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P12823 (POLG_DEN2P) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. 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
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 2 (strain Puerto Rico/PR159-S1/1969) (DENV-2) [Complete proteome]
Taxonomic identifier11066 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Dengue virus group
Virus hostErythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
Diceromyia [TaxID: 53539]
Aedimorphus [TaxID: 53540]
Stegomyia [TaxID: 53541]

Protein attributes

Sequence length3388 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.

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 – 33883388Genome polyprotein
PRO_0000405217
Chain1 – 100100Capsid protein C By similarity
PRO_0000037969
Propeptide101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000037970
Chain115 – 280166prM By similarity
PRO_0000308286
Chain115 – 20591Peptide pr By similarity
PRO_0000308287
Chain206 – 28075Small envelope protein M By similarity
PRO_0000037971
Chain281 – 775495Envelope protein E By similarity
PRO_0000037972
Chain776 – 1127352Non-structural protein 1 By similarity
PRO_0000037973
Chain1128 – 1345218Non-structural protein 2A By similarity
PRO_0000037974
Chain1128 – 1315188Non-structural protein 2A-alpha By similarity
PRO_0000308288
Chain1346 – 1475130Serine protease subunit NS2B By similarity
PRO_0000037975
Chain1476 – 2090615Serine protease NS3 By similarity
PRO_0000037976
Chain2091 – 2217127Non-structural protein 4A By similarity
PRO_0000037977
Peptide2218 – 224023Peptide 2k By similarity
PRO_0000308289
Chain2241 – 2488248Non-structural protein 4B By similarity
PRO_0000037978
Chain2489 – 3388900RNA-directed RNA polymerase NS5 By similarity
PRO_0000037979

Regions

Topological domain1 – 101101Cytoplasmic Potential
Transmembrane102 – 12221Helical; Potential
Topological domain123 – 238116Extracellular Potential
Transmembrane239 – 25921Helical; Potential
Topological domain260 – 2656Cytoplasmic Potential
Transmembrane266 – 28015Helical; Potential
Topological domain281 – 725445Extracellular Potential
Intramembrane726 – 74621Helical; Potential
Topological domain747 – 7526Extracellular Potential
Intramembrane753 – 77321Helical; Potential
Topological domain774 – 1124351Extracellular Potential
Transmembrane1125 – 114521Helical; Potential
Topological domain1146 – 115611Cytoplasmic Potential
Transmembrane1157 – 117721Helical; Potential
Topological domain1178 – 11847Lumenal Potential
Transmembrane1185 – 120521Helical; Potential
Topological domain1206 – 127166Cytoplasmic Potential
Transmembrane1272 – 129221Helical; Potential
Topological domain1293 – 131725Lumenal Potential
Transmembrane1318 – 133821Helical; Potential
Topological domain1339 – 13468Cytoplasmic Potential
Transmembrane1347 – 136721Helical; Potential
Topological domain1368 – 13703Lumenal Potential
Transmembrane1371 – 139121Helical; Potential
Topological domain1392 – 144756Cytoplasmic Potential
Intramembrane1448 – 146821Helical; Potential
Topological domain1469 – 2144676Cytoplasmic Potential
Transmembrane2145 – 216521Helical; Potential
Topological domain2166 – 21672Lumenal Potential
Intramembrane2168 – 218821Helical; Potential
Topological domain21891Lumenal Potential
Transmembrane2190 – 221021Helical; Potential
Topological domain2211 – 222515Cytoplasmic Potential
Transmembrane2226 – 224621Helical; Note=Signal for NS4B; Potential
Topological domain2247 – 227428Lumenal Potential
Intramembrane2275 – 229218Helical; Potential
Topological domain2293 – 231321Lumenal Potential
Intramembrane2314 – 233421Helical; Potential
Topological domain2335 – 234410Lumenal Potential
Transmembrane2345 – 236521Helical; Potential
Topological domain2366 – 241045Cytoplasmic Potential
Transmembrane2411 – 243121Helical; Potential
Topological domain2432 – 245625Lumenal Potential
Transmembrane2457 – 247721Helical; Potential
Topological domain2478 – 3388911Cytoplasmic Potential
Domain1476 – 1653178Peptidase S7
Domain1655 – 1811157Helicase ATP-binding
Domain1821 – 1988168Helicase C-terminal
Domain3017 – 3166150RdRp catalytic
Nucleotide binding1668 – 16758ATP Potential
Region33 – 7442Hydrophobic; homodimerization of capsid protein C By similarity
Region1398 – 143740Interacts with and activates NS3 protease By similarity
Motif1759 – 17624DEAH box
Compositional bias97 – 1004Poly-Arg
Compositional bias1434 – 14374Poly-Glu
Compositional bias2145 – 21517Poly-Leu
Compositional bias2351 – 23544Poly-Leu
Compositional bias3380 – 33834Poly-Glu

Sites

Active site15261Charge relay system; for serine protease NS3 activity By similarity
Active site15501Charge relay system; for serine protease NS3 activity By similarity
Active site16101Charge relay system; for serine protease NS3 activity By similarity
Active site25491For 2'-O-methyltransferase activity By similarity
Active site26341For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Active site26691For 2'-O-methyltransferase activity By similarity
Active site27051For 2'-O-methyltransferase activity 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
Site775 – 7762Cleavage; by host signal peptidase Potential
Site1127 – 11282Cleavage; by host By similarity
Site1345 – 13462Cleavage; by viral protease NS3 Potential
Site1475 – 14762Cleavage; by autolysis Potential
Site2090 – 20912Cleavage; by autolysis Potential
Site2217 – 22182Cleavage; by viral protease NS3 Potential
Site2240 – 22412Cleavage; by host signal peptidase Potential
Site2488 – 24892Cleavage; by viral protease NS3 Potential

Amino acid modifications

Glycosylation1831N-linked (GlcNAc...); by host Potential
Glycosylation3471N-linked (GlcNAc...); by host Potential
Glycosylation4331N-linked (GlcNAc...); by host Potential
Glycosylation9051N-linked (GlcNAc...); by host Potential
Glycosylation9821N-linked (GlcNAc...); by host Potential
Glycosylation22981N-linked (GlcNAc...); by host Potential
Glycosylation23021N-linked (GlcNAc...); by host Potential
Disulfide bond283 ↔ 310 Ref.4
Disulfide bond340 ↔ 401 Ref.4
Disulfide bond354 ↔ 385 Ref.4
Disulfide bond372 ↔ 396 Ref.4
Disulfide bond465 ↔ 565 Ref.4
Disulfide bond582 ↔ 613 Ref.4

Experimental info

Sequence conflict3511D → E Ref.4
Sequence conflict6151T → I Ref.4
Sequence conflict6321T → I Ref.4
Sequence conflict6701D → N Ref.4

Secondary structure

1 ........................................................................................................................... 3388
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12823 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 79B7C87BE64D2D8F

FASTA3,388379,219
        10         20         30         40         50         60 
MNDQRKKARN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL VAFLRFLTIP 

        70         80         90        100        110        120 
PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR TAGMIIMLIP TVMAFHLTTR 

       130        140        150        160        170        180 
NGEPHMIVSR QEKGKSLLFK TKDGTNMCTL MAMDLGELCE DTITYKCPFL KQNEPEDIDC 

       190        200        210        220        230        240 
WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW 

       250        260        270        280        290        300 
ILRHPGFTIM AAILAYTIGT THFQRVLIFI LLTAIAPSMT MRCIGISNRD FVEGVSGGSW 

       310        320        330        340        350        360 
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT DSRCPTQGEP 

       370        380        390        400        410        420 
TLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMEGKIV QPENLEYTVV 

       430        440        450        460        470        480 
ITPHSGEEHA VGNDTGKHGK EVKITPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ 

       490        500        510        520        530        540 
MKDKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM 

       550        560        570        580        590        600 
HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI 

       610        620        630        640        650        660 
VIRVQYEGDG SPCKTPFEIM DLEKRHVLGR LTTVNPIVTE KDSPVNIEAE PPFGDSYIII 

       670        680        690        700        710        720 
GVEPGQLKLD WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF 

       730        740        750        760        770        780 
GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV LVGIVTLYLG VMVQADSGCV 

       790        800        810        820        830        840 
VSWKNKELKC GSGIFVTDNV HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN 

       850        860        870        880        890        900 
LMWKQITSEL NHILSENEVK LTIMTGDIKG IMQVGKRSLR PQPTELRYSW KTWGKAKMLS 

       910        920        930        940        950        960 
TELHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLRLREKQ DAFCDSKLMS 

       970        980        990       1000       1010       1020 
AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW PKSHTLWSNG VLESEMVIPK 

      1030       1040       1050       1060       1070       1080 
NFAGPVSQHN NRPGYHTQTA GPWHLGKLEM DFDFCEGTTV VVTEDCGNRG PSLRTTTASG 

      1090       1100       1110       1120       1130       1140 
KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VSSLVTAGHG QIDNFSLGIL 

      1150       1160       1170       1180       1190       1200 
GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT 

      1210       1220       1230       1240       1250       1260 
YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ SSIPETILEL TDALALGMMV 

      1270       1280       1290       1300       1310       1320 
LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLFLT SSQQKADWIP 

      1330       1340       1350       1360       1370       1380 
LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND TPMTGPLVAG 

      1390       1400       1410       1420       1430       1440 
GLLTVCYVLT GRSADLELER ATDVKWDDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL 

      1450       1460       1470       1480       1490       1500 
TILIRTGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPVGK AELEDGAYRI 

      1510       1520       1530       1540       1550       1560 
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL 

      1570       1580       1590       1600       1610       1620 
EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FRTNTGTIGA VSLDFSPGTS GSPIVDKKGK 

      1630       1640       1650       1660       1670       1680 
VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP 

      1690       1700       1710       1720       1730       1740 
AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF 

      1750       1760       1770       1780       1790       1800 
TMRLLSPIRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF 

      1810       1820       1830       1840       1850       1860 
PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KTGNDIAACL RKNGKRVIQL 

      1870       1880       1890       1900       1910       1920 
SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG 

      1930       1940       1950       1960       1970       1980 
PMPVTHSSAA QRRGRIGRNP RNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII 

      1990       2000       2010       2020       2030       2040 
PSMFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI NYADRRWCFD 

      2050       2060       2070       2080       2090       2100 
GTRNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFAAGRK SLTLNLITEM 

      2110       2120       2130       2140       2150       2160 
GRLPTFMTQK ARDALDNLAV LHTAEAGGKA YNHALSELPE TLETLLLLTL LATVTGGIFL 

      2170       2180       2190       2200       2210       2220 
FLMSGRGIGK MTLGMCCIIT ASILLWYAQI QPHWIAASII LEFFLIVLLI PEPEKQRTPQ 

      2230       2240       2250       2260       2270       2280 
DNQLTYVIIA ILTVVAATMA NEMGFLEKTK KDLGLGNIAT QQPESNILDI DLRPASAWTL 

      2290       2300       2310       2320       2330       2340 
YAVATTFITP MLRHSIENSS VNVSLTAIAN QATVLMGLGK GWPLSKMDIG VPLLAIGCYS 

      2350       2360       2370       2380       2390       2400 
QVNPITLTAA LLLLVAHYAI IGPGLQAKAT REAQKRAAAG IMKNPTVDGI TVIDLDPIPY 

      2410       2420       2430       2440       2450       2460 
DPKFEKQLGQ VMLLVLCVTQ VLMMRTTWAL CEALTLATGP VSTLWEGNPG RFWNTTIAVS 

      2470       2480       2490       2500       2510       2520 
MANIFRGSYL AGAGLLFSIM KNTTSTRRGT GNIGETLGEK WKSRLNALGK SEFQIYKKSG 

      2530       2540       2550       2560       2570       2580 
IQEVDRTLAK EGIKRGETDH HAVSRGSAKL RWFVERNLVT PEGKVVDLGC GRGGWSYYCG 

      2590       2600       2610       2620       2630       2640 
GLKNVREVKG LTKGGPGHEE PIPMSTYGWN LVRLQSGVDV FFVPPEKCDT LLCDIGESSP 

      2650       2660       2670       2680       2690       2700 
NPTVEAGRTL RVLNLVENWL NNNTQFCVKV LNPYMPSVIE RMETLQRKYG GALVRNPLSR 

      2710       2720       2730       2740       2750       2760 
NSTHEMYWVS NASGNIVSSV NMISRMLINR FTMRHKKATY EPDVDLGSGT RNIGIESETP 

      2770       2780       2790       2800       2810       2820 
NLDIIGKRIE KIKQEHETSW HYDQDHPYKT WAYHGSYETK QTGSASSMVN GVVRLLTKPW 

      2830       2840       2850       2860       2870       2880 
DVVPMVTQMA MTDTTPFGQQ RVFKEKVDTR TQEPKEGTKK LMKITAEWLW KELGKKKTPR 

      2890       2900       2910       2920       2930       2940 
MCTREEFTKK VRSNAALGAI FTDENKWKSA REAVEDSRFW ELVDKERNLH LEGKCETCVY 

      2950       2960       2970       2980       2990       3000 
NMMGKREKKL GEFGKAKGSR AIWYMWLGAR FLEFEALGFL NEDHWFSREN SLSGVEGEGL 

      3010       3020       3030       3040       3050       3060 
HKLGYILREV SKKEGGAMYA DDTAGWDTRI TIEDLKNEEM ITNHMAGEHK KLAEAIFKLT 

      3070       3080       3090       3100       3110       3120 
YQNKVVRVQR PTPRGTVMDI ISRRDQRGSG QVGTYGLNTF TNMEAQLIRQ MEGEGIFKSI 

      3130       3140       3150       3160       3170       3180 
QHLTASEEIA VQDWLARVGR ERLSRMAISG DDCVVKPLDD RFARALTALN DMGKVRKDIQ 

      3190       3200       3210       3220       3230       3240 
QWEPSRGWND WTQVPFCSHH FHELIMKDGR TLVVPCRNQD ELIGRARISQ GAGWSLRETA 

      3250       3260       3270       3280       3290       3300 
CLGKSYAQMW SLMYFHRRDL RLAANAICSA VPSHWVPTSR TTWSIHASHE WMTTEDMLTV 

      3310       3320       3330       3340       3350       3360 
WNKVWILENP WMEDKTPVES WEEIPYLGKR EDQWCGSLIG LTSRATWAKN IQTAINQVRS 

      3370       3380 
LIGNEEYTDY MPSMKRFRRE EEEAGVLW

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References

[1]"Nucleotide sequence of dengue 2 RNA and comparison of the encoded proteins with those of other flaviviruses."
Hahn Y.S., Galler R., Hunkapiller T., Dalrymple J.M., Strauss J.H., Strauss E.G.
Virology 162:167-180(1988) [PubMed: 2827375] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Definition of the carboxy termini of the three glycoproteins specified by dengue virus type 2."
Wright P.J., Cauchi M.R., Ng M.L.
Virology 171:61-67(1989) [PubMed: 2741348] [Abstract]
Cited for: C-TERMINUS OF M; E AND NS1.
Strain: New-Guinea.
[3]"An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization."
Egloff M.P., Benarroch D., Selisko B., Romette J.L., Canard B.
EMBO J. 21:2757-2768(2002) [PubMed: 12032088] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2494-2783 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, CHARACTERIZATION OF METHYLTRANSFERASE ACTIVITY.
[4]"A ligand-binding pocket in the dengue virus envelope glycoprotein."
Modis Y., Ogata S., Clements D., Harrison S.C.
Proc. Natl. Acad. Sci. U.S.A. 100:6986-6991(2003) [PubMed: 12759475] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 281-674, DISULFIDE BONDS.
[5]"Structures of immature flavivirus particles."
Zhang Y., Corver J., Chipman P.R., Zhang W., Pletnev S.V., Sedlak D., Baker T.S., Strauss J.H., Kuhn R.J., Rossmann M.G.
EMBO J. 22:2604-2613(2003) [PubMed: 12773377] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (16 ANGSTROMS) OF IMMATURE PARTICLES.
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Pathogen Resource

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M19197 Genomic RNA. Translation: AAA42962.1.
PIRGNWVDP. A29972.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9KX-ray2.40A2492-2784[»]
1OANX-ray2.75A/B281-674[»]
1OK8X-ray2.00A281-674[»]
1OKEX-ray2.40A/B281-674[»]
1P58electron microscopy9.50A/B/C281-775[»]
D/E/F206-280[»]
1R6AX-ray2.60A2492-2784[»]
1R6RNMR-A/B1-100[»]
1THDelectron microscopy9.50A/B/C281-675[»]
2P1DX-ray2.90A2492-2784[»]
2P3LX-ray2.20A2492-2784[»]
2P3OX-ray2.76A2492-2784[»]
2P3QX-ray2.75A2492-2784[»]
2P40X-ray2.70A2492-2784[»]
2P41X-ray1.80A2492-2784[»]
ProteinModelPortalP12823.
SMRP12823. Positions 21-100, 115-195, 281-674, 1394-1440, 1495-2090, 2495-2756, 2762-3371.
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.
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]
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. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_DEN2P
AccessionPrimary (citable) accession number: P12823
Secondary accession number(s): Q88646 expand/collapse secondary AC list , Q88647, Q88648, Q88649, Q88650, Q88651, Q88652, Q88653, Q88654, Q88655
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 16, 2011
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

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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