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Protein

Genome polyprotein

Gene
N/A
Organism
St. louis encephalitis virus (strain MS1-7)
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 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral 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.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. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.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.By similarity
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 sitei1550Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1574Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1634Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1956Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1959Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2537mRNA capPROSITE-ProRule annotation1
Binding sitei2540mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2541mRNA capPROSITE-ProRule annotation1
Binding sitei2543mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2548mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2552mRNA capPROSITE-ProRule annotation1
Binding sitei2580S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2585For 2'-O-MTase activityBy similarity1
Sitei2585Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2610S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2628S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2629S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2655S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2656S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2670For 2'-O-MTase activityBy similarity1
Sitei2670Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2671S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2674mRNA capPROSITE-ProRule annotation1
Active sitei2706For 2'-O-MTase activityBy similarity1
Sitei2706Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2737mRNA capPROSITE-ProRule annotation1
Binding sitei2739mRNA capPROSITE-ProRule annotation1
Active sitei2742For 2'-O-MTase activityBy similarity1
Sitei2742Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2744S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2964Zinc 1By similarity1
Metal bindingi2968Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2973Zinc 1By similarity1
Metal bindingi2976Zinc 1By similarity1
Metal bindingi3241Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3257Zinc 2By similarity1
Metal bindingi3376Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1693 – 1700ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processClathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, mRNA capping, mRNA processing, Transcription, Transcription regulation, 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

MEROPSiS07.003

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
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):
NS5
OrganismiSt. louis encephalitis virus (strain MS1-7)
Taxonomic identifieri11081 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Virus hostiAgelaius tricolor (Tricolored blackbird) [TaxID: 9191]
Cardinalis cardinalis (Northern cardinal) [TaxID: 98964]
Columba livia (Rock dove) [TaxID: 8932]
Culex nigripalpus [TaxID: 42429]
Culex pipiens (House mosquito) [TaxID: 7175]
Culex quinquefasciatus (Southern house mosquito) (Culex pungens) [TaxID: 7176]
Culex tarsalis (Encephalitis mosquito) [TaxID: 7177]
Cyanocitta cristata (Blue jay) [TaxID: 28727]
Euphagus cyanocephalus (Brewer's blackbird) [TaxID: 84817]
Haemorhous mexicanus (House finch) (Carpodacus mexicanus) [TaxID: 30427]
Homo sapiens (Human) [TaxID: 9606]
Mimus polyglottos (Northern mockingbird) [TaxID: 60713]
Passer domesticus (House sparrow) (Fringilla domestica) [TaxID: 48849]
Turdus migratorius (American robin) [TaxID: 9188]
Zenaida macroura (Mourning dove) [TaxID: 47245]

Subcellular locationi

Capsid protein C :
  • Virion By similarity
  • Host nucleus By similarity
  • Host cytoplasm By similarity
  • host perinuclear region By similarity
Peptide pr :
  • Secreted By similarity
Small envelope protein M :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Note: ER membrane retention is mediated by the transmembrane domains.By similarity
Envelope protein E :
  • Virion membrane Curated; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Note: ER membrane retention is mediated by the transmembrane domains.By similarity
Non-structural protein 1 :
  • Secreted By similarity
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
Non-structural protein 2A :
Serine protease subunit NS2B :
Serine protease NS3 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Note: Remains non-covalently associated to serine protease subunit NS2B.PROSITE-ProRule annotation
Non-structural protein 4A :
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Note: Located in RE-associated vesicles hosting the replication complex.By similarity
Non-structural protein 4B :
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Host nucleus By similarity
  • Note: Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 108CytoplasmicSequence analysisAdd BLAST107
Transmembranei109 – 129HelicalSequence analysisAdd BLAST21
Topological domaini130 – 247ExtracellularSequence analysisAdd BLAST118
Transmembranei248 – 268HelicalSequence analysisAdd BLAST21
Topological domaini269 – 273CytoplasmicSequence analysis5
Transmembranei274 – 288HelicalCuratedAdd BLAST15
Topological domaini289 – 741ExtracellularSequence analysisAdd BLAST453
Transmembranei742 – 762HelicalSequence analysisAdd BLAST21
Topological domaini763 – 768CytoplasmicSequence analysis6
Transmembranei769 – 789HelicalSequence analysisAdd BLAST21
Topological domaini790 – 1214ExtracellularSequence analysisAdd BLAST425
Transmembranei1215 – 1235HelicalSequence analysisAdd BLAST21
Topological domaini1236 – 1245CytoplasmicSequence analysis10
Transmembranei1246 – 1266HelicalSequence analysisAdd BLAST21
Topological domaini1267 – 1288LumenalSequence analysisAdd BLAST22
Transmembranei1289 – 1303HelicalSequence analysisAdd BLAST15
Topological domaini1304CytoplasmicSequence analysis1
Transmembranei1305 – 1325HelicalSequence analysisAdd BLAST21
Topological domaini1326 – 1339LumenalSequence analysisAdd BLAST14
Transmembranei1340 – 1360HelicalSequence analysisAdd BLAST21
Topological domaini1361 – 1369CytoplasmicSequence analysis9
Transmembranei1370 – 1390HelicalSequence analysisAdd BLAST21
Topological domaini1391 – 1393LumenalSequence analysis3
Transmembranei1394 – 1414HelicalSequence analysisAdd BLAST21
Topological domaini1415 – 1471CytoplasmicSequence analysisAdd BLAST57
Intramembranei1472 – 1492HelicalSequence analysisAdd BLAST21
Topological domaini1493 – 2167CytoplasmicSequence analysisAdd BLAST675
Transmembranei2168 – 2188HelicalSequence analysisAdd BLAST21
Topological domaini2189 – 2193LumenalSequence analysis5
Intramembranei2194 – 2214HelicalSequence analysisAdd BLAST21
Topological domaini2215LumenalSequence analysis1
Transmembranei2216 – 2236HelicalSequence analysisAdd BLAST21
Topological domaini2237 – 2251CytoplasmicSequence analysisAdd BLAST15
Transmembranei2252 – 2266Helical; Note=Signal for NS4BSequence analysisAdd BLAST15
Topological domaini2267 – 2308LumenalSequence analysisAdd BLAST42
Intramembranei2309 – 2329HelicalSequence analysisAdd BLAST21
Topological domaini2330 – 2376LumenalSequence analysisAdd BLAST47
Transmembranei2377 – 2397HelicalSequence analysisAdd BLAST21
Topological domaini2398 – 2440CytoplasmicSequence analysisAdd BLAST43
Transmembranei2441 – 2461HelicalSequence analysisAdd BLAST21
Topological domaini2462 – 2466LumenalSequence analysis5
Transmembranei2467 – 2487HelicalSequence analysisAdd BLAST21
Topological domaini2488 – ›3412CytoplasmicSequence analysisAdd BLAST›925

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004051431 – ›3412Genome polyproteinAdd BLAST›3412
ChainiPRO_00000377351 – 103Capsid protein CBy similarityAdd BLAST103
PropeptideiPRO_0000405144104 – 121ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000405145122 – 288Protein prMBy similarityAdd BLAST167
ChainiPRO_0000037736122 – 213Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037737214 – 288Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037738289 – 789Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000037739790 – 1141Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000377401142 – 1368Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00000377411369 – 1499Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000377421500 – 2117Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00004051462118 – 2243Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051472244 – 2266Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004051482267 – 2524Non-structural protein 4BBy similarityAdd BLAST258
ChainiPRO_00004051492525 – ›3412RNA-directed RNA polymerase NS5By similarityAdd BLAST›888

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi136N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi291 ↔ 318By similarity
Disulfide bondi348 ↔ 409By similarity
Disulfide bondi348 ↔ 404By similarity
Disulfide bondi362 ↔ 393By similarity
Disulfide bondi380 ↔ 409By similarity
Disulfide bondi380 ↔ 404By similarity
Disulfide bondi478 ↔ 576By similarity
Disulfide bondi593 ↔ 624By similarity
Disulfide bondi793 ↔ 804By similarity
Disulfide bondi844 ↔ 932By similarity
Glycosylationi919N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi964N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi968 ↔ 1012By similarity
Glycosylationi996N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1069 ↔ 1118By similarity
Disulfide bondi1080 ↔ 1102By similarity
Disulfide bondi1080 ↔ 1101By similarity
Disulfide bondi1101 ↔ 1105By similarity
Disulfide bondi1102 ↔ 1105By similarity
Modified residuei2580PhosphoserineBy 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: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei103 – 104Cleavage; by viral protease NS3By similarity2
Sitei121 – 122Cleavage; by host signal peptidaseBy similarity2
Sitei213 – 214Cleavage; by host furinBy similarity2
Sitei288 – 289Cleavage; by host signal peptidaseBy similarity2
Sitei789 – 790Cleavage; by host signal peptidaseBy similarity2
Sitei1141 – 1142Cleavage; by hostBy similarity2
Sitei1368 – 1369Cleavage; by viral protease NS3By similarity2
Sitei1499 – 1500Cleavage; by autolysisBy similarity2
Sitei2117 – 2118Cleavage; by autolysisBy similarity2
Sitei2243 – 2244Cleavage; by viral protease NS3By similarity2
Sitei2266 – 2267Cleavage; by host signal peptidaseBy similarity2
Sitei2524 – 2525Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRIDEiP09732

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. NS1 interacts with NS4B. Interacts with host complement protein CFH; this interaction leads to the degradation of C3. 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 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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FG0X-ray3.90A289-695[»]
ProteinModelPortaliP09732
SMRiP09732
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1500 – 1677Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1680 – 1836Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1847 – 2011Helicase C-terminalPROSITE-ProRule annotationAdd BLAST165
Domaini2525 – 2790mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3054 – 3206RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni386 – 399Fusion peptideBy similarityAdd BLAST14
Regioni1422 – 1461Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1684 – 1687Important for RNA-bindingBy similarity4
Regioni2162 – 2166Regulates the ATPase activity of NS3 helicaseBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1784 – 1787DEAH boxPROSITE-ProRule annotation4

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

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, 1 hit
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
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
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: Fragment.

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

P09732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKPGKPGR NRVVNMLKRG VSRVNPLTGL KRILGSLLDG RGPVRFILAI
60 70 80 90 100
LTFFRFTALQ PTEALKRRWR AVDKRTALKH LNGFKRDLGS MLDTINRRPS
110 120 130 140 150
KKRGGTRSLL GLAALIGLAS SLQLSTYQGK VLMSINKTDA QSAINIPSAN
160 170 180 190 200
GANTCIVRAL DVGVMCKNDI TYLCPVLSAG NDPEDIDCWC DVEEVWVHYG
210 220 230 240 250
RCTRMGHSRR SRRSISVQHH GDSTLATKNT PWLDTVKTTK YLTKVENWVL
260 270 280 290 300
RNPGYALVAL AIGWMLGSNN TQRVVFVIML MLIAPAYSFN CLGTSNRDFV
310 320 330 340 350
EGASGATWID LVLEGGSCVT VMAPEKPTLD FKVMKMEATE LATVREYCYE
360 370 380 390 400
ATLDTLSTVA RCPTTGEAHN TKRSDPTFVC KRDVVDRGWG NGCGLFGKGS
410 420 430 440 450
IDTCAKFTCK NKATGKTILR ENIKYEVAIF VHGSTDSTSH GNYFEQIGKN
460 470 480 490 500
QAARFTISPQ APSFTANMGE YGTVTIDCEA RSGINTEDYY VFTVKEKSWL
510 520 530 540 550
VNRDWFHDLN LPWTSPATTD WRNRETLVEF EEPHATKQTV VALGSQEGAL
560 570 580 590 600
HTALAGAIPA TVSSSTLTLQ SGHLKCRAKL DKVKIKGTTY GMCDSAFTFS
610 620 630 640 650
KNPADTGHGT VIVELQYTGS NGPCRVPISV TANLMDLTPV GRLVTVNPFI
660 670 680 690 700
STGGANNKVM IEVEPPFGDS YIVVGRGTTQ INYHWHKEGS SIGKALATTW
710 720 730 740 750
KGAQRLAVLG DTAWDFGSIG GVFNSIGKAV HQVFGGAFRT LFGGMSWITQ
760 770 780 790 800
GLLGALLLWM GLQARDRSIS LTLLAVGGIL IFLATSVQAD SGCAIDLQRR
810 820 830 840 850
ELKCGGGIFV YNDVEKWKSD YKYFPLTPTG LAHVIQEAHA NGICGIRSTS
860 870 880 890 900
RLEHLMWENI QRELNAIFED NEIDLSVVVQ EDPKYYKRAP RRLKKLEDEL
910 920 930 940 950
DYGWKKWGKT LFVEPRLGNN TFVVDGPETK ECPTANRAWN SFKVEDFGFG
960 970 980 990 1000
MVFTRLWLTI REENTTECDS AIIGTAIKGD RAVHSDLSYW IESKKNETWQ
1010 1020 1030 1040 1050
LERAVMGEVK SCTWPETHTL WGDGVVESEM IIPVTLGGPK SHHNKRNGYH
1060 1070 1080 1090 1100
TQTKGPWSEG EITLDFDYCP GTTVTVTEHC GNRGASLRTT TASGKLVTDW
1110 1120 1130 1140 1150
CCRSCSLPPL RYTTKDGCWY GMEIRPVKEE EAKLVKSRVT AGVAGGMEPF
1160 1170 1180 1190 1200
QLGLLVAFIA TQEVLKRRWT GKLTLTSLAV CLALLIFGNL TYMDLVRYLV
1210 1220 1230 1240 1250
LVGTAFAEMN TGGDVIHLAL VAVFKVQPAF LAGLFLRMQW SNQENILMVI
1260 1270 1280 1290 1300
GAAFLQMAAN DLKLEVLPIL NAMSIAWMLI RAMKEGKVAM YALPILCALT
1310 1320 1330 1340 1350
PGMRMAGLDV IRCLLLIIGI VTLLNERRES VAKKKGGYLL AAALCQAGVC
1360 1370 1380 1390 1400
SPLIMMGGLI LAHPNGKRSW PASEVLTGVG LMCALAGGLL EFEETSMVVP
1410 1420 1430 1440 1450
FAIAGLMYIT YTVSGKAAEM WIEKAADITW EQNAEITGTS PRLDVDLDSH
1460 1470 1480 1490 1500
GNFKLLNDPG APVHLFALRF ILLGLSARFH WFIPFGVLGF WLLGKHSKRG
1510 1520 1530 1540 1550
GALWDVPSPK VYPKCETKPG IYRIMTRGIL GTFQAGVGVM HEGVFHTMWH
1560 1570 1580 1590 1600
ATEGAVLRNG EGRLDPYAGD VRNDLISYGG PWKLSATWDG TEEVQMIAVA
1610 1620 1630 1640 1650
PGKPAINVQT TPGVFKTPFG TIGAVTLDFP KGTSGSPIIN KKGEIIGLYG
1660 1670 1680 1690 1700
NGVLIGQGEY VSGIIQGERT EEPIPDAYNE EMLRKRKLTV LELHPGAGKT
1710 1720 1730 1740 1750
RKVLPQIIKD CIQKRLRTAV LAPTRVVACE IAEALKGLPI RYLTPAVRNE
1760 1770 1780 1790 1800
HQGNEIVDVM CHATLTQKLL TPTRVPNYQV YIMDEAHFID PASIAARGYI
1810 1820 1830 1840 1850
STKVELGEAA AIFMTATPPG TNDPFPDSNS PILDVEAQVP DKAWSTGYEW
1860 1870 1880 1890 1900
ITNFTGRTVW FVPSVKSGNE IAICLQKAGK RVIQLNRKSF DTEYPKTKNN
1910 1920 1930 1940 1950
EWDFVVTTDI SEMGANFGAH RVIDSRKCVK PVILEDDDRV ILNGPMAITS
1960 1970 1980 1990 2000
ASAAQRRGRI GRNPSQIGDE YHYGGATNED DHDLANWTEA KILLDNIYLP
2010 2020 2030 2040 2050
NGLVAQMYQP ERDKVFTMDG EFRLRGEERK NFVELMRNGD LPVWLAYKVA
2060 2070 2080 2090 2100
SNGHSYQDRS WCFTGQTNNT ILEDNNEVEV FTKTGDRKIL RPKWMDARVC
2110 2120 2130 2140 2150
CDYQALKSFK EFAAGKRSAL GMMEVMGRMP NHFWEKTVAA ADTLYLLGTS
2160 2170 2180 2190 2200
EANSRAHKEA LAELPDSLET LLLIGMLCVM SMGTFIFLMN RKGVGKMGLG
2210 2220 2230 2240 2250
AFVMTLATAL LWAAEVPGTQ IAGVLLIVFL LMIVLIPEPE KQRSQTDNQL
2260 2270 2280 2290 2300
AVFLICIMTL MGVVAANEMG LLEKTKSDIA KLFGSQPGSV GFATRTTPWD
2310 2320 2330 2340 2350
ISLDIKPATA WALYAAATMV MTPLIKHLIT TQYVNFSLTA IASQAGVLLG
2360 2370 2380 2390 2400
LTNGMPFTAM DLSVPLLVLG CWNQMTLPSL AVAVMLLAIH YAFMIPGWQA
2410 2420 2430 2440 2450
EAMRAAQRRT AAGIMKNAVV DGIVATDIPD LSPATPMTEK KMGQILLIAA
2460 2470 2480 2490 2500
AVLAVLVRPG ICSIKEFGVL GSAALVTLIE GTAGVVWNCT TAVGLCNLMR
2510 2520 2530 2540 2550
GGWLAGMSIT WTVYKNVDKP KGKRGGGKGA TLGEIWKSRL NQLTRAEFMA
2560 2570 2580 2590 2600
YRKDGIVEVD RAPARKARRE GRLTGGHPVS RGSAKLRWIT ERGFVKPMGK
2610 2620 2630 2640 2650
VVDLGCGRGG WSYYCATLKH VQEVKGFTKG GPGHEEPQLM QSYGWNLVHM
2660 2670 2680 2690 2700
KSGVDVFHKP AEPADTVLCD IGESNPSCEV EEARTARVLD MVEEWLKKGA
2710 2720 2730 2740 2750
TEFCIKVLCP YTPKIIEKLE KLQRKYGGGL VRVPLSRNST HEMYWVSGAA
2760 2770 2780 2790 2800
GNIIHAVSMT SQVLMGRMDK QNRSGPRYEE DVNLGSGTRS VGKLTEKPDL
2810 2820 2830 2840 2850
RKVGERIRRL REEYQQTWTY DHNNPYRTWN YHGSYEVKPT GSASSMVNGV
2860 2870 2880 2890 2900
VRLLSKPWDM ITNVTTMAMT DTTPFGQQRV FKEKVDTKAP EPPLGVAQIM
2910 2920 2930 2940 2950
DVTTDWLWDF VAREKKPRVC TPEEFKAKVN SHAALGAMFE EQNQWSSARE
2960 2970 2980 2990 3000
AVEDPKFWEM VDEEREAHLK GECHTCIYNM MGKREKKTGE FGKAKGSRAI
3010 3020 3030 3040 3050
WYMWLGARFL EFEALGFLNE DHWMSRENSY GGVEGKGLQK LGYILQEISQ
3060 3070 3080 3090 3100
IPGGKMYADD TAGWDTRITK EDLKNEAKIT KRMEERHRKL AEAIIDLTYR
3110 3120 3130 3140 3150
HKVVKVMRPG PDGKTYMDVI SREDQRGSGQ VVTYALNTFT NLAVQLIRCM
3160 3170 3180 3190 3200
EAEGVVDEDD ITRVRLGRLA KAVEWLRKNG PERLSRMAVS GDDCVVKPID
3210 3220 3230 3240 3250
DRFATALHFL NNMSKIRKDI QEWKPSTGWH NWQEVPFCSH HFNELMLKDG
3260 3270 3280 3290 3300
RTIVVPCRSQ DELIGRARIS PGAGWNVKET ACLSKSYAQM WLLMYFHRRD
3310 3320 3330 3340 3350
LRMMANAICS AVPVNWVPTG RTTWSIHGKG EWMTTEDMLS VWNRVWIEEN
3360 3370 3380 3390 3400
EYMKDKTPLA AWNDIPYLGK REDIWCGSLI GTRTRATWAE NIYAPIMQIR
3410
NLIGEEEYRD YM
Length:3,412
Mass (Da):378,483
Last modified:February 8, 2011 - v2
Checksum:iF89336D9D434A11F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei34121

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti47I → M. 1
Natural varianti164V → I. 1
Natural varianti168N → D. 1
Natural varianti249 – 250VL → FC. 2
Natural varianti346E → K. 1
Natural varianti444F → S. 1
Natural varianti604A → T. 1
Natural varianti796D → S. 1
Natural varianti843I → Y. 1
Natural varianti955R → Q. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF158050 Genomic RNA Translation: ABN11812.1
M16614 Genomic RNA Translation: AAA47786.1

Similar proteinsi

Entry informationi

Entry nameiPOLG_STEVM
AccessioniPrimary (citable) accession number: P09732
Secondary accession number(s): A3EZ58
, Q88781, Q88782, Q88783, Q88784, Q88785, Q88786, Q88787, Q88788
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 8, 2011
Last modified: May 23, 2018
This is version 138 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
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Main funding by: National Institutes of Health