Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Genome polyprotein

Gene
N/A
Organism
West Nile virus (WNV)
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
Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.By similarity
RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) 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 JAK1 and TYK2 phosphorylation, thereby preventing activation of 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)DescriptionActionsGraphical viewLength
Active sitei1552Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1576Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1636Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Binding sitei2538mRNA capPROSITE-ProRule annotation1
Binding sitei2541mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2542mRNA capPROSITE-ProRule annotation1
Binding sitei2544mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2549mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2553mRNA capPROSITE-ProRule annotation1
Binding sitei2581S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2586Essential for 2'-O-methyltransferase activity1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2612S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2629S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2630S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2656S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2657S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2671Essential for 2'-O-methyltransferase and N-7 methyltransferase activity1
Sitei2672S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2675mRNA capPROSITE-ProRule annotation1
Sitei2707Essential for 2'-O-methyltransferase activity1
Binding sitei2738mRNA capPROSITE-ProRule annotation1
Binding sitei2740mRNA capPROSITE-ProRule annotation1
Sitei2743Essential for 2'-O-methyltransferase activity1
Binding sitei2745S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1695 – 1702ATPPROSITE-ProRule annotation8

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, Inhibition of host JAK1 by virus, Inhibition of host TYK2 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

Enzyme and pathway databases

BRENDAi2.7.7.48. 6687.
3.4.21.91. 6687.

Protein family/group databases

MEROPSiS07.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Alternative name(s):
NS5
OrganismiWest Nile virus (WNV)
Taxonomic identifieri11082 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Virus hostiAedes [TaxID: 7158]
Amblyomma variegatum (Tropical bont tick) [TaxID: 34610]
Aves [TaxID: 8782]
Culex [TaxID: 53527]
Homo sapiens (Human) [TaxID: 9606]
Hyalomma marginatum [TaxID: 34627]
Mansonia uniformis [TaxID: 308735]
Mimomyia [TaxID: 308737]
Rhipicephalus [TaxID: 34630]
Proteomesi
  • UP000008600 Componenti: Genome

Subcellular locationi

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 1 Publication

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 105CytoplasmicSequence analysisAdd BLAST104
Transmembranei106 – 126HelicalSequence analysisAdd BLAST21
Topological domaini127 – 248ExtracellularSequence analysisAdd BLAST122
Transmembranei249 – 269HelicalSequence analysisAdd BLAST21
Topological domaini270 – 275CytoplasmicSequence analysis6
Transmembranei276 – 292HelicalSequence analysisAdd BLAST17
Topological domaini293 – 739ExtracellularSequence analysisAdd BLAST447
Intramembranei740 – 760HelicalSequence analysisAdd BLAST21
Topological domaini761 – 766ExtracellularSequence analysis6
Intramembranei767 – 787HelicalSequence analysisAdd BLAST21
Topological domaini788 – 1138ExtracellularSequence analysisAdd BLAST351
Transmembranei1139 – 1159HelicalSequence analysisAdd BLAST21
Topological domaini1160 – 1212CytoplasmicSequence analysisAdd BLAST53
Transmembranei1213 – 1233HelicalSequence analysisAdd BLAST21
Topological domaini1234 – 1243LumenalSequence analysis10
Transmembranei1244 – 1264HelicalSequence analysisAdd BLAST21
Topological domaini1265 – 1292CytoplasmicSequence analysisAdd BLAST28
Transmembranei1293 – 1313HelicalSequence analysisAdd BLAST21
Topological domaini1314 – 1340LumenalSequence analysisAdd BLAST27
Transmembranei1341 – 1361HelicalSequence analysisAdd BLAST21
Topological domaini1362 – 1371CytoplasmicSequence analysis10
Transmembranei1372 – 1392HelicalSequence analysisAdd BLAST21
Topological domaini1393 – 1395LumenalSequence analysis3
Transmembranei1396 – 1416HelicalSequence analysisAdd BLAST21
Topological domaini1417 – 1473CytoplasmicSequence analysisAdd BLAST57
Intramembranei1474 – 1494HelicalSequence analysisAdd BLAST21
Topological domaini1495 – 2170CytoplasmicSequence analysisAdd BLAST676
Transmembranei2171 – 2191HelicalSequence analysisAdd BLAST21
Topological domaini2192 – 2196LumenalSequence analysis5
Intramembranei2197 – 2217HelicalSequence analysisAdd BLAST21
Topological domaini2218LumenalSequence analysis1
Transmembranei2219 – 2239HelicalSequence analysisAdd BLAST21
Topological domaini2240 – 2254CytoplasmicSequence analysisAdd BLAST15
Transmembranei2255 – 2275Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2276 – 2309LumenalSequence analysisAdd BLAST34
Intramembranei2310 – 2330HelicalSequence analysisAdd BLAST21
Topological domaini2331 – 2355LumenalSequence analysisAdd BLAST25
Intramembranei2356 – 2376HelicalSequence analysisAdd BLAST21
Topological domaini2377LumenalSequence analysis1
Transmembranei2378 – 2398HelicalSequence analysisAdd BLAST21
Topological domaini2399 – 2441CytoplasmicSequence analysisAdd BLAST43
Transmembranei2442 – 2462HelicalSequence analysisAdd BLAST21
Topological domaini2463 – 2467LumenalSequence analysis5
Transmembranei2468 – 2488HelicalSequence analysisAdd BLAST21
Topological domaini2489 – 3430CytoplasmicSequence analysisAdd BLAST942

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2586K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication1
Mutagenesisi2671D → A: Lethal for the virus. Complete loss of 2'-O and N-7 methyltransferase activies. 1 Publication1
Mutagenesisi2707K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication1
Mutagenesisi2743E → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5419.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostSequence analysis
ChainiPRO_00000377432 – 105Capsid protein CAdd BLAST104
PropeptideiPRO_0000037744106 – 123ER anchor for the protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000405150124 – 290prMAdd BLAST167
ChainiPRO_0000405151124 – 215Peptide prAdd BLAST92
ChainiPRO_0000037745216 – 290Small envelope protein MAdd BLAST75
ChainiPRO_0000037746291 – 787Envelope protein EAdd BLAST497
ChainiPRO_0000037747788 – 1139Non-structural protein 1Add BLAST352
ChainiPRO_00000377481140 – 1370Non-structural protein 2AAdd BLAST231
ChainiPRO_00000377491371 – 1501Serine protease subunit NS2BAdd BLAST131
ChainiPRO_00000377501502 – 2120Serine protease NS3Add BLAST619
ChainiPRO_00000377512121 – 2246Non-structural protein 4AAdd BLAST126
PeptideiPRO_00004051522247 – 2269Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000377522270 – 2525Non-structural protein 4BAdd BLAST256
ChainiPRO_00000377532526 – 3430RNA-directed RNA polymerase NS5Add BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi293 ↔ 3201 Publication
Disulfide bondi350 ↔ 4061 Publication
Disulfide bondi364 ↔ 3951 Publication
Disulfide bondi382 ↔ 4111 Publication
Disulfide bondi476 ↔ 5741 Publication
Disulfide bondi591 ↔ 6221 Publication
Glycosylationi917N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi962N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi994N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2336N-linked (GlcNAc...); by hostSequence analysis1

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)DescriptionActionsGraphical viewLength
Sitei105 – 106Cleavage; by viral protease NS32
Sitei123 – 124Cleavage; by host signal peptidaseBy similarity2
Sitei215 – 216Cleavage; by host furinSequence analysis2
Sitei290 – 291Cleavage; by host signal peptidaseSequence analysis2
Sitei787 – 788Cleavage; by host signal peptidaseSequence analysis2
Sitei1139 – 1140Cleavage; by hostSequence analysis2
Sitei1370 – 1371Cleavage; by viral protease NS32
Sitei1501 – 1502Cleavage; by autolysis2
Sitei2120 – 2121Cleavage; by autolysis2
Sitei2246 – 2247Cleavage; by viral protease NS32
Sitei2269 – 2270Cleavage; by host signal peptidaseSequence analysis2
Sitei2525 – 2526Cleavage; by viral protease NS32

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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CTLMA15Q17NZ65EBI-2912469,EBI-2912457From a different organism.
ITGB3P051064EBI-981051,EBI-702847From a different organism.

Protein-protein interaction databases

IntActiP06935. 4 interactors.

Chemistry databases

BindingDBiP06935.

Structurei

Secondary structure

13430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi595 – 603Combined sources9
Beta strandi605 – 607Combined sources3
Beta strandi609 – 615Combined sources7
Beta strandi621 – 623Combined sources3
Beta strandi626 – 631Combined sources6
Beta strandi634 – 637Combined sources4
Beta strandi639 – 643Combined sources5
Beta strandi657 – 662Combined sources6
Beta strandi665 – 673Combined sources9
Beta strandi679 – 685Combined sources7
Beta strandi1423 – 1428Combined sources6
Helixi1434 – 1439Combined sources6
Beta strandi1440 – 1443Combined sources4
Beta strandi1444 – 1449Combined sources6
Beta strandi1451 – 1453Combined sources3
Beta strandi1455 – 1457Combined sources3
Beta strandi1522 – 1527Combined sources6
Beta strandi1536 – 1543Combined sources8
Beta strandi1546 – 1550Combined sources5
Helixi1551 – 1554Combined sources4
Beta strandi1559 – 1561Combined sources3
Beta strandi1564 – 1566Combined sources3
Beta strandi1568 – 1572Combined sources5
Turni1573 – 1576Combined sources4
Beta strandi1577 – 1583Combined sources7
Beta strandi1592 – 1594Combined sources3
Beta strandi1596 – 1600Combined sources5
Beta strandi1608 – 1612Combined sources5
Beta strandi1615 – 1619Combined sources5
Beta strandi1622 – 1627Combined sources6
Helixi1633 – 1635Combined sources3
Beta strandi1639 – 1641Combined sources3
Beta strandi1647 – 1651Combined sources5
Beta strandi1654 – 1656Combined sources3
Beta strandi1662 – 1665Combined sources4
Beta strandi1672 – 1674Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FP7X-ray1.68A1420-1466[»]
B1517-1688[»]
2G05model-D1675-2120[»]
2G2Gmodel-D1675-2120[»]
2GGVX-ray1.80A1419-1525[»]
B1503-1679[»]
2IJOX-ray2.30A1419-1482[»]
B1502-1685[»]
2P5PX-ray2.80A/B/C585-701[»]
2YOLX-ray3.20A1420-1465[»]
A1502-1671[»]
3E90X-ray2.45A/C1420-1463[»]
B/D1502-1685[»]
3I50X-ray3.00E291-688[»]
DisProtiDP00673.
ProteinModelPortaliP06935.
SMRiP06935.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06935.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1502 – 1679Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1682 – 1838Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1849 – 2014Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2526 – 2791mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3055 – 3207RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 74Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST42
Regioni388 – 401Involved in fusionAdd BLAST14
Regioni1424 – 1463Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1786 – 1789DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi281 – 284Poly-Leu4
Compositional biasi2675 – 2678Poly-Ser4

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. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_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.
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.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[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.

P06935-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL
60 70 80 90 100
LAFFRFTAIA PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST
110 120 130 140 150
KQKKRGGTAG FTILLGLIAC AGAVTLSNFQ GKVMMTVNAT DVTDVITIPT
160 170 180 190 200
AAGKNLCIVR AMDVGYLCED TITYECPVLA AGNDPEDIDC WCTKSSVYVR
210 220 230 240 250
YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWLDSTKA TRYLVKTESW
260 270 280 290 300
ILRNPGYALV AAVIGWMLGS NTMQRVVFAI LLLLVAPAYS FNCLGMSNRD
310 320 330 340 350
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLADVRSYC
360 370 380 390 400
YLASVSDLST RAACPTMGEA HNEKRADPAF VCKQGVVDRG WGNGCGLFGK
410 420 430 440 450
GSIDTCAKFA CTTKATGWII QKENIKYEVA IFVHGPTTVE SHGKIGATQA
460 470 480 490 500
GRFSITPSAP SYTLKLGEYG EVTVDCEPRS GIDTSAYYVM SVGEKSFLVH
510 520 530 540 550
REWFMDLNLP WSSAGSTTWR NRETLMEFEE PHATKQSVVA LGSQEGALHQ
560 570 580 590 600
ALAGAIPVEF SSNTVKLTSG HLKCRVKMEK LQLKGTTYGV CSKAFKFART
610 620 630 640 650
PADTGHGTVV LELQYTGTDG PCKVPISSVA SLNDLTPVGR LVTVNPFVSV
660 670 680 690 700
ATANSKVLIE LEPPFGDSYI VVGRGEQQIN HHWHKSGSSI GKAFTTTLRG
710 720 730 740 750
AQRLAALGDT AWDFGSVGGV FTSVGKAIHQ VFGGAFRSLF GGMSWITQGL
760 770 780 790 800
LGALLLWMGI NARDRSIAMT FLAVGGVLLF LSVNVHADTG CAIDIGRQEL
810 820 830 840 850
RCGSGVFIHN DVEAWMDRYK FYPETPQGLA KIIQKAHAEG VCGLRSVSRL
860 870 880 890 900
EHQMWEAIKD ELNTLLKENG VDLSVVVEKQ NGMYKAAPKR LAATTEKLEM
910 920 930 940 950
GWKAWGKSII FAPELANNTF VIDGPETEEC PTANRAWNSM EVEDFGFGLT
960 970 980 990 1000
STRMFLRIRE TNTTECDSKI IGTAVKNNMA VHSDLSYWIE SGLNDTWKLE
1010 1020 1030 1040 1050
RAVLGEVKSC TWPETHTLWG DGVLESDLII PITLAGPRSN HNRRPGYKTQ
1060 1070 1080 1090 1100
NQGPWDEGRV EIDFDYCPGT TVTISDSCEH RGPAARTTTE SGKLITDWCC
1110 1120 1130 1140 1150
RSCTLPPLRF QTENGCWYGM EIRPTRHDEK TLVQSRVNAY NADMIDPFQL
1160 1170 1180 1190 1200
GLMVVFLATQ EVLRKRWTAK ISIPAIMLAL LVLVFGGITY TDVLRYVILV
1210 1220 1230 1240 1250
GAAFAEANSG GDVVHLALMA TFKIQPVFLV ASFLKARWTN QESILLMLAA
1260 1270 1280 1290 1300
AFFQMAYYDA KNVLSWEVPD VLNSLSVAWM ILRAISFTNT SNVVVPLLAL
1310 1320 1330 1340 1350
LTPGLKCLNL DVYRILLLMV GVGSLIKEKR SSAAKKKGAC LICLALASTG
1360 1370 1380 1390 1400
VFNPMILAAG LMACDPNRKR GWPATEVMTA VGLMFAIVGG LAELDIDSMA
1410 1420 1430 1440 1450
IPMTIAGLMF AAFVISGKST DMWIERTADI TWESDAEITG SSERVDVRLD
1460 1470 1480 1490 1500
DDGNFQLMND PGAPWKIWML RMACLAISAY TPWAILPSVI GFWITLQYTK
1510 1520 1530 1540 1550
RGGVLWDTPS PKEYKKGDTT TGVYRIMTRG LLGSYQAGAG VMVEGVFHTL
1560 1570 1580 1590 1600
WHTTKGAALM SGEGRLDPYW GSVKEDRLCY GGPWKLQHKW NGHDEVQMIV
1610 1620 1630 1640 1650
VEPGKNVKNV QTKPGVFKTP EGEIGAVTLD YPTGTSGSPI VDKNGDVIGL
1660 1670 1680 1690 1700
YGNGVIMPNG SYISAIVQGE RMEEPAPAGF EPEMLRKKQI TVLDLHPGAG
1710 1720 1730 1740 1750
KTRKILPQII KEAINKRLRT AVLAPTRVVA AEMSEALRGL PIRYQTSAVH
1760 1770 1780 1790 1800
REHSGNEIVD VMCHATLTHR LMSPHRVPNY NLFIMDEAHF TDPASIAARG
1810 1820 1830 1840 1850
YIATKVELGE AAAIFMTATP PGTSDPFPES NAPISDMQTE IPDRAWNTGY
1860 1870 1880 1890 1900
EWITEYVGKT VWFVPSVKMG NEIALCLQRA GKKVIQLNRK SYETEYPKCK
1910 1920 1930 1940 1950
NDDWDFVITT DISEMGANFK ASRVIDSRKS VKPTIIEEGD GRVILGEPSA
1960 1970 1980 1990 2000
ITAASAAQRR GRIGRNPSQV GDEYCYGGHT NEDDSNFAHW TEARIMLDNI
2010 2020 2030 2040 2050
NMPNGLVAQL YQPEREKVYT MDGEYRLRGE ERKNFLEFLR TADLPVWLAY
2060 2070 2080 2090 2100
KVAAAGISYH DRKWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWADA
2110 2120 2130 2140 2150
RVYSDHQALK SFKDFASGKR SQIGLVEVLG RMPEHFMVKT WEALDTMYVV
2160 2170 2180 2190 2200
ATAEKGGRAH RMALEELPDA LQTIVLIALL SVMSLGVFFL LMQRKGIGKI
2210 2220 2230 2240 2250
GLGGVILGAA TFFCWMAEVP GTKIAGMLLL SLLLMIVLIP EPEKQRSQTD
2260 2270 2280 2290 2300
NQLAVFLICV LTLVGAVAAN EMGWLDKTKN DIGSLLGHRP EARETTLGVE
2310 2320 2330 2340 2350
SFLLDLRPAT AWSLYAVTTA VLTPLLKHLI TSDYINTSLT SINVQASALF
2360 2370 2380 2390 2400
TLARGFPFVD VGVSALLLAV GCWGQVTLTV TVTAAALLFC HYAYMVPGWQ
2410 2420 2430 2440 2450
AEAMRSAQRR TAAGIMKNVV VDGIVATDVP ELERTTPVMQ KKVGQIILIL
2460 2470 2480 2490 2500
VSMAAVVVNP SVRTVREAGI LTTAAAVTLW ENGASSVWNA TTAIGLCHIM
2510 2520 2530 2540 2550
RGGWLSCLSI MWTLIKNMEK PGLKRGGAKG RTLGEVWKER LNHMTKEEFT
2560 2570 2580 2590 2600
RYRKEAITEV DRSAAKHARR EGNITGGHPV SRGTAKLRWL VERRFLEPVG
2610 2620 2630 2640 2650
KVVDLGCGRG GWCYYMATQK RVQEVKGYTK GGPGHEEPQL VQSYGWNIVT
2660 2670 2680 2690 2700
MKSGVDVFYR PSEASDTLLC DIGESSSSAE VEEHRTVRVL EMVEDWLHRG
2710 2720 2730 2740 2750
PKEFCIKVLC PYMPKVIEKM ETLQRRYGGG LIRNPLSRNS THEMYWVSHA
2760 2770 2780 2790 2800
SGNIVHSVNM TSQVLLGRME KKTWKGPQFE EDVNLGSGTR AVGKPLLNSD
2810 2820 2830 2840 2850
TSKIKNRIER LKKEYSSTWH QDANHPYRTW NYHGSYEVKP TGSASSLVNG
2860 2870 2880 2890 2900
VVRLLSKPWD TITNVTTMAM TDTTPFGQQR VFKEKVDTKA PEPPEGVKYV
2910 2920 2930 2940 2950
LNETTNWLWA FLARDKKPRM CSREEFIGKV NSNAALGAMF EEQNQWKNAR
2960 2970 2980 2990 3000
EAVEDPKFWE MVDEEREAHL RGECNTCIYN MMGKREKKPG EFGKAKGSRA
3010 3020 3030 3040 3050
IWFMWLGARF LEFEALGFLN EDHWLGRKNS GGGVEGLGLQ KLGYILKEVG
3060 3070 3080 3090 3100
TKPGGKVYAD DTAGWDTRIT KADLENEAKV LELLDGEHRR LARSIIELTY
3110 3120 3130 3140 3150
RHKVVKVMRP AADGKTVMDV ISREDQRGSG QVVTYALNTF TNLAVQLVRM
3160 3170 3180 3190 3200
MEGEGVIGPD DVEKLGKGKG PKVRTWLFEN GEERLSRMAV SGDDCVVKPL
3210 3220 3230 3240 3250
DDRFATSLHF LNAMSKVRKD IQEWKPSTGW YDWQQVPFCS NHFTELIMKD
3260 3270 3280 3290 3300
GRTLVVPCRG QDELIGRARI SPGAGWNVRD TACLAKSYAQ MWLLLYFHRR
3310 3320 3330 3340 3350
DLRLMANAIC SAVPANWVPT GRTTWSIHAK GEWMTTEDML AVWNRVWIEE
3360 3370 3380 3390 3400
NEWMEDKTPV ERWSDVPYSG KREDIWCGSL IGTRTRATWA ENIHVAINQV
3410 3420 3430
RSVIGEEKYV DYMSSLRRYE DTIVVEDTVL
Length:3,430
Mass (Da):380,110
Last modified:October 24, 2003 - v2
Checksum:i42D71B7CB12DC45B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12294 Genomic RNA. Translation: AAA48498.2.
PIRiA25256. GNWVWV.
RefSeqiNP_041724.2. NC_001563.2.

Genome annotation databases

GeneIDi912267.
KEGGivg:912267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12294 Genomic RNA. Translation: AAA48498.2.
PIRiA25256. GNWVWV.
RefSeqiNP_041724.2. NC_001563.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FP7X-ray1.68A1420-1466[»]
B1517-1688[»]
2G05model-D1675-2120[»]
2G2Gmodel-D1675-2120[»]
2GGVX-ray1.80A1419-1525[»]
B1503-1679[»]
2IJOX-ray2.30A1419-1482[»]
B1502-1685[»]
2P5PX-ray2.80A/B/C585-701[»]
2YOLX-ray3.20A1420-1465[»]
A1502-1671[»]
3E90X-ray2.45A/C1420-1463[»]
B/D1502-1685[»]
3I50X-ray3.00E291-688[»]
DisProtiDP00673.
ProteinModelPortaliP06935.
SMRiP06935.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06935. 4 interactors.

Chemistry databases

BindingDBiP06935.
ChEMBLiCHEMBL5419.

Protein family/group databases

MEROPSiS07.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi912267.
KEGGivg:912267.

Enzyme and pathway databases

BRENDAi2.7.7.48. 6687.
3.4.21.91. 6687.

Miscellaneous databases

EvolutionaryTraceiP06935.
PROiP06935.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_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.
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.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[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_WNV
AccessioniPrimary (citable) accession number: P06935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 24, 2003
Last modified: November 2, 2016
This is version 168 of the entry and version 2 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.