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Protein

Genome polyprotein

Gene
N/A
Organism
Tick-borne encephalitis virus (strain Hypr) (TBEV)
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.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 immune response.By similarity
Non-structural protein 2B: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.PROSITE-ProRule annotation
Non-structural protein 4A: 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 (-) genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:18042258). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:18042258).By similarity1 Publication

Miscellaneous

The non-structural protein NS1 presents 2. alternative cleavage sites for its C-terminus (either at position 1128 or at 1190), which may define a soluble or a membrane-bound form of NS1.

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 sitei1543Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1567Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1627Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1949Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1952Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2524mRNA capPROSITE-ProRule annotation1
Binding sitei2527mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2528mRNA capPROSITE-ProRule annotation1
Binding sitei2530mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2535mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2539mRNA capPROSITE-ProRule annotation1
Binding sitei2567S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2572For 2'-O-MTase activityBy similarity1
Sitei2572Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2597S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2598S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2615S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2616S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2642S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2643S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2657For 2'-O-MTase activityBy similarity1
Sitei2657Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2658S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2661mRNA capPROSITE-ProRule annotation1
Active sitei2694For 2'-O-MTase activityBy similarity1
Sitei2694Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2725mRNA capPROSITE-ProRule annotation1
Binding sitei2727mRNA capPROSITE-ProRule annotation1
Active sitei2730For 2'-O-MTase activityBy similarity1
Sitei2730Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2732S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2950Zinc 1By similarity1
Metal bindingi2954Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2959Zinc 1By similarity1
Metal bindingi2962Zinc 1By similarity1
Metal bindingi3224Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3240Zinc 2By similarity1
Metal bindingi3359Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1688 – 1695ATPPROSITE-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 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 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

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):
Non-structural protein 5
OrganismiTick-borne encephalitis virus (strain Hypr) (TBEV)
Taxonomic identifieri70733 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Ixodes persulcatus (Taiga tick) [TaxID: 34615]
Ixodes ricinus (Common tick) [TaxID: 34613]
Proteomesi
  • UP000007400 Componenti: Genome

Subcellular locationi

Capsid protein C :
  • Virion By similarity
  • Host nucleus By similarity
  • host perinuclear region By similarity
  • Host cytoplasm 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 domaini1 – 98CytoplasmicSequence analysisAdd BLAST98
Transmembranei99 – 119HelicalSequence analysisAdd BLAST21
Topological domaini120 – 242ExtracellularSequence analysisAdd BLAST123
Transmembranei243 – 260HelicalSequence analysisAdd BLAST18
Topological domaini261CytoplasmicSequence analysis1
Transmembranei262 – 280HelicalSequence analysisAdd BLAST19
Topological domaini281 – 727ExtracellularSequence analysisAdd BLAST447
Transmembranei728 – 748HelicalSequence analysisAdd BLAST21
Topological domaini749 – 755Extracellular7
Transmembranei756 – 776HelicalCuratedAdd BLAST21
Topological domaini777 – 1132ExtracellularSequence analysisAdd BLAST356
Transmembranei1133 – 1153HelicalSequence analysisAdd BLAST21
Topological domaini1154 – 1158CytoplasmicSequence analysis5
Transmembranei1159 – 1179HelicalSequence analysisAdd BLAST21
Topological domaini1180 – 1187LumenalSequence analysis8
Transmembranei1188 – 1208HelicalSequence analysisAdd BLAST21
Topological domaini1209 – 1293CytoplasmicSequence analysisAdd BLAST85
Transmembranei1294 – 1314HelicalSequence analysisAdd BLAST21
Topological domaini1315 – 1327LumenalSequence analysisAdd BLAST13
Transmembranei1328 – 1348HelicalSequence analysisAdd BLAST21
Topological domaini1349 – 1359CytoplasmicSequence analysisAdd BLAST11
Transmembranei1360 – 1377HelicalSequence analysisAdd BLAST18
Topological domaini1378 – 1382LumenalSequence analysis5
Transmembranei1383 – 1403HelicalSequence analysisAdd BLAST21
Topological domaini1404 – 1454CytoplasmicSequence analysisAdd BLAST51
Intramembranei1455 – 1475HelicalSequence analysisAdd BLAST21
Topological domaini1476 – 2160CytoplasmicSequence analysisAdd BLAST685
Transmembranei2161 – 2181HelicalSequence analysisAdd BLAST21
Topological domaini2182 – 2189LumenalSequence analysis8
Intramembranei2190 – 2210HelicalSequence analysisAdd BLAST21
Topological domaini2211LumenalSequence analysis1
Transmembranei2212 – 2232HelicalSequence analysisAdd BLAST21
Topological domaini2233 – 2244CytoplasmicSequence analysisAdd BLAST12
Transmembranei2245 – 2265Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2266 – 2299LumenalSequence analysisAdd BLAST34
Intramembranei2300 – 2320HelicalSequence analysisAdd BLAST21
Topological domaini2321 – 2343LumenalSequence analysisAdd BLAST23
Intramembranei2344 – 2364HelicalSequence analysisAdd BLAST21
Topological domaini2365 – 2368LumenalSequence analysis4
Transmembranei2369 – 2389HelicalSequence analysisAdd BLAST21
Topological domaini2390 – 2432CytoplasmicSequence analysisAdd BLAST43
Transmembranei2433 – 2453HelicalSequence analysisAdd BLAST21
Topological domaini2454 – 2477LumenalSequence analysisAdd BLAST24
Transmembranei2478 – 2498HelicalSequence analysisAdd BLAST21
Topological domaini2499 – 3414CytoplasmicSequence analysisAdd BLAST916

GO - Cellular componenti

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2733 – 2734YS → AA: Relocalizes RNA-directed RNA polymerase NS5 away from the host cell membrane and nucleus. Reduced JAK-STAT signalling inhibition and IFN inhibition. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004051671 – 3414Genome polyproteinAdd BLAST3414
ChainiPRO_00000377931 – 96Capsid protein CBy similarityAdd BLAST96
PropeptideiPRO_000040516897 – 117ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST21
ChainiPRO_0000405169118 – 280Protein prMBy similarityAdd BLAST163
ChainiPRO_0000037794118 – 205Peptide prBy similarityAdd BLAST88
ChainiPRO_0000037795206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037796281 – 776Envelope protein EBy similarityAdd BLAST496
ChainiPRO_0000037797777 – 1128Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000377981129 – 1358Non-structural protein 2ABy similarityAdd BLAST230
ChainiPRO_00000377991359 – 1489Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000378001490 – 2110Serine protease NS3By similarityAdd BLAST621
ChainiPRO_00000378012111 – 2236Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051702237 – 2259Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000378022260 – 2511Non-structural protein 4BBy similarityAdd BLAST252
ChainiPRO_00000378032512 – 3414RNA-directed RNA polymerase NS5By similarityAdd BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi144N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Disulfide bondi340 ↔ 396By similarity
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 401By similarity
Disulfide bondi372 ↔ 396By similarity
Glycosylationi434N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotationBy similarity1
Disulfide bondi466 ↔ 570By similarity
Disulfide bondi587 ↔ 618By similarity
Disulfide bondi780 ↔ 791By similarity
Disulfide bondi831 ↔ 920By similarity
Glycosylationi861N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi955 ↔ 1000By similarity
Glycosylationi983N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi999N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi1057 ↔ 1106By similarity
Disulfide bondi1068 ↔ 1090By similarity
Disulfide bondi1089 ↔ 1093By similarity
Modified residuei2567PhosphoserineBy 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
Sitei96 – 97Cleavage; by viral protease NS3By similarity2
Sitei117 – 118Cleavage; by host signal peptidaseBy similarity2
Sitei205 – 206Cleavage; by host furinBy similarity2
Sitei280 – 281Cleavage; by host signal peptidaseBy similarity2
Sitei776 – 777Cleavage; by host signal peptidaseBy similarity2
Sitei1128 – 1129Cleavage; by hostBy similarity2
Sitei1358 – 1359Cleavage; by viral protease NS3By similarity2
Sitei1489 – 1490Cleavage; by autolysisBy similarity2
Sitei2110 – 2111Cleavage; by autolysisBy similarity2
Sitei2236 – 2237Cleavage; by viral protease NS3By similarity2
Sitei2259 – 2260Cleavage; by host signal peptidaseBy similarity2
Sitei2511 – 2512Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRIDEiQ01299

Interactioni

Subunit structurei

Capsid protein C: Homodimer (By similarity). Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity). Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (By similarity). Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi (By similarity). Interacts with protein prM. Interacts with non-structural protein 1 (By similarity). Non-structural protein 1: Homodimer; Homohexamer when secreted (By similarity). Interacts with envelope protein E. Non-structural protein 2A: Interacts (via N-terminus) with serine protease NS3 (By similarity). Non-structural protein 2B: Forms a heterodimer with serine protease NS3 (By similarity). May form homooligomers (By similarity). Serine protease NS3: Forms a heterodimer with NS2B. Interacts with NS4B (By similarity). Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). Non-structural protein 4B: Interacts with serine protease NS3 (By similarity). RNA-directed RNA polymerase NS5: Homodimer (By similarity). Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (By similarity). Interacts with serine protease NS3 (By similarity). Interacts with host SCRIB; this interaction targets NS5 to the cell membrane periphery and nucleus, thereby allowing efficient host nuclear STAT1 inhibition (PubMed:18042258).By similarity1 Publication

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ01299
SMRiQ01299
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1490 – 1669Peptidase S7PROSITE-ProRule annotationAdd BLAST180
Domaini1675 – 1831Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1841 – 2000Helicase C-terminalPROSITE-ProRule annotationAdd BLAST160
Domaini2512 – 2776mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3040 – 3189RdRp catalyticPROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni378 – 391Fusion peptideBy similarityAdd BLAST14
Regioni1410 – 1449Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni2730 – 2734Interaction with host SCRIB1 Publication5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1779 – 1782DEAH boxPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1970 – 1973Poly-Asp4
Compositional biasi2201 – 2204Poly-Leu4

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

OrthoDBiVOG090000ZS

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.8.970, 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
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
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
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 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
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit
TIGRFAMsiTIGR04240 flavi_E_stem, 1 hit
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.

Q01299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKKAILKGK GGGPPRRVSK ETATKTRQPR VQMPNGLVLM RMMGILWHAV
60 70 80 90 100
AGTARNPVLK AFWNSVPLKQ ATAALRKIKR TVSALMVGLQ KRGKRRSATD
110 120 130 140 150
WMSWLLVITL LGMTIAATVR KERDGSTVIR AEGKDAATQV RVENGTCVIL
160 170 180 190 200
ATDMGSWCDD SLSYECVTID QGEEPVDVDC FCRNVDGVYL EYGRCGKQEG
210 220 230 240 250
SRTRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW VWKNRLLALA
260 270 280 290 300
MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
310 320 330 340 350
VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAQTREYC LHAKLSDTKV
360 370 380 390 400
AARCPTMGPA TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA
410 420 430 440 450
CEAKKKATGH VYDANKIVYT VKVEPHTGDY VAANETHSGR KTASFTVSSE
460 470 480 490 500
KTILTMGEYG DVSLLCRVAS GVDLAQTVIL ELDKTVEHLP TAWQVHRDWF
510 520 530 540 550
NDLALPWKHE GARNWNNAER LVEFGAPHAV KMDVYNLGDQ TGVLLKALAG
560 570 580 590 600
VPVAHIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRAPTD
610 620 630 640 650
SGHDTVVMEV TFSGTKPCRI PVRAVAHGSP DVNVAMLITP NPTIENNGGG
660 670 680 690 700
FIEMQLPPGD NIIYVGELSY QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA
710 720 730 740 750
WDFGSAGGFL SSIGKALHTV LGGAFNSIFG GVGFLPKLLL GVALAWLGLN
760 770 780 790 800
MRNPTMSMSF LLAGVLVLAM TLGVGADVGC AVDTERMELR CGEGLVVWRE
810 820 830 840 850
VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE MAMWRSSVTE
860 870 880 890 900
LNLALAEGEA NLTVMVDKFD PTDYRGGVPG LLKKGKDIKV SWKSWGHSMI
910 920 930 940 950
WSIPEAPRRF MVGTEGQSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE
960 970 980 990 1000
PTHECDTGVM GAAVKNGMAI HTDQSLWMRS MKNDTGTYIV ELLVTDLRNC
1010 1020 1030 1040 1050
SWPASHTIDN ADVVDSELFL PASLAGPRSW YNRIPGYSEQ VKGPWKHTPI
1060 1070 1080 1090 1100
RVIREECPGT TVTINAKCDK RGASVRSTTE SGKVIPEWCC RACTMPPVTF
1110 1120 1130 1140 1150
RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP GIVALFVVLE
1160 1170 1180 1190 1200
YIIRRRPSTG STVVWGGIVV LALLVTGMVR MESLVRYVVA VGITFHLELG
1210 1220 1230 1240 1250
PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPS
1260 1270 1280 1290 1300
ANLEDFWKWG DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG
1310 1320 1330 1340 1350
LVCFLSAASA CSIWRLLRGH REQKGLTWIV PLARLLGGEG SGIRLLAFWE
1360 1370 1380 1390 1400
LSAHRGRRSF SEPLTVVGVM LTLASGMMRH TSQEALCALA VASFLLLMLV
1410 1420 1430 1440 1450
LGTRKMQLVA EWSGCVEWHP ELVNEGGEVS LRVRQDAMGN FHLTELEKEE
1460 1470 1480 1490 1500
RMMAFWLIAG LAASAIHWSG IIGVMGLWTL TKMLRSSRRS DLVFSGQGGR
1510 1520 1530 1540 1550
ERGDRPFEVK DGVYRIFSPG LFWGQNQVGV GYGSKGVLHT MWHVTRGAAL
1560 1570 1580 1590 1600
SIDDAVAGPY WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGKAHEVH
1610 1620 1630 1640 1650
QCQPGELILD TGRKLGAIPI DLVKGTSGSP ILNAQGVVVG LYGNGLKTNE
1660 1670 1680 1690 1700
TYVSSIAQGE AEKSRPNLPQ AVVGTGWTSK GQITVLDMHP GSGKTHRVLP
1710 1720 1730 1740 1750
ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP AVSDQQAGGA
1760 1770 1780 1790 1800
IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
1810 1820 1830 1840 1850
ENKCALVLMT ATPPGKSEPF PESNGAITSE ERQIPNGEWR DGFDWITEYE
1860 1870 1880 1890 1900
GRTAWFVPSI AKGGAIARTL RQKGKSVICL NSKTFEKDYS RVRDEKPDFV
1910 1920 1930 1940 1950
VTTDISEMGA NLDVSRVIDG RTNIKPEEVD GKVELTGTRR VTTASAAQRR
1960 1970 1980 1990 2000
GRVGRQDGRT DEYIYSGQCD DDDSGLVQWK EAQILLDNIT TLRGPVATFY
2010 2020 2030 2040 2050
GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH VAANVSSVTD
2060 2070 2080 2090 2100
RSWTWEGPEA NAVDEASGGL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK
2110 2120 2130 2140 2150
EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEKPDSRAM
2160 2170 2180 2190 2200
RMAERDAPEA FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS
2210 2220 2230 2240 2250
LLLLWAGGVG YGNMAGVALI FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL
2260 2270 2280 2290 2300
CSLAGLVAAN EMGFLEKTKA DLSTVLWSER EEPRPWSEWT NVDIQPARSW
2310 2320 2330 2340 2350
GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ASGAQAMRDL GGGAPFFGVA
2360 2370 2380 2390 2400
GHVMTLGVVS LIGATPTSLM VGVGLAALHL AIVVSGLEAE LTQRAHKVFF
2410 2420 2430 2440 2450
SAMVRNPMVD GDVINPFGEG EAKPALYERR MSLVLAIVLC LMSVVMNRTV
2460 2470 2480 2490 2500
ASITEASAVG LAAAGQLLRP EADTLWTMPV ACGMSGVVRG SLWGFLPLGH
2510 2520 2530 2540 2550
RLWLRASGGR RGGSEGDTLG DLWKRRLNNC TREEFFVYRR TGILETERDK
2560 2570 2580 2590 2600
ARELLRRGET NMGLAVSRGT AKLAWLEERG YATLKGEVVD LGCGRGGWSY
2610 2620 2630 2640 2650
YAASRPAVMS VRAYTIGGRG HEAPKMVTSL GWNLIKFRSG MDVFSMQPHR
2660 2670 2680 2690 2700
ADTVMCDIGE SSPDAAVEGE RTRKVILLME QWKNRNPTAA CVFKVLAPYR
2710 2720 2730 2740 2750
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAVTGN IVNSVNVQSR
2760 2770 2780 2790 2800
KLLARFGDQR GPTRVPELDL GVGTRCVVLA EDKVKEQDVQ ERIKALREQY
2810 2820 2830 2840 2850
SETWHMDEEH PYRTWQYWGS YRTAPTGSAA SLINGVVKLL SWPWNAREDV
2860 2870 2880 2890 2900
VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP GTRVIMRAVN DWILERLAQK
2910 2920 2930 2940 2950
SKPRMCSREE FIAKVKSNAA LGAWSDEQNR WASAREAVED PAFWHLVDEE
2960 2970 2980 2990 3000
RERHLMGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
3010 3020 3030 3040 3050
LGFLNEDHWA SRESSGAGVE GISLNYLGWH LKKLSTLNGG LFYADDTAGW
3060 3070 3080 3090 3100
DTKVTNADLE DEEQILRYME GEHKQLATTI MQKAYHAKVV KVARPSRDGG
3110 3120 3130 3140 3150
CIMDVITRRD QRGSGQVVTY ALNTLTNIKV QLIRMMEGEG VIEAADAHNP
3160 3170 3180 3190 3200
RLLRVERWLK EHGEERLGRM LVSGDDCVVR PLDDRFGKAL YFLNDMAKTR
3210 3220 3230 3240 3250
KDIGEWEHSA GLSSWEEVPF CSHHFHELVM KDGRTLVVPC RDQDELVGRA
3260 3270 3280 3290 3300
RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPVDWV
3310 3320 3330 3340 3350
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKG KVMEWRDVPY
3360 3370 3380 3390 3400
LPKAQDMLCS SLVGRKERAE WAKNIWGAVE KVRKMIGPEK FKDYLSCMDR
3410
HDLHWELRLE SSII
Length:3,414
Mass (Da):378,545
Last modified:October 1, 1996 - v1
Checksum:iEC0B1A5325A08C19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39292 Genomic RNA Translation: AAB53095.1
M76660 Genomic RNA Translation: AAA47904.1

Similar proteinsi

Entry informationi

Entry nameiPOLG_TBEVH
AccessioniPrimary (citable) accession number: Q01299
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 20, 2018
This is version 141 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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