Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9WDA6 (POLG_DEN2Q)

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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:
Capsid protein C
Alternative name(s):
Core protein
Protein prM
Peptide pr
Small envelope protein M
Alternative name(s):
Matrix protein
Envelope protein E
Non-structural protein 1
Short name:
NS1
Non-structural protein 2A
Short name:
NS2A
Serine protease subunit NS2B
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
Non-structural protein 4A
Short name:
NS4A
Peptide 2k
Non-structural protein 4B
Short name:
NS4B
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 lineageiViruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus ›
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 subunit NS2B :
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

View the complete GO annotation on QuickGO ...

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

View the complete GO annotation on QuickGO ...

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again