRDVVDRGW GNGCGLFGKG GVVTCAKFSC SGKITGNLVQ IENLEYTVVV 

       430        440        450        460        470        480 
TVHNGDTHAV GNDTSNHGVT AMITPRSPSV EVKLPDYGEL TLDCEPRSGI DFNEMILMKM 

       490        500        510        520        530        540 
KKKTWLVHKQ WFLDLPLPWT AGADTSEVHW NYKERMVTFK VPHAKRQDVT VLGSQEGAMH 

       550        560        570        580        590        600 
SALAGATEVD SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV 

       610        620        630        640        650        660 
VKVKYEGAGA PCKVPIEIRD VNKEKVVGRI ISSTPLAENT NSVTNIELEP PFGDSYIVIG 

       670        680        690        700        710        720 
VGNSALTLHW FRKGSSIGKM FESTYRGAKR MAILGETAWD FGSVGGLFTS LGKAVHQVFG 

       730        740        750        760        770        780 
SVYTTMFGGV SWMIRILIGF LVLWIGTNSR NTSMAMTCIA VGGITLFLGF TVQADMGCVA 

       790        800        810        820        830        840 
SWSGKELKCG SGIFVVDNVH TWTEQYKFQP ESPARLASAI LNAHKDGVCG IRSTTRLENV 

       850        860        870        880        890        900 
MWKQITNELN YVLWEGGHDL TVVAGDVKGV LTKGKRALTP PVSDLKYSWK TWGKAKIFTP 

       910        920        930        940        950        960 
EARNSTFLID GPDTSECPNE RRAWNSLEVE DYGFGMFTTN IWMKFREGSS EVCDHRLMSA 

       970        980        990       1000       1010       1020 
AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP KTHTLWSNGV LESQMLIPKS 

      1030       1040       1050       1060       1070       1080 
YAGPFSQHNY RQGYATQTVG PWHLGKLEID FGECPGTTVT IQEDCDHRGP SLRTTTASGK 

      1090       1100       1110       1120       1130       1140 
LVTQWCCRSC TMPPLRFLGE DGCWYGMEIR PLSEKEENMV KSQVTAGQGT SETFSMGLLC 

      1150       1160       1170       1180       1190       1200 
LTLFVEECLR RRVTRKHMIL VVVITLCAII LGGLTWMDLL RALIMLGDTM SGRIGGQIHL 

      1210       1220       1230       1240       1250       1260 
AIMAVFKMSP GYVLGVFLRK LTSRETALMV IGMAMTTVLS IPHDLMELID GISLGLILLK 

      1270       1280       1290       1300       1310       1320 
IVTQFDNTQV GTLALSLTFI RSTMPLVMAW RTIMAVLFVV TLIPLCRTSC LQKQSHWVEI 

      1330       1340       1350       1360       1370       1380 
TALILGAQAL PVYLMTLMKG ASRRSWPLNE GIMAVGLVSL LGSALLKNDV PLAGPMVAGG 

      1390       1400       1410       1420       1430       1440 
LLLAAYVMSG SSADLSLEKA ANVQWDEMAD ITGSSPIIEV KQDEDGSFSI RDVEETNMIT 

      1450       1460       1470       1480       1490       1500 
LLVKLALITV SGLYPLAIPV TMTLWYMWQV KTQRSGALWD VPSPAATKKA ALSEGVYRIM 

      1510       1520       1530       1540       1550       1560 
QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHETGRLE PSWADVRNDM ISYGGGWRLG 

      1570       1580       1590       1600       1610       1620 
DKWDKEEDVQ VLAIEPGKNP KHVQTKPGLF KTLTGEIGAV TLDFKPGTSG SPIINRKGKV 

      1630       1640       1650       1660       1670       1680 
IGLYGNGVVT KSGDYVSAIT QAERIGEPDY EVDEDIFRKK RLTIMDLHPG AGKTKRILPS 

      1690       1700       1710       1720       1730       1740 
IVREALKRRL RTLILAPTRV VAAEMEEALR GLPIRYQTPA VKSEHTGREI VDLMCHATFT 

      1750       1760       1770       1780       1790       1800 
TRLLSSTRVP NYNLIVMDEA HFTDPSSVAA RGYISTRVEM GEAAAIFMTA TPPGATDPFP 

      1810       1820       1830       1840       1850       1860 
QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR KSGKKVIQLS 

      1870       1880       1890       1900       1910       1920 
RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR RCLKPVILPD GPERVILAGP 

      1930       1940       1950       1960       1970       1980 
IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG DPLKNDEDHA HWTEAKMLLD NIYTPEGIIP 

      1990       2000       2010       2020       2030       2040 
TLFGPEREKT QAIDGEFRLR GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG 

      2050       2060       2070       2080       2090       2100 
ERNNQILEEN MEVEIWTREG EKKKLRPRWL DARVYADPMA LKDFKEFASG RKSITLDILT 

      2110       2120       2130       2140       2150       2160 
EIASLPTYLS SRAKLALDNI VMLHTTERGG RAYQHALNEL PESLETLMLV ALLGAMTAGI 

      2170       2180       2190       2200       2210       2220 
FLFFMQGKGI GKLSMGLITI AVASGLLWVA EIQPQWIAAS IILEFFLMVL LIPEPEKQRT 

      2230       2240       2250       2260       2270       2280 
PQDNQLIYVI LTILTIIGLI AANEMGLIEK TKTDFGFYQV KTETTILDVD LRPASAWTLY 

      2290       2300       2310       2320       2330       2340 
AVATTILTPM LRHTIENTSA NLSLAAIANQ AAVLMGLGKG WPLHRMDLGV PLLAMGCYSQ 

      2350       2360       2370       2380       2390       2400 
VNPTTLTASL VMLLVHYAII GPGLQAKATR EAQKRTAAGI MKNPTVDGIT VIDLEPISYD 

      2410       2420       2430       2440       2450       2460 
PKFEKQLGQV MLLVLCAGQL LLMRTTWAFC EVLTLATGPI LTLWEGNPGR FWNTTIAVST 

      2470       2480       2490       2500       2510       2520 
ANIFRGSYLA GAGLAFSLIK NAQTPRRGTG TTGETLGEKW KRQLNSLDRK EFEEYKRSGI 

      2530       2540       2550       2560       2570       2580 
LEVDRTEAKS ALKDGSKIKH AVSRGSSKIR WIVERGMVKP KGKVVDLGCG RGGWSYYMAT 

      2590       2600       2610       2620       2630       2640 
LKNVTEVKGY TKGGPGHEEP IPMATYGWNL VKLHSGVDVF YKPTEQVDTL LCDIGESSSN 

      2650       2660       2670       2680       2690       2700 
PTIEEGRTLR VLKMVEPWLS SKPEFCIKVL NPYMPTVIEE LEKLQRKHGG NLVRCPLSRN 

      2710       2720       2730       2740       2750       2760 
STHEMYWVSG ASGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDVDLGAGTR SVSTETEKPD 

      2770       2780       2790       2800       2810       2820 
MTIIGRRLQR LQEEHKETWH YDQENPYRTW AYHGSYEAPS TGSASSMVNG VVKLLTKPWD 

      2830       2840       2850       2860       2870       2880 
VIPMVTQLAM TDTTPFGQQR VFKEKVDTRT PQPKPGTRMV MTTTANWLWA LLGKKKNPRL 

      2890       2900       2910       2920       2930       2940 
CTREEFISKV RSNAAIGAVF QEEQGWTSAS EAVNDSRFWE LVDKERALHQ EGKCESCVYN 

      2950       2960       2970       2980       2990       3000 
MMGKREKKLG EFGRAKGSRA IWYMWLGARF LEFEALGFLN EDHWFGRENS WSGVEGEGLH 

      3010       3020       3030       3040       3050       3060 
RLGYILEEID KKDGDLMYAD DTAGWDTRIT EDDLQNEELI TEQMAPHHKI LAKAIFKLTY 

      3070       3080       3090       3100       3110       3120 
QNKVVKVLRP TPRGAVMDII SRKDQRGSGQ VGTYGLNTFT NMEVQLIRQM EAEGVITQDD 

      3130       3140       3150       3160       3170       3180 
MQNPKGLKER VEKWLKECGV DRLKRMAISG DDCVVKPLDE RFGTSLLFLN DMGKVRKDIP 

      3190       3200       3210       3220       3230       3240 
QWEPSKGWKN WQEVPFCSHH FHKIFMKDGR SLVVPCRNQD ELIGRARISQ GAGWSLRETA 

      3250       3260       3270       3280       3290       3300 
CLGKAYAQMW SLMYFHRRDL RLASMAICSA VPTEWFPTSR TTWSIHAHHQ WMTTEDMLKV 

      3310       3320       3330       3340       3350       3360 
WNRVWIEDNP NMTDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN IHTAITQVRN 

      3370       3380 
LIGKEEYVDY MPVMKRYSAP SESEGVL

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References

[1]Yamashiro T., Shameem G., Lai C.-J.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION.
[2]"A live attenuated dengue virus type 4 vaccine candidate with a 30 nucleotide deletion in the 3' untranslated region is highly attenuated and immunogenic in humans."
Durbin A.P., Karron R.A., Sun W., Vaughn D.W., Reynolds M.J., Perreault J.R., Men R.H., Lai C.-J., Elkins W.R., Chanock R.M., Murphy B.R., Whitehead S.S.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Cloning full-length dengue type 4 viral DNA sequences: analysis of genes coding for structural proteins."
Zhao B., Mackow E., Buckler-White A., Markoff L., Chancock R.M., Lai C.-J., Makino Y.
Virology 155:77-88(1986) [PubMed: 3022479] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-777.
[4]"The nucleotide sequence of dengue type 4 virus: analysis of genes coding for nonstructural proteins."
Mackow E., Makino Y., Zhao B., Zhang Y.M., Markoff L., Buckler-White A., Guiler M., Chanock R., Lai C.-J.
Virology 159:217-228(1987) [PubMed: 3039728] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 775-3387.
[5]"In vitro processing of dengue virus structural proteins: cleavage of the pre-membrane protein."
Markoff L.
J. Virol. 63:3345-3352(1989) [PubMed: 2501515] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF THE M PROTEIN.
Strain: 814669.
[6]"Solution structure of the envelope protein domain III of dengue-4 virus."
Volk D.E., Lee Y.C., Li X., Thiviyanathan V., Gromowski G.D., Li L., Lamb A.R., Beasley D.W., Barrett A.D., Gorenstein D.G.
Virology 364:147-154(2007) [PubMed: 17395234] [Abstract]
Cited for: STRUCTURE BY NMR OF 568-679.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M14931 Genomic RNA. Translation: AAA42964.2.
AF326825 Genomic RNA. Translation: AAG45435.1.
AF326826 Genomic RNA. Translation: AAG45436.1.
AF326827 Genomic RNA. Translation: AAG45437.1.
AF326573 Genomic RNA. Translation: AAK01233.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0PNMR-A568-679[»]
ProteinModelPortalP09866.
SMRP09866. Positions 20-99, 114-194, 280-679, 1493-2092, 2494-2755, 2761-3371.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR014001. DEAD-like_helicase.
IPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013756. Flav_glyE_cen_dom_subdom2.
IPR013754. Flav_glyE_dim.
IPR001122. Flavi_capsidC.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flv_glyE_Ig-like.
IPR014412. Gen_Poly_FLV.
IPR011999. GlycoprotE_cen/dimer_Flavivir.
IPR011998. GlycoprotE_cen/dimer_vir.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR001850. Peptidase_S7.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_RrmJ/FtsJ.
[Graphical view]
Gene3DG3DSA:3.30.67.10. Flav_glyE_cen_2. 1 hit.
G3DSA:2.60.98.10. Flav_glyE_dim. 3 hits.
G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.
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.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMSSF56983. Flavi_glycoprotE. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. False negative.
PS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. False negative.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_DEN4D
AccessionPrimary (citable) accession number: P09866
Secondary accession number(s): Q88661 expand/collapse secondary AC list , Q88662, Q88663, Q88664, Q88665, Q88666, Q88667, Q88668, Q88669, Q88670, Q88671, Q99BK4, Q9DKQ5, Q9DKQ6, Q9DKQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 16, 2004
Last modified: November 16, 2011
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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