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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 1 (strain Singapore/S275/1990) (DENV-1)
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 c. 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 sitei1525Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1549Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1609Charge 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 sitei2506mRNA capPROSITE-ProRule annotation1
Binding sitei2509mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2510mRNA capPROSITE-ProRule annotation1
Binding sitei2512mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2517mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2521mRNA capPROSITE-ProRule annotation1
Binding sitei2548S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2553For 2'-O-MTase activityBy similarity1
Sitei2553Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2578S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2579S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2596S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2597S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2623S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2624S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2638For 2'-O-MTase activityBy similarity1
Sitei2638Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2639S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2642mRNA 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 1 (strain Singapore/S275/1990) (DENV-1)
Taxonomic identifieri33741 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007194 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 – 119HelicalSequence analysisAdd BLAST18
Topological domaini120 – 242ExtracellularSequence analysisAdd BLAST123
Transmembranei243 – 260HelicalSequence analysisAdd BLAST18
Topological domaini261CytoplasmicSequence analysis1
Transmembranei262 – 280HelicalSequence analysisAdd BLAST19
Topological domaini281 – 725ExtracellularSequence analysisAdd BLAST445
Transmembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 752CytoplasmicSequence analysis6
Transmembranei753 – 773HelicalSequence analysisAdd BLAST21
Topological domaini774 – 1198ExtracellularSequence analysisAdd BLAST425
Transmembranei1199 – 1219HelicalSequence analysisAdd BLAST21
Topological domaini1220 – 1225CytoplasmicSequence analysis6
Transmembranei1226 – 1244HelicalSequence analysisAdd BLAST19
Topological domaini1245 – 1268LumenalSequence analysisAdd BLAST24
Transmembranei1269 – 1289HelicalSequence analysisAdd BLAST21
Topological domaini1290CytoplasmicSequence analysis1
Transmembranei1291 – 1309HelicalSequence analysisAdd BLAST19
Topological domaini1310 – 1314LumenalSequence analysis5
Transmembranei1315 – 1335HelicalSequence analysisAdd BLAST21
Topological domaini1336 – 1345CytoplasmicSequence analysis10
Transmembranei1346 – 1366HelicalSequence analysisAdd BLAST21
Topological domaini1367 – 1369LumenalSequence analysis3
Transmembranei1370 – 1390HelicalSequence analysisAdd BLAST21
Topological domaini1391 – 1446CytoplasmicSequence analysisAdd BLAST56
Intramembranei1447 – 1467HelicalSequence analysisAdd BLAST21
Topological domaini1468 – 2147CytoplasmicSequence analysisAdd BLAST680
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 – 2275LumenalSequence analysisAdd BLAST26
Intramembranei2276 – 2296HelicalSequence analysisAdd BLAST21
Topological domaini2297 – 2348LumenalSequence analysisAdd BLAST52
Transmembranei2349 – 2369HelicalSequence analysisAdd BLAST21
Topological domaini2370 – 2414CytoplasmicSequence analysisAdd BLAST45
Transmembranei2415 – 2435HelicalSequence analysisAdd BLAST21
Topological domaini2436 – 2460LumenalSequence analysisAdd BLAST25
Transmembranei2461 – 2481HelicalSequence analysisAdd BLAST21
Topological domaini2482 – 3391CytoplasmicSequence analysisAdd BLAST910

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_00004052061 – 3391Genome polyproteinAdd BLAST3391
ChainiPRO_00000378941 – 100Capsid protein CBy similarityAdd BLAST100
PropeptideiPRO_0000037895101 – 114ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST14
ChainiPRO_0000264654115 – 280Protein prMBy similarityAdd BLAST166
ChainiPRO_0000264655115 – 205Peptide prBy similarityAdd BLAST91
ChainiPRO_0000037896206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037897281 – 774Envelope protein EBy similarityAdd BLAST494
ChainiPRO_0000037898775 – 1126Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000378991127 – 1344Non-structural protein 2ABy similarityAdd BLAST218
ChainiPRO_00000379001345 – 1474Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00000379011475 – 2093Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00000379022094 – 2220Non-structural protein 4ABy similarityAdd BLAST127
PeptideiPRO_00002646572221 – 2243Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000379032244 – 2492Non-structural protein 4BBy similarityAdd BLAST249
ChainiPRO_00004379902493 – 3391RNA-directed RNA polymerase NS5By similarityAdd BLAST899

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 bondi778 ↔ 789By similarity
Disulfide bondi829 ↔ 917By similarity
Glycosylationi904N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi953 ↔ 997By similarity
Glycosylationi981N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi1054 ↔ 1103By similarity
Disulfide bondi1065 ↔ 1087By similarity
Disulfide bondi1086 ↔ 1090By similarity
Glycosylationi1189N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2302N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2306N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2458N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Modified residuei2548PhosphoserineBy 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
Sitei774 – 775Cleavage; by host signal peptidaseBy similarity2
Sitei1126 – 1127Cleavage; by hostBy similarity2
Sitei1344 – 1345Cleavage; by viral protease NS3By similarity2
Sitei1474 – 1475Cleavage; by autolysisBy similarity2
Sitei2093 – 2094Cleavage; by autolysisBy similarity2
Sitei2220 – 2221Cleavage; by viral protease NS3By similarity2
Sitei2243 – 2244Cleavage; by host signal peptidaseBy similarity2
Sitei2492 – 2493Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRIDEiP33478

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

Secondary structure

13391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP33478
SMRiP33478
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1475 – 1652Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1655 – 1811Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1821 – 1988Helicase C-terminalPROSITE-ProRule annotationAdd BLAST168
Domaini2494 – 2755mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST262
Domaini3019 – 3168RdRp 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
Regioni1397 – 1436Interacts 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
Motifi2569 – 2572SUMO-interacting motifBy similarity4

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

OrthoDBiVOG090001ER

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
cd00079 HELICc, 1 hit
cd06174 MFS, 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, 1 hit
3.30.387.10, 1 hit
3.30.67.10, 1 hit
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
IPR020846 MFS_dom
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.

P33478-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNNQRKKTAR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF
60 70 80 90 100
IAFLRFLAIP PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR
110 120 130 140 150
SVTMLLMLLP TALAFHLTTR GGEPHMIVSK QEREKSLLFK TSVGVNMCTL
160 170 180 190 200
IAMDLGELCE DTMTYKCPRI TEAEPDDVDC WCNATDTWVT YGTCSQTGEH
210 220 230 240 250
RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQRVETW ALRHPGFTVI
260 270 280 290 300
ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGSRD FVEGLSGATW
310 320 330 340 350
VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT
360 370 380 390 400
DSRCPTQGEA TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLLTCAKFK
410 420 430 440 450
CVTKLEGKIV QYENLKYSVI VTVHTGDQHQ VGNETTEHGT IATITPQAPT
460 470 480 490 500
SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT MKEKSWLVHK QWFLDLPLPW
510 520 530 540 550
TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM HTALTGATEI
560 570 580 590 600
QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV
610 620 630 640 650
LVQVKYEGTD APCKIPFSTQ DEKGVTQNRL ITANPIVTDK EKPVNIETEP
660 670 680 690 700
PFGESYIVVG AGEKALKQCW FKKGSSIGKM FEATARGARR MAILGDTAWD
710 720 730 740 750
FGSIGGVFTS VGKLVHQVFG TAYGVLFSGV SWTMKIGIGI LLTWLGLNSR
760 770 780 790 800
STSLSMTCIA VGMVTLYLGV MVQADSGCVI NWKGRELKCG SGIFVTNEVH
810 820 830 840 850
TWTEQYKFQA DSPKRLSAAI GKAWEEGVCG IRSATRLENI MWKQISNELN
860 870 880 890 900
HILLENDMKF TVVVGDVVGI LAQGKKMIRP QPMEHKYSWK SWGKAKIIGA
910 920 930 940 950
DIQNTTFIID GPDTPECPDD QRAWNIWEVE DYGFGIFTTN IWLKLRDSYT
960 970 980 990 1000
QMCDHRLMSA AIKDSKAVHA DMGYWIESEK NETWKLARAS FIEVKTCVWP
1010 1020 1030 1040 1050
KSHTLWSNGV LESEMIIPKI YGGPISQHNY RPGYFTQTAG PWHLGKLELD
1060 1070 1080 1090 1100
FDLCEGTTVV VDEHCGNRGP SLRTTTVTGK IIHEWCCRSC TLPPLRFKGE
1110 1120 1130 1140 1150
DGCWYGMEIR PVKEKEENLV KSMVSAGSGE VDSFSLGLLC ISIMIEEVMR
1160 1170 1180 1190 1200
SRWSRKMLMT GTLAVFLLLI MGQLTWNDLI RLCIMVGANA SDRMGMGTTY
1210 1220 1230 1240 1250
LALMATFKMR PMFAVGLLFR RLTSREVLLL TIGLSLVASV ELPNSLEELG
1260 1270 1280 1290 1300
DGLAMGIMIL KLLTDFQSHQ LWATLLSLTF VKTTFSLHYA WKTMAMVLSI
1310 1320 1330 1340 1350
VSLFPLCLST TSQKTTWLPV LLGSLGCKPL TMFLIAENKI WGRKSWPLNE
1360 1370 1380 1390 1400
GIMAVGIVSI LLSSLLKNDV PLAGPLIAGG MLIACYVISG SSADLSLEKA
1410 1420 1430 1440 1450
AEVSWEEEAE HSGASHNILV EVQDDGTMKI KDEERDDTLT ILLKATLLAV
1460 1470 1480 1490 1500
SGVYPLSIPA TLFVWYFWQK KKQRSGVLWD TPSPPEVERA VLDDGIYRIM
1510 1520 1530 1540 1550
QRGLLGRSQV GVGVFQDGVF HTMWHVTRGA VLMYQGKRLE PSWASVKKDL
1560 1570 1580 1590 1600
ISYGGGWRFQ GSWNTGEEVQ VIAVEPGKNP KNVQTAPGTF KTPEGEVGAI
1610 1620 1630 1640 1650
ALDFKPGTSG SPIVNREGKI VGLYGNGVVT TSGTYVSAIA QAKASQEGPL
1660 1670 1680 1690 1700
PEIEDEVFRK RNLTIMDLHP GSGKTRRYLP AIVREAIRRN VRTLILAPTR
1710 1720 1730 1740 1750
VVASEMAEAL KGMPIRYQTT AVKSEHTGKE IVDLMCHATF TMRLLSPVRV
1760 1770 1780 1790 1800
PNYNMIIMDE AHFTDPASIA RRGYISTRVG MGEAAAIFMT ATPPGSVEAF
1810 1820 1830 1840 1850
PQSNAVIQDE ERDIPERSWN SGYEWITDFP GKTVWFVPSI KSGNDIANCL
1860 1870 1880 1890 1900
RKNGKRVIQL SRKTFDTEYQ KTKNNDWDYV VTTDISEMGA NFRADRVIDP
1910 1920 1930 1940 1950
RRCLKPVILK DGPERVILAG PMPVTVASAA QRRGRIGRNQ NKEGDQYVYM
1960 1970 1980 1990 2000
GQPLNNDEDH AHWTEAKMLL DNINTPEGII PALFEPEREK SAAIDGEYRL
2010 2020 2030 2040 2050
RGEARKTFVE LMRRGDLPVW LSYKVASEGF QYSDRRWCFD GERNNQVLEE
2060 2070 2080 2090 2100
NMDVEMWTKE GERKKLRPRW LDARTYSDPL ALREFKEFAA GRRSVSGDLI
2110 2120 2130 2140 2150
LEIGKLPQHL TQRAQNALDN LVMLHNSEQG GRAYRHAMEE LPDTIETLML
2160 2170 2180 2190 2200
LALIAVLTGG VTLFFLSGKG LGKTSIGLLC VMASSVLLWM ASVEPHWIAA
2210 2220 2230 2240 2250
SIILEFFLMV LLIPEPDRQR TPQDNQLAYV VIGLLFMILT VAANEMGLLE
2260 2270 2280 2290 2300
TTKKDLGIGH VAAENHHHAT MLDVDLRPAS AWTLYAVATT VITPMMRHTI
2310 2320 2330 2340 2350
ENTTANISLT AIANQAAILM GLDKGWPISK MDIGVPLLAL GCYSQVNPLT
2360 2370 2380 2390 2400
LTAAVLMLVA HYAIIGPGLQ AKATREAQKR TAAGIMKNPT VDGIVAIDLD
2410 2420 2430 2440 2450
PVVYDAKFEK QLGQIMLLIL CTSQILLMRT TWALCESITL ATGPLTTLWE
2460 2470 2480 2490 2500
GSPGKFWNTT IAVSMANIFR GSYLAGAGLA FSLMKSLGGG RRGTGAKGKH
2510 2520 2530 2540 2550
WERNGKDRLN QLSKSEFNTY KRSGIMEVDR SEAKEGLKRG ETTKHAVSRG
2560 2570 2580 2590 2600
TAKLRWFVER NLVKPEGKVI DLGCGRGGWS YYCAGLKKVT EVKGYTKGGP
2610 2620 2630 2640 2650
GHEEPIPMAT YGWNLVKLYS GKDVFFTPPE KCDTLLCDIG ESSPNPTIEE
2660 2670 2680 2690 2700
GRTLRVLKMV EPWLRGNQFC IKILNPYMPS VVETLEQMQR KHGGMLVRNP
2710 2720 2730 2740 2750
LSRNSTHEMY WVSCGTGNIV SAVNMTSRML LNRFTMAHRK PTYERDVDLG
2760 2770 2780 2790 2800
AGTRHVAVEP EVANLDIIGQ RIENIKHEHK STWHYDEDNP YKTWAYHGSY
2810 2820 2830 2840 2850
EVKPSGSASS MVNGVVKLLT KPWDAIPMVT QIAMTDTTPF GQQRVFKEKV
2860 2870 2880 2890 2900
DTRTPKAKRG TAQIMEVTAR WLWGFLSRNK KPRICTREEF TRKVRSNAAI
2910 2920 2930 2940 2950
GAVFVDENQW NSAKEAVEDE RFWDLVHRER ELHKQGKCAT CVYNMMGKRE
2960 2970 2980 2990 3000
KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFMNEDHWFS RENSLSGVEG
3010 3020 3030 3040 3050
EGLHKLGYIL RDISKIPGGN MYADDTAGWD TRITEDDLQN EAKITDIMEP
3060 3070 3080 3090 3100
EHALLATSIF KLTYQNKVVR VQRPAKNGTV MDVISRRDQR GSGQVGTYGL
3110 3120 3130 3140 3150
NTFTNMEAQL IRQMESEGIF SPSELETPNL AERVLDWLEK YGVERLKRMA
3160 3170 3180 3190 3200
ISGDDCVVKP IDDRFATALT ALNDMGKVRK DIPQWEPSKG WNDWQQVPFC
3210 3220 3230 3240 3250
SHHFHQLIMK DGREIVVPCR NQDELVGRAR VSQGAGWSLR ETACLGKSYA
3260 3270 3280 3290 3300
QMWQLMYFHR RDLRLAANAI CSAVPVDWVP TSRTTWSIHA HHQWMTTEDM
3310 3320 3330 3340 3350
LSVWNRVWIE ENPWMEDKTH VSSWEDVPYL GKREDQWCGS LIGLTARATW
3360 3370 3380 3390
ATNIQVAINQ VRRLIGNENY LDYMTSMKRF KNESDPEGAL W
Length:3,391
Mass (Da):379,086
Last modified:September 27, 2017 - v2
Checksum:i6F24E1E8FC56AE5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87512 Genomic RNA No translation available.
PIRiA42551

Similar proteinsi

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87512 Genomic RNA No translation available.
PIRiA42551

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L6PX-ray2.20A1393-1439[»]
A1475-1499[»]
3LKWX-ray2.00A1393-1439[»]
A1475-1499[»]
ProteinModelPortaliP33478
SMRiP33478
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001

Proteomic databases

PRIDEiP33478

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG090001ER

Miscellaneous databases

PROiPR:P33478

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
cd00079 HELICc, 1 hit
cd06174 MFS, 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, 1 hit
3.30.387.10, 1 hit
3.30.67.10, 1 hit
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
IPR020846 MFS_dom
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_DEN1S
AccessioniPrimary (citable) accession number: P33478
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: September 27, 2017
Last modified: November 7, 2018
This is version 161 of the entry and version 2 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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