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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: -Experimental evidence at protein leveli

Functioni

Capsid protein C: Plays a role in virus budding by binding to the cell 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 into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.By similarity
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.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 probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, 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 ectodomain. 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 particle 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 inefficient, 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. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).By similarity
Non-structural protein 1: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.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
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. 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: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired.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: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. 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 (-) RNA 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 RNA 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'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].PROSITE-ProRule annotation

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
Sitei1932Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1935Involved in NS3 ATPase and RTPase activitiesBy similarity1
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
Active sitei2552For 2'-O-MTase activityBy similarity1
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
Active sitei2637For 2'-O-MTase activityBy similarity1
Sitei2637Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2638S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2641mRNA capPROSITE-ProRule annotation1
Active sitei2672For 2'-O-MTase activityBy similarity1
Sitei2672Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2703mRNA capPROSITE-ProRule annotation1
Binding sitei2705mRNA capPROSITE-ProRule annotation1
Active sitei2708For 2'-O-MTase activityBy similarity1
Sitei2708Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2710S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2929Zinc 1By similarity1
Metal bindingi2933Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2938Zinc 1By similarity1
Metal bindingi2941Zinc 1By similarity1
Metal bindingi3203Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3219Zinc 2By similarity1
Metal bindingi3338Zinc 2By similarity1

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase, Viral ion channel
Biological processActivation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host MAVS by virus, Inhibition of host RLR 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
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPSiS07.001

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
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 stageFlaviviridaeFlavivirus
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

Capsid protein C :
Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :

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
Transmembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 752CytoplasmicSequence analysis6
Transmembranei753 – 773HelicalSequence analysisAdd BLAST21
Topological domaini774 – 1195ExtracellularSequence analysisAdd BLAST422
Transmembranei1196 – 1220HelicalSequence analysisAdd BLAST25
Topological domaini1221 – 1226CytoplasmicSequence analysis6
Transmembranei1227 – 1245HelicalSequence analysisAdd BLAST19
Topological domaini1246 – 1269LumenalSequence analysisAdd BLAST24
Transmembranei1270 – 1290HelicalSequence analysisAdd BLAST21
Topological domaini1291CytoplasmicSequence analysis1
Transmembranei1292 – 1312HelicalSequence analysisAdd BLAST21
Topological domaini1313 – 1317LumenalSequence analysis5
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 – 2274LumenalSequence analysisAdd BLAST25
Intramembranei2275 – 2295HelicalSequence analysisAdd BLAST21
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

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004052181 – 3391Genome polyproteinAdd BLAST3391
ChainiPRO_00002680281 – 100Capsid protein CBy similarityAdd BLAST100
PropeptideiPRO_0000268029101 – 114ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST14
ChainiPRO_0000268030115 – 280Protein prMBy 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_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 2kBy similarityAdd 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...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Glycosylationi347N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 396By similarity
Glycosylationi433N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi465 ↔ 565By similarity
Disulfide bondi582 ↔ 613By similarity
Disulfide bondi779 ↔ 790By similarity
Disulfide bondi830 ↔ 918By similarity
Glycosylationi905N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi954 ↔ 998By similarity
Glycosylationi982N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi1055 ↔ 1104By similarity
Disulfide bondi1066 ↔ 1088By similarity
Disulfide bondi1087 ↔ 1091By similarity
Glycosylationi1134N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2301N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2305N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2457N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Modified residuei2547PhosphoserineBy similarity1

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, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.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
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated. 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: Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei100 – 101Cleavage; by viral protease NS3By similarity2
Sitei114 – 115Cleavage; by host signal peptidaseBy similarity2
Sitei205 – 206Cleavage; by host furinSequence analysisBy similarity2
Sitei280 – 281Cleavage; by host signal peptidaseBy similarity2
Sitei775 – 776Cleavage; by host signal peptidaseBy similarity2
Sitei1127 – 1128Cleavage; by hostBy similarity2
Sitei1345 – 1346Cleavage; by viral protease NS3By similarity2
Sitei1475 – 1476Cleavage; by autolysisBy similarity2
Sitei2093 – 2094Cleavage; by autolysisBy similarity2
Sitei2220 – 2221Cleavage; by viral protease NS3By similarity2
Sitei2243 – 2244Cleavage; by host signal peptidaseBy similarity2
Sitei2491 – 2492Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRIDEiQ9WDA6

Interactioni

Subunit structurei

Capsid protein C: Homodimer. Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway. Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi. Interacts with protein prM. Interacts with non-structural protein 1. Non-structural protein 1: Homodimer; Homohexamer when secreted. Interacts with envelope protein E. Non-structural protein 2A: Interacts (via N-terminus) with serine protease NS3. Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers. Serine protease NS3: Forms a heterodimer with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. Non-structural protein 4A: Interacts with host MAVS; this interaction inhibits the synthesis of IFN-beta. Non-structural protein 4B: Interacts with serine protease NS3. RNA-directed RNA polymerase NS5: Homodimer. Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation. Interacts with serine protease NS3.By similarity

GO - Molecular functioni

Structurei

3D structure databases

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
Regioni1 – 15Interaction with host EXOC1By similarityAdd BLAST15
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni378 – 391Fusion peptideBy similarityAdd BLAST14
Regioni1398 – 1437Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1659 – 1662Important for RNA-bindingBy similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1759 – 1762DEAH boxPROSITE-ProRule annotation4
Motifi2568 – 2571SUMO-interacting motifBy similarity4

Compositional bias

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

Domaini

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG09000016

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 3 hits
3.30.387.10, 2 hits
3.30.67.10, 4 hits
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
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
PfamiView protein in Pfam
PF01003 Flavi_capsid, 1 hit
PF07652 Flavi_DEAD, 1 hit
PF02832 Flavi_glycop_C, 1 hit
PF00869 Flavi_glycoprot, 1 hit
PF01004 Flavi_M, 1 hit
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 1 hit
PF01002 Flavi_NS2B, 1 hit
PF01350 Flavi_NS4A, 1 hit
PF01349 Flavi_NS4B, 1 hit
PF00972 Flavi_NS5, 1 hit
PF01570 Flavi_propep, 1 hit
PF01728 FtsJ, 1 hit
PF00949 Peptidase_S7, 1 hit
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF101257 SSF101257, 1 hit
SSF50494 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
PROSITEiView protein in PROSITE
PS51527 FLAVIVIRUS_NS2B, 1 hit
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit

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

Similar proteinsi

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

Proteomic databases

PRIDEiQ9WDA6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG09000016

Miscellaneous databases

EvolutionaryTraceiQ9WDA6
PROiPR:Q9WDA6

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 3 hits
3.30.387.10, 2 hits
3.30.67.10, 4 hits
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
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
PfamiView protein in Pfam
PF01003 Flavi_capsid, 1 hit
PF07652 Flavi_DEAD, 1 hit
PF02832 Flavi_glycop_C, 1 hit
PF00869 Flavi_glycoprot, 1 hit
PF01004 Flavi_M, 1 hit
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 1 hit
PF01002 Flavi_NS2B, 1 hit
PF01350 Flavi_NS4A, 1 hit
PF01349 Flavi_NS4B, 1 hit
PF00972 Flavi_NS5, 1 hit
PF01570 Flavi_propep, 1 hit
PF01728 FtsJ, 1 hit
PF00949 Peptidase_S7, 1 hit
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF101257 SSF101257, 1 hit
SSF50494 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
PROSITEiView protein in PROSITE
PS51527 FLAVIVIRUS_NS2B, 1 hit
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_DEN2Q
AccessioniPrimary (citable) accession number: Q9WDA6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1999
Last modified: June 20, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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