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Protein

Genome polyprotein

Gene
N/A
Organism
Tick-borne encephalitis virus European subtype (strain Neudoerfl) (NEUV) (Neudoerfl virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA.By similarity
prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated.By similarity
Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes.By similarity
Non-structural protein 1 is involved in virus replication and regulation of the innate immune response.By similarity
Non-structural protein 2A may be involved viral RNA replication and capsid assembly.Curated
Non-structural protein 2B is a required cofactor for the serine protease function of NS3.PROSITE-ProRule annotation
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 (By similarity).PROSITE-ProRule annotation
Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase.By similarity
Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.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 SCRIB and prevents activation of downstream JAK-STAT signaling pathway (By similarity).PROSITE-ProRule annotation

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'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1543 – 15431Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1567 – 15671Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1627 – 16271Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Binding sitei2524 – 25241mRNA capPROSITE-ProRule annotation
Binding sitei2527 – 25271mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2528 – 25281mRNA capPROSITE-ProRule annotation
Binding sitei2530 – 25301mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2535 – 25351mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2539 – 25391mRNA capPROSITE-ProRule annotation
Binding sitei2567 – 25671S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2572 – 25721Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2597 – 25971S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2598 – 25981S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2615 – 26151S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2616 – 26161S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2642 – 26421S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2643 – 26431S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2657 – 26571Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2658 – 26581S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2661 – 26611mRNA capPROSITE-ProRule annotation
Sitei2694 – 26941Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2725 – 27251mRNA capPROSITE-ProRule annotation
Binding sitei2727 – 27271mRNA capPROSITE-ProRule annotation
Sitei2730 – 27301Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2732 – 27321S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1688 – 16958ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase

Keywords - Biological processi

Activation 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, 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

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

Protein family/group databases

MEROPSiS07.001.
TCDBi1.G.3.1.1. the viral pore-forming membrane fusion protein-3 (vmfp3) family.

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
Alternative name(s):
Non-structural protein 5
OrganismiTick-borne encephalitis virus European subtype (strain Neudoerfl) (NEUV) (Neudoerfl virus)
Taxonomic identifieri11088 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirustick-borne encephalitis virus group
Virus hostiIxodes persulcatus (Taiga tick) [TaxID: 34615]
Ixodes ricinus (Common tick) [TaxID: 34613]
Proteomesi
  • UP000007402 Componenti: Genome

Subcellular locationi

Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
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 NS3 protease.PROSITE-ProRule annotation
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Host nucleus By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9898CytoplasmicSequence analysisAdd
BLAST
Transmembranei99 – 11921HelicalSequence analysisAdd
BLAST
Topological domaini120 – 242123ExtracellularSequence analysisAdd
BLAST
Transmembranei243 – 26018HelicalSequence analysisAdd
BLAST
Topological domaini261 – 2611CytoplasmicSequence analysis
Transmembranei262 – 28019HelicalSequence analysisAdd
BLAST
Topological domaini281 – 727447ExtracellularSequence analysisAdd
BLAST
Intramembranei728 – 74821HelicalSequence analysisAdd
BLAST
Topological domaini749 – 75911ExtracellularSequence analysisAdd
BLAST
Intramembranei760 – 78021HelicalSequence analysisAdd
BLAST
Topological domaini781 – 1132352ExtracellularSequence analysisAdd
BLAST
Transmembranei1133 – 115321HelicalSequence analysisAdd
BLAST
Topological domaini1154 – 11585CytoplasmicSequence analysis
Transmembranei1159 – 117921HelicalSequence analysisAdd
BLAST
Topological domaini1180 – 11878LumenalSequence analysis
Transmembranei1188 – 120821HelicalSequence analysisAdd
BLAST
Topological domaini1209 – 129385CytoplasmicSequence analysisAdd
BLAST
Transmembranei1294 – 131421HelicalSequence analysisAdd
BLAST
Topological domaini1315 – 132713LumenalSequence analysisAdd
BLAST
Transmembranei1328 – 134821HelicalSequence analysisAdd
BLAST
Topological domaini1349 – 135911CytoplasmicSequence analysisAdd
BLAST
Transmembranei1360 – 137819HelicalSequence analysisAdd
BLAST
Topological domaini1379 – 13824LumenalSequence analysis
Transmembranei1383 – 140321HelicalSequence analysisAdd
BLAST
Topological domaini1404 – 145451CytoplasmicSequence analysisAdd
BLAST
Intramembranei1455 – 147521HelicalSequence analysisAdd
BLAST
Topological domaini1476 – 2160685CytoplasmicSequence analysisAdd
BLAST
Transmembranei2161 – 218121HelicalSequence analysisAdd
BLAST
Topological domaini2182 – 21898LumenalSequence analysis
Intramembranei2190 – 221021HelicalSequence analysisAdd
BLAST
Topological domaini2211 – 22111LumenalSequence analysis
Transmembranei2212 – 223221HelicalSequence analysisAdd
BLAST
Topological domaini2233 – 224412CytoplasmicSequence analysisAdd
BLAST
Transmembranei2245 – 226521Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2266 – 229934LumenalSequence analysisAdd
BLAST
Intramembranei2300 – 232021HelicalSequence analysisAdd
BLAST
Topological domaini2321 – 234323LumenalSequence analysisAdd
BLAST
Intramembranei2344 – 236421HelicalSequence analysisAdd
BLAST
Topological domaini2365 – 23684LumenalSequence analysis
Transmembranei2369 – 238921HelicalSequence analysisAdd
BLAST
Topological domaini2390 – 243243CytoplasmicSequence analysisAdd
BLAST
Transmembranei2433 – 245321HelicalSequence analysisAdd
BLAST
Topological domaini2454 – 247724LumenalSequence analysisAdd
BLAST
Transmembranei2478 – 249821HelicalSequence analysisAdd
BLAST
Topological domaini2499 – 3414916CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 34143414Genome polyproteinPRO_0000405175Add
BLAST
Chaini1 – 9696Capsid protein CBy similarityPRO_0000037815Add
BLAST
Propeptidei97 – 11721ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000405176Add
BLAST
Chaini118 – 280163prMBy similarityPRO_0000405177Add
BLAST
Chaini118 – 20588Peptide prBy similarityPRO_0000037816Add
BLAST
Chaini206 – 28075Small envelope protein MBy similarityPRO_0000037817Add
BLAST
Chaini281 – 776496Envelope protein EBy similarityPRO_0000037818Add
BLAST
Chaini777 – 1128352Non-structural protein 1By similarityPRO_0000037819Add
BLAST
Chaini1129 – 1358230Non-structural protein 2ABy similarityPRO_0000037820Add
BLAST
Chaini1359 – 1489131Serine protease subunit NS2BBy similarityPRO_0000037821Add
BLAST
Chaini1490 – 2110621Serine protease NS3By similarityPRO_0000037822Add
BLAST
Chaini2111 – 2236126Non-structural protein 4ABy similarityPRO_0000037823Add
BLAST
Peptidei2237 – 225923Peptide 2kBy similarityPRO_0000405178Add
BLAST
Chaini2260 – 2511252Non-structural protein 4BBy similarityPRO_0000037824Add
BLAST
Chaini2512 – 3414903RNA-directed RNA polymerase NS5By similarityPRO_0000037825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi283 ↔ 310
Disulfide bondi340 ↔ 396
Disulfide bondi354 ↔ 385
Disulfide bondi372 ↔ 401
Glycosylationi434 – 4341N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi466 ↔ 570
Disulfide bondi587 ↔ 618
Glycosylationi861 – 8611N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi983 – 9831N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi999 – 9991N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral protease NS3 and host cell enzymes yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature soluble protein C is released after cleavage by NS3 protease at a site upstream of this hydrophobic domain. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei96 – 972Cleavage; by viral protease NS3Sequence analysis
Sitei117 – 1182Cleavage; by host signal peptidaseBy similarity
Sitei205 – 2062Cleavage; by host furinBy similarity
Sitei280 – 2812Cleavage; by host signal peptidaseSequence analysis
Sitei776 – 7772Cleavage; by host signal peptidaseSequence analysis
Sitei1128 – 11292Cleavage; by hostSequence analysis
Sitei1358 – 13592Cleavage; by viral protease NS3Sequence analysis
Sitei1489 – 14902Cleavage; by autolysisSequence analysis
Sitei2110 – 21112Cleavage; by autolysisSequence analysis
Sitei2236 – 22372Cleavage; by viral protease NS3Sequence analysis
Sitei2259 – 22602Cleavage; by host signal peptidaseSequence analysis
Sitei2511 – 25122Cleavage; by viral protease NS3Sequence analysis

Keywords - PTMi

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

Interactioni

Subunit structurei

Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity. NS5 interacts with human SCRIB (via PDZ domain); this interaction inhibits STAT1 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.By similarity

Structurei

Secondary structure

1
3414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi282 – 2854Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi300 – 3067Combined sources
Beta strandi311 – 3155Combined sources
Beta strandi318 – 33215Combined sources
Beta strandi334 – 35219Combined sources
Helixi363 – 3664Combined sources
Beta strandi370 – 38011Combined sources
Helixi381 – 3833Combined sources
Beta strandi389 – 40113Combined sources
Beta strandi406 – 4116Combined sources
Turni414 – 4163Combined sources
Beta strandi418 – 4258Combined sources
Beta strandi441 – 4466Combined sources
Beta strandi451 – 4555Combined sources
Helixi457 – 4593Combined sources
Beta strandi460 – 4678Combined sources
Helixi468 – 4703Combined sources
Beta strandi477 – 4826Combined sources
Beta strandi491 – 4966Combined sources
Helixi497 – 5015Combined sources
Helixi518 – 5214Combined sources
Beta strandi522 – 5243Combined sources
Beta strandi534 – 5363Combined sources
Helixi541 – 5477Combined sources
Turni548 – 5503Combined sources
Beta strandi553 – 5575Combined sources
Beta strandi560 – 5623Combined sources
Beta strandi567 – 5737Combined sources
Beta strandi591 – 60010Combined sources
Beta strandi602 – 6043Combined sources
Beta strandi606 – 6127Combined sources
Beta strandi616 – 6194Combined sources
Beta strandi622 – 6265Combined sources
Beta strandi636 – 6416Combined sources
Beta strandi643 – 6453Combined sources
Beta strandi651 – 6555Combined sources
Beta strandi658 – 6658Combined sources
Beta strandi668 – 6747Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N6Gelectron microscopy16.00A/B/C281-675[»]
1NA4electron microscopy-A/B/C281-675[»]
1SVBX-ray1.90A281-675[»]
1URZX-ray2.70A/B/C/D/E/F281-681[»]
ProteinModelPortaliP14336.
SMRiP14336. Positions 281-675, 2512-2775, 2789-3402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14336.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1490 – 1669180Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1675 – 1831157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1841 – 2000160Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2512 – 2776265mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3040 – 3189150RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 6845Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni378 – 39114Involved in fusionAdd
BLAST
Regioni1410 – 144940Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1779 – 17824DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1970 – 19734Poly-Asp
Compositional biasi2201 – 22044Poly-Leu

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
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 mRNA cap 0-1 NS5-type MT domain.PROSITE-ProRule annotation
Contains 1 peptidase S7 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 1 hit.
3.30.387.10. 1 hit.
3.30.67.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. 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.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013756. GlyE_cen_dom_subdom2.
IPR013754. GlyE_dim.
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.
[Graphical view]
PfamiPF01003. 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.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
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.
PROSITEiPS51527. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14336-1 [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 LGMTLAATVR KERDGSTVIR AEGKDAATQV RVENGTCVIL
160 170 180 190 200
ATDMGSWCDD SLSYECVTID QGEEPVDVDC FCRNVDGVYL EYGRCGKQEG
210 220 230 240 250
SRTRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW VWKNKLLALA
260 270 280 290 300
MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
310 320 330 340 350
VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAKTREYC LHAKLSDTKV
360 370 380 390 400
AARCPTMGPA TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA
410 420 430 440 450
CEAKKKATGH VYDANKIVYT VKVEPHTGDY VAANETHSGR KTASFTISSE
460 470 480 490 500
KTILTMGEYG DVSLLCRVAS GVDLAQTVIL ELDKTVEHLP TAWQVHRDWF
510 520 530 540 550
NDLALPWKHE GAQNWNNAER 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 NIIYVGELSH QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA
710 720 730 740 750
WDFGSAGGFL SSIGKAVHTV LGGAFNSIFG GVGFLPKLLL GVALAWLGLN
760 770 780 790 800
MRNPTMSMSF LLAGGLVLAM TLGVGADVGC AVDTERMELR CGEGLVVWRE
810 820 830 840 850
VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE MAMWRSSVTE
860 870 880 890 900
LNLALAEGEA NLTVVVDKFD 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 VKGPWKYTPI
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 TTVVWGGIVV LALLVTGMVR IESLVRYVVA VGITFHLELG
1210 1220 1230 1240 1250
PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPG
1260 1270 1280 1290 1300
ASLEEFWKWG DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG
1310 1320 1330 1340 1350
LVCFLSVASA CSVWRLLKGH REQKGLTWVV PLAGLLGGEG SGIRLLAFWE
1360 1370 1380 1390 1400
LSAHRGRRSF SEPLTVVGVM LTLASGMMRH TSQEALCALA VASFLLLMLV
1410 1420 1430 1440 1450
LGTRKMQLVA EWSGCVEWYP ELVNEGGEVS LRVRQDAMGN FHLTELEKEE
1460 1470 1480 1490 1500
RMMAFWLIAG LAASAIHWSG ILGVMGLWTL TEMLRSSRRS DLVFSGQGGR
1510 1520 1530 1540 1550
ERGDRPFEVK DGVYRIFSPG LFWGQNQVGV GYGSKGVLHT MWHVTRGAAL
1560 1570 1580 1590 1600
SIDDAVAGPY WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH
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 ERQIPDGEWR 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 NAVDEASGDL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK
2110 2120 2130 2140 2150
EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEEPGSRAM
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 DLSTALWSER 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 EAKPALYERK MSLVLATVLC 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 NVGLAVSRGT AKLAWLEERG YATLKGEVVD LGCGRGGWSY
2610 2620 2630 2640 2650
YAASRPAVMS VRAYTIGGKG 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 GPTKVPELDL GVGTRCVVLA EDKVKEQDVQ ERIRALREQY
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 PAFWRLVDEE
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 GFSSWEEVPF CSHHFHELVM KDGRTLVVPC RDQDELVGRA
3260 3270 3280 3290 3300
RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPADWV
3310 3320 3330 3340 3350
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKE RVMEWRDVPY
3360 3370 3380 3390 3400
LPKAQDMLCS SLVGRRERAE WAKNIWGAVE KVRKMIGPEK FKDYLSCMDR
3410
HDLHWELRLE SSII
Length:3,414
Mass (Da):378,322
Last modified:May 30, 2000 - v4
Checksum:i35DBCE014B310B79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27495 Genomic RNA. Translation: AAA86870.1.
PIRiA31052. GNWVNE.
RefSeqiNP_043135.1. NC_001672.1.

Genome annotation databases

GeneIDi1489719.
KEGGivg:1489719.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27495 Genomic RNA. Translation: AAA86870.1.
PIRiA31052. GNWVNE.
RefSeqiNP_043135.1. NC_001672.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N6Gelectron microscopy16.00A/B/C281-675[»]
1NA4electron microscopy-A/B/C281-675[»]
1SVBX-ray1.90A281-675[»]
1URZX-ray2.70A/B/C/D/E/F281-681[»]
ProteinModelPortaliP14336.
SMRiP14336. Positions 281-675, 2512-2775, 2789-3402.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.
TCDBi1.G.3.1.1. the viral pore-forming membrane fusion protein-3 (vmfp3) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489719.
KEGGivg:1489719.

Miscellaneous databases

EvolutionaryTraceiP14336.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 1 hit.
3.30.387.10. 1 hit.
3.30.67.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. 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.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013756. GlyE_cen_dom_subdom2.
IPR013754. GlyE_dim.
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.
[Graphical view]
PfamiPF01003. 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.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
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.
PROSITEiPS51527. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_TBEVW
AccessioniPrimary (citable) accession number: P14336
Secondary accession number(s): Q88493
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 30, 2000
Last modified: September 7, 2016
This is version 160 of the entry and version 4 of the sequence. [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
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.