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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 2 (strain Peru/IQT2913/1996) (DENV-2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein C: Plays a role in virus budding by binding to membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration in host cytoplasm after hemifusion induced by surface proteins. Can migrate tot cell nucleus where it modulates host functions.By similarity
Peptide pr: Prevents premature fusion activity of envelope proteins in trans Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space gets dissociated from E dimers.By similarity
Protein prM: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network. Presumably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Small envelope protein M: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M extodomain. May display a viroporin activity.By similarity
Envelope protein E: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particule is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Non-structural protein 1: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. May plays a role in viral genome replication. Assist membrane bending and envelopment of genomic RNA at the endoplasmic reticulum. Excreted as a hexameric lipoparticle that plays a role against host immune responce.By similarity
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.By similarity
Non-structural protein 2B: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy 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.PROSITE-ProRule annotation
Non-structural protein 4A: Induces host endoplasmic 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 activityi

Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1526Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1550Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1610Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Binding sitei2505mRNA capPROSITE-ProRule annotation1
Binding sitei2508mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2509mRNA capPROSITE-ProRule annotation1
Binding sitei2511mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2516mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2520mRNA capPROSITE-ProRule annotation1
Binding sitei2547S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2552Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2577S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2578S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2595S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2596S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2622S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2623S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2637Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2638S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2641mRNA capPROSITE-ProRule annotation1
Sitei2672Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2703mRNA capPROSITE-ProRule annotation1
Binding sitei2705mRNA capPROSITE-ProRule annotation1
Sitei2708Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2710S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1668 – 1675ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT2 by virus, Inhibition of host TYK2 by virus, Ion transport, mRNA capping, mRNA processing, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

Protein family/group databases

MEROPSiS07.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 14 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Non-structural protein 2A-alpha
Short name:
NS2A-alpha
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Alternative name(s):
Non-structural protein 5
OrganismiDengue virus type 2 (strain Peru/IQT2913/1996) (DENV-2)
Taxonomic identifieri408694 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostiAedimorphus [TaxID: 53540]
Diceromyia [TaxID: 53539]
Erythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
Stegomyia [TaxID: 53541]
Proteomesi
  • UP000002329 Componenti: Genome

Subcellular locationi

Protein C :
  • Virion By similarity
  • Host nucleus By similarity
Peptide pr :
  • Secreted By similarity
Small envelope protein M :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotationBy similarity; Multi-pass membrane protein By similarity
Envelope protein E :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotationBy similarity; Multi-pass membrane protein By similarity
Non-structural protein 1 :
  • Secreted By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Lumenal side By similarity
Non-structural protein 2A-alpha :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
Non-structural protein 2A :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
Serine protease subunit NS2B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotationBy similarity
Serine protease NS3 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation

  • Note: Remains non-covalently associated to NS3 protease.PROSITE-ProRule annotation
Non-structural protein 4A :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.By similarity
Non-structural protein 4B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Host nucleus By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 101CytoplasmicSequence analysisAdd BLAST101
Transmembranei102 – 122HelicalSequence analysisAdd BLAST21
Topological domaini123 – 238ExtracellularSequence analysisAdd BLAST116
Transmembranei239 – 259HelicalSequence analysisAdd BLAST21
Topological domaini260 – 265CytoplasmicSequence analysis6
Transmembranei266 – 280HelicalSequence analysisAdd BLAST15
Topological domaini281 – 725ExtracellularSequence analysisAdd BLAST445
Intramembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 752ExtracellularSequence analysis6
Intramembranei753 – 773HelicalSequence analysisAdd BLAST21
Topological domaini774 – 1124ExtracellularSequence analysisAdd BLAST351
Transmembranei1125 – 1145HelicalSequence analysisAdd BLAST21
Topological domaini1146 – 1156CytoplasmicSequence analysisAdd BLAST11
Transmembranei1157 – 1177HelicalSequence analysisAdd BLAST21
Topological domaini1178 – 1184LumenalSequence analysis7
Transmembranei1185 – 1205HelicalSequence analysisAdd BLAST21
Topological domaini1206 – 1271CytoplasmicSequence analysisAdd BLAST66
Transmembranei1272 – 1292HelicalSequence analysisAdd BLAST21
Topological domaini1293 – 1317LumenalSequence analysisAdd BLAST25
Transmembranei1318 – 1338HelicalSequence analysisAdd BLAST21
Topological domaini1339 – 1346CytoplasmicSequence analysis8
Transmembranei1347 – 1367HelicalSequence analysisAdd BLAST21
Topological domaini1368 – 1370LumenalSequence analysis3
Transmembranei1371 – 1391HelicalSequence analysisAdd BLAST21
Topological domaini1392 – 1447CytoplasmicSequence analysisAdd BLAST56
Intramembranei1448 – 1468HelicalSequence analysisAdd BLAST21
Topological domaini1469 – 2147CytoplasmicSequence analysisAdd BLAST679
Transmembranei2148 – 2168HelicalSequence analysisAdd BLAST21
Topological domaini2169 – 2170LumenalSequence analysis2
Intramembranei2171 – 2191HelicalSequence analysisAdd BLAST21
Topological domaini2192LumenalSequence analysis1
Transmembranei2193 – 2213HelicalSequence analysisAdd BLAST21
Topological domaini2214 – 2228CytoplasmicSequence analysisAdd BLAST15
Transmembranei2229 – 2249Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2250 – 2277LumenalSequence analysisAdd BLAST28
Intramembranei2278 – 2295HelicalSequence analysisAdd BLAST18
Topological domaini2296 – 2316LumenalSequence analysisAdd BLAST21
Intramembranei2317 – 2337HelicalSequence analysisAdd BLAST21
Topological domaini2338 – 2347LumenalSequence analysis10
Transmembranei2348 – 2368HelicalSequence analysisAdd BLAST21
Topological domaini2369 – 2413CytoplasmicSequence analysisAdd BLAST45
Transmembranei2414 – 2434HelicalSequence analysisAdd BLAST21
Topological domaini2435 – 2459LumenalSequence analysisAdd BLAST25
Transmembranei2460 – 2480HelicalSequence analysisAdd BLAST21
Topological domaini2481 – 3391CytoplasmicSequence analysisAdd BLAST911

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Secreted, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004052181 – 3391Genome polyproteinAdd BLAST3391
ChainiPRO_00002680281 – 100Protein CBy similarityAdd BLAST100
PropeptideiPRO_0000268029101 – 114ER anchor for the protein C, removed in mature form by serine protease NS3Add BLAST14
ChainiPRO_0000268030115 – 280prMBy similarityAdd BLAST166
ChainiPRO_0000268031115 – 205Peptide prBy similarityAdd BLAST91
ChainiPRO_0000268032206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000268033281 – 775Envelope protein EBy similarityAdd BLAST495
ChainiPRO_0000268034776 – 1127Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00002680361128 – 1345Non-structural protein 2ABy similarityAdd BLAST218
ChainiPRO_00002680351128 – 1315Non-structural protein 2A-alphaBy similarityAdd BLAST188
ChainiPRO_00002680371346 – 1475Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00002680381476 – 2093Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00002680392094 – 2220Non-structural protein 4ABy similarityAdd BLAST127
PeptideiPRO_00002680402221 – 2243Peptide 2kAdd BLAST23
ChainiPRO_00002680412244 – 2491Non-structural protein 4BBy similarityAdd BLAST248
ChainiPRO_00002680422492 – 3391RNA-directed RNA polymerase NS5By similarityAdd BLAST900

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi183N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Glycosylationi347N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 396By similarity
Glycosylationi433N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi465 ↔ 565By similarity
Disulfide bondi582 ↔ 613By similarity
Disulfide bondi779 ↔ 790By similarity
Disulfide bondi830 ↔ 918By similarity
Disulfide bondi954 ↔ 998By similarity
Glycosylationi982N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi1055 ↔ 1104By similarity
Disulfide bondi1066 ↔ 1088By similarity
Disulfide bondi1087 ↔ 1091By similarity
Glycosylationi2301N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2305N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2457N-linked (GlcNAc...); by hostSequence analysis1

Post-translational modificationi

Genome polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, wereas cleavages in the cytoplasmic side are performed by the Serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Non-structural protein 2A-alpha: A C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3.By similarity
Protein prM: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
Non-structural protein 1: The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei100 – 101Cleavage; by viral protease NS3Sequence analysis2
Sitei114 – 115Cleavage; by host signal peptidaseBy similarity2
Sitei205 – 206Cleavage; by host furinSequence analysis2
Sitei280 – 281Cleavage; by host signal peptidaseSequence analysis2
Sitei775 – 776Cleavage; by host signal peptidaseSequence analysis2
Sitei1127 – 1128Cleavage; by hostBy similarity2
Sitei1345 – 1346Cleavage; by viral protease NS3Sequence analysis2
Sitei1475 – 1476Cleavage; by autolysisSequence analysis2
Sitei2093 – 2094Cleavage; by autolysisSequence analysis2
Sitei2220 – 2221Cleavage; by viral protease NS3Sequence analysis2
Sitei2243 – 2244Cleavage; by host signal peptidaseSequence analysis2
Sitei2491 – 2492Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Interactioni

Subunit structurei

Protein C: Homodimerizes. Protein prM: Forms homodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Forms homodimers with envelope protein E in the endoplasmic reticulum and Golgi. Non-structural protein 1: Forms homodimers as well as homohexamers. NS1 may interact with NS4A. Non-structural protein 2B: Forms a heterodimer with Non-structural protein 3. May form homooligomers. Non-structural protein 3: Forms a heterodimer with Non-structural protein 2B. Interacts with Non-structural protein 4B. Interacts with unphosphorylated Non-structural protein 5; this interaction stimulates Non-structural protein 5 guanylyltransferase activity. Non-structural protein 4B: Interacts with non-structural protein 3. Non-structural protein 5: 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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IXYelectron microscopy-A/B/C281-675[»]
ProteinModelPortaliQ9WDA6.
SMRiQ9WDA6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WDA6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1476 – 1653Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1655 – 1811Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1821 – 1988Helicase C-terminalPROSITE-ProRule annotationAdd BLAST168
Domaini2493 – 2755mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST263
Domaini3020 – 3169RdRp catalyticPROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 74Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST42
Regioni1398 – 1437Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1759 – 1762DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi97 – 100Poly-Arg4
Compositional biasi1434 – 1437Poly-Glu4
Compositional biasi2148 – 2154Poly-Leu7
Compositional biasi3383 – 3386Poly-Glu4

Domaini

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

Sequence similaritiesi

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 mRNA cap 0-1 NS5-type MT domain.PROSITE-ProRule annotation
Contains 1 peptidase S7 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR027287. Flavi_E_Ig-like.
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.
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.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WDA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNQRKKARN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL
60 70 80 90 100
VAFLRFLTIP PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR
110 120 130 140 150
TAGMIIMLIP TVMAFHLTTR NGEPHMIVSR QEKGKSLLFK TKDGTNMCTL
160 170 180 190 200
MAMDLGELCE DTITYKCPFL KQNEPEDIDC WCNSTSTWVT YGTCTTTGEH
210 220 230 240 250
RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW ILRHPGFTIM
260 270 280 290 300
AAILAYTIGT THFQRVLIFI LLTAIAPSMT MRCIGISNRD FVEGVSGGSW
310 320 330 340 350
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT
360 370 380 390 400
DSRCPTQGEP TLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT
410 420 430 440 450
CKKNMEGKIV QPENLEYTVV ITPHSGEEHA VGNDTGKHGK EVKITPQSSI
460 470 480 490 500
TEAELTGYGT VTMECSPRTG LDFNEMVLLQ MEDKAWLVHR QWFLDLPLPW
510 520 530 540 550
LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM HTALTGATEI
560 570 580 590 600
QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKIVK EIAETQHGTI
610 620 630 640 650
VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE
660 670 680 690 700
PPFGDSYIII GAEPGQLKLD WFKKGSSIGQ MFETTMRGAK RMAILGDTAW
710 720 730 740 750
DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS
760 770 780 790 800
RSTSLSVSLV LVGIVTLYLG VMVQADSGCV VSWKNKELKC GSGIFVTDNV
810 820 830 840 850
HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN LMWKQITSEL
860 870 880 890 900
NHILSENEVK LTIMTGDIKG IMQVGKRSLR PQPTELRYSW KTWGKAKMLS
910 920 930 940 950
TELHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLRLREKQ
960 970 980 990 1000
DAFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW
1010 1020 1030 1040 1050
PKSHTLWSNG VLESEMVIPK NIAGPVSQHN NRPGYHTQTA GPWHLGKLEM
1060 1070 1080 1090 1100
DFDFCEGTTV VVTEECGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG
1110 1120 1130 1140 1150
EDGCWYGMEI RPLKEKEENL VSSLVTAGHG QIDNFSLGIL GMALFLEEML
1160 1170 1180 1190 1200
RTRVGTKHAI LLVAVSFLTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT
1210 1220 1230 1240 1250
YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ SSIPETILEL
1260 1270 1280 1290 1300
TDALALGMMV LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTTLA
1310 1320 1330 1340 1350
VVSVSPLLLT SSQQKADWIP LALTIKGLNP TAIFLTTLTR TSKKRSWPLN
1360 1370 1380 1390 1400
EAIMAVGMVS ILASSLLKND IPMTGPLVAG GLLTVCYVLT GRSADLELER
1410 1420 1430 1440 1450
ATDVKWDDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL TILIRTGLLV
1460 1470 1480 1490 1500
ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPVGR AELEDGAYRI
1510 1520 1530 1540 1550
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD
1560 1570 1580 1590 1600
LISYGGGWKL EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FRTNTGTIGA
1610 1620 1630 1640 1650
VSLDFSPGTS GSPIVDKKGK VVGLYGNGVV TRGGAYVSAI AQTEKGIEDN
1660 1670 1680 1690 1700
PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP AIVREAIKRG LRTLILAPTR
1710 1720 1730 1740 1750
VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF TMRLLSPIRV
1760 1770 1780 1790 1800
PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
1810 1820 1830 1840 1850
PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KTGNDIAACL
1860 1870 1880 1890 1900
RKNGKRVIQL SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP
1910 1920 1930 1940 1950
RRCMKPVILT DGEERVILAG PMPVTHSSAA QRRGRIGRNP RNENDQYIYM
1960 1970 1980 1990 2000
GEPLENDEDC AHWKEAKMLL DNINTPEGII PSMFEPEREK VDAIDGEYRL
2010 2020 2030 2040 2050
RGEARKTFVD LMRRGDLPVW LAYKVAAEGI NYADRRWCFD GTRNNQILEE
2060 2070 2080 2090 2100
NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
2110 2120 2130 2140 2150
TEMGRLPTFM TQKARDALDN LAVLHTAEAG GKAYNHALSE LPETLETLLL
2160 2170 2180 2190 2200
LTLLATVTGG IFLFLMSGRG IGKMTLGMCC IITASILLWY AQIQPHWIAA
2210 2220 2230 2240 2250
SIILEFFLIV LLIPEPEKQR TPQDNQLTYV IIAILTVVAA TMANEMGFLE
2260 2270 2280 2290 2300
KTKKDLGLGH IATQQPESNI LDIDLRPASA WTLYAVATTF ITPMLRHSIE
2310 2320 2330 2340 2350
NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG CYSQVNPITL
2360 2370 2380 2390 2400
TAALLMLVAH YAIIGPGLQA KATREAQKRA AAGIMKNPTV DGITVIDLDP
2410 2420 2430 2440 2450
IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEALTLA TGPVSTLWEG
2460 2470 2480 2490 2500
NPGRFWNTTI AVSMANIFRG SYLAGAGLLF SIMKNTTSTR RGTGNMGETL
2510 2520 2530 2540 2550
GEKWKNRLNA LGKSEFQIYK KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS
2560 2570 2580 2590 2600
AKLRWFVERN LVTPEGKVVD LGCGRGGWSY YCGGLKNVRE VKGLTKGGPG
2610 2620 2630 2640 2650
HEEPIPMSTY GWNLVRLQSG VDVFFVPPEK CDTLLCDIGE SSPNPTVEAG
2660 2670 2680 2690 2700
RTLRVLNLVE NWLNNNTQFC VKVLNPYMPS VIERMETLQR KYGGALVRNP
2710 2720 2730 2740 2750
LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRHKK ATYEPDVDLG
2760 2770 2780 2790 2800
SGTRNIGIES ETPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY
2810 2820 2830 2840 2850
ETKQTGSASS MVNGVVRLLT KPWDVIPMVT QMAMTDTTPF GQQRVFKEKV
2860 2870 2880 2890 2900
DTRTQEPKEG TKKLMKITAE WLWKELGKKK TPRMCTREEF TKKVRSNAAL
2910 2920 2930 2940 2950
GAIFTDENKW KSAREAVEDN RFWELVDKER NLHLEGKCET CVYNMMGKRE
2960 2970 2980 2990 3000
KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG
3010 3020 3030 3040 3050
EGLHKLGYIL REVSKKEGGA MYADDTAGWD TRITIEDLKN EEMITNHMAG
3060 3070 3080 3090 3100
EHKKLAEAIF KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVVTYGL
3110 3120 3130 3140 3150
NTFTNMEAQL IRQMEGEGVF KSIQHLTASE EIAVQDWLVR VGRERLSRMA
3160 3170 3180 3190 3200
ISGDDCVVKP LDDRFAKALT ALNDMGKVRK DIQQWEPSRG WNDWTQVPFC
3210 3220 3230 3240 3250
SHHFHELIMK DGRTLVVPCR NQDELIGRAR ISQGAGWSLR ETACLGKSYA
3260 3270 3280 3290 3300
QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA SHEWMTTEDM
3310 3320 3330 3340 3350
LTVWNRVWIL ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW
3360 3370 3380 3390
AKNIQTAINQ VRSLIGNEEY TDYMPSMKRF RREEEEVGVL W
Length:3,391
Mass (Da):379,787
Last modified:November 1, 1999 - v1
Checksum:i35CBA7037DDF9E5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100468 Genomic RNA. Translation: AAD32963.1.
PIRiB25817.
JS0219.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100468 Genomic RNA. Translation: AAD32963.1.
PIRiB25817.
JS0219.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IXYelectron microscopy-A/B/C281-675[»]
ProteinModelPortaliQ9WDA6.
SMRiQ9WDA6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WDA6.
PROiQ9WDA6.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR027287. Flavi_E_Ig-like.
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.
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.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_DEN2Q
AccessioniPrimary (citable) accession number: Q9WDA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.