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Protein

Genome polyprotein

Gene
N/A
Organism
Tick-borne encephalitis virus Far Eastern subtype (strain Sofjin) (SOFV) (Sofjin virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. 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. 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 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 sitei2523mRNA capPROSITE-ProRule annotation1
Binding sitei2526mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2527mRNA capPROSITE-ProRule annotation1
Binding sitei2529mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2534mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2538mRNA capPROSITE-ProRule annotation1
Binding sitei2566S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2571For 2'-O-MTase activityBy similarity1
Sitei2571Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2596S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2597S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2615S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2641S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2642S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2656For 2'-O-MTase activityBy similarity1
Sitei2656Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2657S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2660mRNA capPROSITE-ProRule annotation1
Active sitei2693For 2'-O-MTase activityBy similarity1
Sitei2693Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2724mRNA capPROSITE-ProRule annotation1
Binding sitei2726mRNA capPROSITE-ProRule annotation1
Active sitei2729For 2'-O-MTase activityBy similarity1
Sitei2729Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2731S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2948Zinc 1By similarity1
Metal bindingi2952Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2957Zinc 1By similarity1
Metal bindingi2960Zinc 1By similarity1
Metal bindingi3222Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3238Zinc 2By similarity1
Metal bindingi3357Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1688 – 1695ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Methyltransferase, 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 Far Eastern subtype (strain Sofjin) (SOFV) (Sofjin virus)
Taxonomic identifieri11087 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirustick-borne encephalitis virus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Ixodes persulcatus (Taiga tick) [TaxID: 34615]
Ixodes ricinus (Common tick) [TaxID: 34613]
Proteomesi
  • UP000007401 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 – 755CytoplasmicSequence analysis7
Transmembranei756 – 776HelicalCuratedAdd BLAST21
Topological domaini777 – 1187ExtracellularSequence analysisAdd BLAST411
Transmembranei1188 – 1208HelicalSequence analysisAdd BLAST21
Topological domaini1209 – 1236CytoplasmicSequence analysisAdd BLAST28
Transmembranei1237 – 1257HelicalSequence analysisBy similarityAdd BLAST21
Topological domaini1258 – 1293LumenalSequence analysisBy similarityAdd BLAST36
Transmembranei1294 – 1314HelicalSequence analysisBy similarityAdd BLAST21
Topological domaini1315 – 1327CytoplasmicSequence analysisBy similarityAdd BLAST13
Transmembranei1328 – 1348HelicalSequence analysisBy similarityAdd BLAST21
Topological domaini1349 – 1359CytoplasmicSequence analysisBy similarityAdd BLAST11
Transmembranei1360 – 1378HelicalSequence analysisAdd BLAST19
Topological domaini1379 – 1382LumenalSequence analysis4
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 – 2430CytoplasmicSequence analysisAdd BLAST41
Transmembranei2431 – 2451HelicalSequence analysisAdd BLAST21
Topological domaini2452 – 2476LumenalSequence analysisAdd BLAST25
Transmembranei2477 – 2497HelicalSequence analysisAdd BLAST21
Topological domaini2498 – 3412CytoplasmicSequence analysisAdd BLAST915

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_00004051711 – 3412Genome polyproteinAdd BLAST3412
ChainiPRO_00000378041 – 96Capsid protein CBy similarityAdd BLAST96
PropeptideiPRO_000040517297 – 117ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST21
ChainiPRO_0000405173118 – 280Protein prMBy similarityAdd BLAST163
ChainiPRO_0000037805118 – 205Peptide prBy similarityAdd BLAST88
ChainiPRO_0000037806206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037807281 – 776Envelope protein EBy similarityAdd BLAST496
ChainiPRO_0000037808777 – 1128Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000378091129 – 1358Non-structural protein 2ABy similarityAdd BLAST230
ChainiPRO_00000378101359 – 1489Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000378111490 – 2110Serine protease NS3By similarityAdd BLAST621
ChainiPRO_00000378122111 – 2236Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051742237 – 2259Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000378132260 – 2510Non-structural protein 4BBy similarityAdd BLAST251
ChainiPRO_00000378142511 – 3412RNA-directed RNA polymerase NS5By similarityAdd BLAST902

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 residuei2566PhosphoserineBy 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.1 Publication
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
Sitei2510 – 2511Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

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 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. Interacts with host SCRIB; this interaction targets NS5 to the cell membrane periphery and nucleus, thereby allowing efficient host nuclear STAT1 inhibition.By similarity

GO - Molecular functioni

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K4Relectron microscopy24.00A/B/C281-675[»]
ProteinModelPortaliP07720.
SMRiP07720.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07720.

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
Domaini2511 – 2775mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3038 – 3187RdRp 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
Regioni2729 – 2733Interaction with host SCRIBBy similarity5

Motif

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi266 – 271Poly-Val6
Compositional biasi1970 – 1973Poly-Asp4

Domaini

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900014M.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
3.30.387.10. 1 hit.
3.30.67.10. 1 hit.
InterProiView protein in InterPro
IPR011492. DEAD_Flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR027287. Flavi_E_Ig-like.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like_sf.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR036253. Glycoprot_cen/dimer_sf.
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.

P07720-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKAILKGK GGGPPRRVSK ETAKKTRQSR VQMPNGLVLM RMMGILWHAV
60 70 80 90 100
AGTARSPVLK SFWKSVPLKQ ATAALRKIKK AVSTLMVGLQ RRGKRRSAVD
110 120 130 140 150
WTGWLLVVVL LGVTLAATVR KERDGTTVIR AEGKDAATQV RVENGTCVIL
160 170 180 190 200
ATDMGSWCDD SLTYECVTID QGEEPVDVDC SCRNVDGVYL EYGRCGKQEG
210 220 230 240 250
SRTRRSVLIP SHAQGDLTGR GHKWLEGDSL RTHLTRVEGW VWKNKVLTLA
260 270 280 290 300
VIAVVWLTVE SVVTRVAVVV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
310 320 330 340 350
VTLVLELGGC VTITAEGKPS MDVWLDSIYQ ENPAKTREYC LHAKLSDTKV
360 370 380 390 400
AARCPTMGPA TLAEEHQSGT VCKRDQSDRG WGNHCGLFGK GSIVTCVKAS
410 420 430 440 450
CEAKKKATGH VYDANKIVYT VKVEPHTGDY VAANETHSGR KTASFTVSSE
460 470 480 490 500
RTILTMGDYG DVSLLCRVAS GVDLAQTVIL ELDKTSEHLP TAWQVHRDWF
510 520 530 540 550
NDLALPWKHE GAQNWNNAER LVEFGAPHAV KMDVYNLGDQ TGVLLKSLAG
560 570 580 590 600
VPVAHIDGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRIPTD
610 620 630 640 650
SGHDTVVMEV AFSGTKPCRI PVRAVAHGSP DVNVAMLMTP NPTIENNGGG
660 670 680 690 700
FIEMQLPPGD NIIYVGELSH QWFQKGSSIG RVFQKTRKGI ERLTVIGEHA
710 720 730 740 750
WDFGSTGGFL TSVGKALHTV LGGAFNSLFG GVGFLPKILV GVVLAWLGLN
760 770 780 790 800
MRNPTMSMSF LLAGGLVLAM TLGVGADVGC AVDTERMELR CGEGLVVWRE
810 820 830 840 850
VSEWYDNYAY YPETLGALAS AIKETFEEGT CGIVPQNRLE MAMWRSSATE
860 870 880 890 900
LNLALVEGDA NLTVVVDKLD PTDYRGGIPS LLKKGKDIKV SWKSWGHSMI
910 920 930 940 950
WSVPEAPRLF MVGTEGSSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE
960 970 980 990 1000
STHECDTGVM GAAVKNGMAV HTDQSLWMKS VRNDTGTYIV ELLVTDLRNC
1010 1020 1030 1040 1050
SWPASHTIDN AEVVDSELFL PASLAGPRSW YNRIPGYSEQ VKGPWKYSPI
1060 1070 1080 1090 1100
RVTREECPGT RVTINADCDK RGASVRSTTE SGKVIPEWCC RTCTLPPVTF
1110 1120 1130 1140 1150
RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGIP GIVALFVVLE
1160 1170 1180 1190 1200
YVIRRRPATG TTAMWGGIVV LALLVTGLVK IESLVRYVVA VGITFHLELG
1210 1220 1230 1240 1250
PEIVALTLLQ AVFELRVGLL SAFALRSNLT VREMVTIYFL LLVLELGLPS
1260 1270 1280 1290 1300
EGLGALWKWG DALAMGALIF RACTAEEKTG VGLLLMALMT QQDLATVHYG
1310 1320 1330 1340 1350
LMLFLGVASC CSIWKLIRGH REQKGLTWIV PLAGLLGGEG SGVRLVAFWE
1360 1370 1380 1390 1400
LTVHGRRRSF SEPLTVVGVM LTLASGMIRH TSQEALCALA VASFLLLMLV
1410 1420 1430 1440 1450
LGTRKMQLVA EWSGCVEWHP ELMNEGGEVS LRVRQDSMGN FHLTELEKEE
1460 1470 1480 1490 1500
RVMAFWLLAG LAASAFHWSG ILGVMGLWTL SEMLRTARRS GLVFSGQGGR
1510 1520 1530 1540 1550
ERGDRPFEVK DGVYRIFSPG LLWGQRQVGV GYGSKGVLHT MWHVTRGAAL
1560 1570 1580 1590 1600
SIDDAVAGPY WADVKEDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH
1610 1620 1630 1640 1650
QCQPGELLLD TGRRIGAVPI DLAKGTSGSP ILNSQGVVVG LYGNGLKTNE
1660 1670 1680 1690 1700
TYVSSIAQGE AEKSRPNLPP AVTGTGWTAK GQITVLDMHP GSGKTHRVLP
1710 1720 1730 1740 1750
ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP AVGDQQVGGS
1760 1770 1780 1790 1800
IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
1810 1820 1830 1840 1850
ENKCALVLMT ATPPGKSEPF PESNGAISSE EKQIPDGEWR DGFDWITEYE
1860 1870 1880 1890 1900
GRTAWFVPSS AKGGIIARTL IQKGKSVICL NSKTFEKDYS RVRDEKPDFV
1910 1920 1930 1940 1950
VTTDISEMGA NLDVSRVIDG RTNIKPEEVD GRVELTGTRR VTTASAAQRR
1960 1970 1980 1990 2000
GRVGRQEGRT DEYIYSGQCD DDDSGLVQWK EAQILLDNIT TLRGPVATFY
2010 2020 2030 2040 2050
GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH VAANVSSVTS
2060 2070 2080 2090 2100
RNWTWEGPEE NTVDEANGDL VTFRSPNGAE RTLRPVWRDA RMFREGRDIR
2110 2120 2130 2140 2150
EFVAYASGRR SFGDVLSGMS GVPELLRHRC VSAMDVFYTL MHEEPGSRAM
2160 2170 2180 2190 2200
KMAERDAPEA FLTVVEMMVL GLATLGVVWC FVVRTSISRM MLGTLVLLAS
2210 2220 2230 2240 2250
LALLWAGGVS YGNMAGVALI FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL
2260 2270 2280 2290 2300
CSLAGLVAAN EMGFLEKTKA DLSTVLWSEH EELRSWEEWT NIDIQPARSW
2310 2320 2330 2340 2350
GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ATGAQAMRDL GGGAPFFGVA
2360 2370 2380 2390 2400
GHVMALGVVS LVGATPTSLV VGVGLAAFHL AIVVSGLEAE LTQRAHKVFF
2410 2420 2430 2440 2450
SAMVRNPMVD GDVINPFGEG EAKPALYERK MSLVLAIVLC LMSVVMNRTV
2460 2470 2480 2490 2500
PSTPRLLLWD WRQRDNCSNQ RRTPFGRCQA CGLSGVVRGS LWGFCPLGHR
2510 2520 2530 2540 2550
LWLRASGSRR GGSEGDTLGD LWKRKLNGCT KEEFFAYRRT GILETERDKA
2560 2570 2580 2590 2600
RELLKRGETN MGLAVSRGTA KLAWLEERGY ATLKGEVVDL GCGRGGWSYY
2610 2620 2630 2640 2650
AASRPAVMSV KACAIAGKGH ETPKMVTSLG WNLIKFRAGM DVFSMQPHRA
2660 2670 2680 2690 2700
DTIMCDIGES NPDAVVEGER TRKVILLMEQ WKNRNPTATC VFKALAPYRP
2710 2720 2730 2740 2750
EVTEALHRFQ LQWGGGLVRT PFSRNSTHEM YYSTAITGNI VNSVNIQSRK
2760 2770 2780 2790 2800
LLARFGDQRG PTRVPELDLG VGTRCVVLAE DKVKEKDVQE RISALREQYG
2810 2820 2830 2840 2850
ETWHMDREHP YRTWQYWAAT ACANRVGGAL INGVVKLLSW PWNAREDVVR
2860 2870 2880 2890 2900
MAMTDTTAFG QQRVFKEKVD TKAQEPQPGT KVIMRAVNDW ILERLARKSK
2910 2920 2930 2940 2950
PRMCSREEFI AKVKSNAALG AWSDEQNRWS SAKEAVEDPA FWQLVDEERE
2960 2970 2980 2990 3000
RHLAGRCAHC VYNMMGKREK KLGEFGVAKG SRAIWYMWLG SRFLEFEALG
3010 3020 3030 3040 3050
FLNEDHWASR GSSGSGVEGI SLNYLGWHLK GLSTLEGGLF YADDTAGWDT
3060 3070 3080 3090 3100
KVTNADLEDE EQLLRYMEGE HKQLAATIMQ KAYHAKVVKV ARPSRDGGCI
3110 3120 3130 3140 3150
MDVITRRDQR GSGQVVTYAL NTLTNIKVQL IRMMEGEGVI EASDAHNPRL
3160 3170 3180 3190 3200
LRVERWLRDH GEERLGRMLV SGDDCVVRPV DDRFSGALYF LNDMAKTRKD
3210 3220 3230 3240 3250
IGEWDHSVGF SNWEEVPFCS HHFHELVMKD GRTLIVPCRD QDELVGRARV
3260 3270 3280 3290 3300
SPGCGRSVRE TACLSKAYGQ MWLLSYFHRR DLRTLGLAIC SAVPVDWVPA
3310 3320 3330 3340 3350
GRTTWSIHAS GAWMTTEDML DVWNRVWILD NPFMHSKEKI AEWRDVPYLP
3360 3370 3380 3390 3400
KSHDMLCSSL VGRKERAEWA KNIWGAVEKV RKMIGQEKFK DYLSCMDRHD
3410
LHWESKLESS II
Length:3,412
Mass (Da):377,981
Last modified:May 1, 1991 - v3
Checksum:i0F61CE6DCCDC5965
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti381W → S in CAA27500 (PubMed:3709796).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07755 Genomic RNA. Translation: CAA30581.1.
X03870 Genomic RNA. Translation: CAA27500.1.
X03870 Genomic RNA. Translation: CAA27501.1. Sequence problems.
X03870 Genomic RNA. Translation: CAA27502.1. Sequence problems.
X03870 Genomic RNA. Translation: CAA27503.1. Sequence problems.
X03871 Genomic RNA. Translation: CAA27505.1.
PIRiA33776. GNWVTB.

Similar proteinsi

Entry informationi

Entry nameiPOLG_TBEVS
AccessioniPrimary (citable) accession number: P07720
Secondary accession number(s): P07721
, Q88475, Q88476, Q88477, Q88478, Q88479, Q88877, Q88878, Q88879
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: May 1, 1991
Last modified: November 22, 2017
This is version 165 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references