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
Japanese encephalitis virus (strain SA-14)
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 TYK2 and STAT1 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1555 – 15551Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1579 – 15791Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1639 – 16391Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Binding sitei2540 – 25401mRNA capPROSITE-ProRule annotation
Binding sitei2543 – 25431mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2544 – 25441mRNA capPROSITE-ProRule annotation
Binding sitei2546 – 25461mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2551 – 25511mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2555 – 25551mRNA capPROSITE-ProRule annotation
Binding sitei2583 – 25831S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2588 – 25881Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2613 – 26131S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2614 – 26141S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2631 – 26311S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2632 – 26321S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2658 – 26581S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2659 – 26591S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2673 – 26731Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2674 – 26741S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2677 – 26771mRNA capPROSITE-ProRule annotation
Sitei2709 – 27091Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2740 – 27401mRNA capPROSITE-ProRule annotation
Binding sitei2742 – 27421mRNA capPROSITE-ProRule annotation
Sitei2745 – 27451Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2747 – 27471S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1698 – 17058ATPPROSITE-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, Inhibition of host STAT1 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

BRENDAi3.6.4.12. 2787.
3.6.4.13. 2787.

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):
Non-structural protein 5
OrganismiJapanese encephalitis virus (strain SA-14)
Taxonomic identifieri11073 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Virus hostiArdeidae (herons) [TaxID: 8899]
Bos taurus (Bovine) [TaxID: 9913]
Culex gelidus [TaxID: 308713]
Culex tritaeniorhynchus (Mosquito) [TaxID: 7178]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000008380 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 domaini2 – 109108CytoplasmicSequence analysisAdd
BLAST
Transmembranei110 – 13021HelicalSequence analysisAdd
BLAST
Topological domaini131 – 253123ExtracellularSequence analysisAdd
BLAST
Transmembranei254 – 27421HelicalSequence analysisAdd
BLAST
Topological domaini275 – 2795CytoplasmicSequence analysis
Transmembranei280 – 29415HelicalSequence analysisAdd
BLAST
Topological domaini295 – 746452ExtracellularSequence analysisAdd
BLAST
Intramembranei747 – 76721HelicalSequence analysisAdd
BLAST
Topological domaini768 – 7736ExtracellularSequence analysis
Intramembranei774 – 79421HelicalSequence analysisAdd
BLAST
Topological domaini795 – 1145351ExtracellularSequence analysisAdd
BLAST
Transmembranei1146 – 116621HelicalSequence analysisAdd
BLAST
Topological domaini1167 – 117711CytoplasmicSequence analysisAdd
BLAST
Transmembranei1178 – 119821HelicalSequence analysisAdd
BLAST
Topological domaini1199 – 121921LumenalSequence analysisAdd
BLAST
Transmembranei1220 – 124021HelicalSequence analysisAdd
BLAST
Topological domaini1241 – 125010CytoplasmicSequence analysis
Transmembranei1251 – 127121HelicalSequence analysisAdd
BLAST
Topological domaini1272 – 12721LumenalSequence analysis
Transmembranei1273 – 129321HelicalSequence analysisAdd
BLAST
Topological domaini1294 – 137481CytoplasmicSequence analysisAdd
BLAST
Transmembranei1375 – 139521HelicalSequence analysisAdd
BLAST
Topological domaini1396 – 13983LumenalSequence analysis
Transmembranei1399 – 141921HelicalSequence analysisAdd
BLAST
Topological domaini1420 – 147657CytoplasmicSequence analysisAdd
BLAST
Intramembranei1477 – 149721HelicalSequence analysisAdd
BLAST
Topological domaini1498 – 2173676CytoplasmicSequence analysisAdd
BLAST
Transmembranei2174 – 219421HelicalSequence analysisAdd
BLAST
Topological domaini2195 – 21995LumenalSequence analysis
Intramembranei2200 – 222021HelicalSequence analysisAdd
BLAST
Topological domaini2221 – 22211LumenalSequence analysis
Transmembranei2222 – 224221HelicalSequence analysisAdd
BLAST
Topological domaini2243 – 225715CytoplasmicSequence analysisAdd
BLAST
Transmembranei2258 – 227821Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2279 – 231133LumenalSequence analysisAdd
BLAST
Intramembranei2312 – 233221HelicalSequence analysisAdd
BLAST
Topological domaini2333 – 236836LumenalSequence analysisAdd
BLAST
Intramembranei2369 – 238921HelicalSequence analysisAdd
BLAST
Topological domaini2390 – 244455LumenalSequence analysisAdd
BLAST
Transmembranei2445 – 246521HelicalSequence analysisAdd
BLAST
Topological domaini2466 – 24694CytoplasmicSequence analysis
Transmembranei2470 – 249021HelicalSequence analysisAdd
BLAST
Topological domaini2491 – 24966LumenalSequence analysis
Transmembranei2497 – 251721HelicalSequence analysisAdd
BLAST
Topological domaini2518 – 3432915CytoplasmicSequence 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1703 – 17031G → A: Complete loss of both the ATPase and helicase activities. 1 Publication
Mutagenesisi1704 – 17041K → D, E, H, N, Q or R: Complete loss of both the ATPase and helicase activities. 1 Publication
Mutagenesisi1705 – 17051T → A: Complete loss of both the ATPase and helicase activities. 1 Publication
Mutagenesisi1961 – 19611Q → A: 80% loss of ATPase activity. 1 Publication
Mutagenesisi1962 – 19621R → A: 90% loss of ATPase activity. 1 Publication
Mutagenesisi1965 – 19651R → A: Complete loss of ATPase activity. 1 Publication
Mutagenesisi1968 – 19681R → A: Complete loss of ATPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by hostSequence analysis
Chaini2 – 34323431Genome polyproteinPRO_0000405188Add
BLAST
Chaini2 – 105104Capsid protein CBy similarityPRO_0000037836Add
BLAST
Propeptidei106 – 12722ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000405189Add
BLAST
Chaini128 – 294167prMBy similarityPRO_0000405190Add
BLAST
Chaini128 – 21992Peptide prBy similarityPRO_0000037837Add
BLAST
Chaini220 – 29475Small envelope protein MBy similarityPRO_0000037838Add
BLAST
Chaini295 – 794500Envelope protein EBy similarityPRO_0000037839Add
BLAST
Chaini795 – 1146352Non-structural protein 1By similarityPRO_0000037840Add
BLAST
Chaini1147 – 1373227Non-structural protein 2ABy similarityPRO_0000037841Add
BLAST
Chaini1374 – 1504131Serine protease subunit NS2BBy similarityPRO_0000037842Add
BLAST
Chaini1505 – 2123619Serine protease NS3By similarityPRO_0000037843Add
BLAST
Chaini2124 – 2249126Non-structural protein 4ABy similarityPRO_0000037844Add
BLAST
Peptidei2250 – 227223Peptide 2kBy similarityPRO_0000405191Add
BLAST
Chaini2273 – 2527255Non-structural protein 4BBy similarityPRO_0000037845Add
BLAST
Chaini2528 – 3432905RNA-directed RNA polymerase NS5By similarityPRO_0000037846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi142 – 1421N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi297 ↔ 324By similarity
Disulfide bondi354 ↔ 410By similarity
Disulfide bondi368 ↔ 399By similarity
Disulfide bondi386 ↔ 415By similarity
Glycosylationi448 – 4481N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi484 ↔ 581By similarity
Disulfide bondi598 ↔ 629By similarity
Glycosylationi924 – 9241N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi1001 – 10011N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2491 – 24911N-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
Sitei105 – 1062Cleavage; by viral protease NS3Sequence analysis
Sitei127 – 1282Cleavage; by host signal peptidaseBy similarity
Sitei219 – 2202Cleavage; by host furinBy similarity
Sitei294 – 2952Cleavage; by host signal peptidaseSequence analysis
Sitei794 – 7952Cleavage; by host signal peptidaseSequence analysis
Sitei1146 – 11472Cleavage; by hostBy similarity
Sitei1373 – 13742Cleavage; by viral protease NS3Sequence analysis
Sitei1504 – 15052Cleavage; by autolysisSequence analysis
Sitei2123 – 21242Cleavage; by autolysisSequence analysis
Sitei2249 – 22502Cleavage; by viral protease NS3Sequence analysis
Sitei2272 – 22732Cleavage; by host signal peptidaseSequence analysis
Sitei2527 – 25282Cleavage; 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.

Structurei

Secondary structure

1
3432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi301 – 3077Combined sources
Beta strandi313 – 32210Combined sources
Beta strandi324 – 3285Combined sources
Beta strandi335 – 34410Combined sources
Beta strandi348 – 36619Combined sources
Helixi377 – 3804Combined sources
Beta strandi384 – 39411Combined sources
Helixi395 – 3973Combined sources
Beta strandi403 – 42321Combined sources
Beta strandi428 – 43710Combined sources
Turni443 – 4475Combined sources
Helixi449 – 4546Combined sources
Beta strandi458 – 4636Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi469 – 4735Combined sources
Helixi475 – 4773Combined sources
Beta strandi478 – 4858Combined sources
Helixi486 – 4883Combined sources
Beta strandi494 – 5007Combined sources
Beta strandi503 – 5086Combined sources
Turni509 – 5146Combined sources
Beta strandi519 – 5213Combined sources
Beta strandi524 – 5285Combined sources
Helixi530 – 5334Combined sources
Beta strandi534 – 5407Combined sources
Beta strandi543 – 5486Combined sources
Helixi553 – 5597Combined sources
Beta strandi561 – 57515Combined sources
Beta strandi578 – 5847Combined sources
Turni591 – 5944Combined sources
Beta strandi602 – 6109Combined sources
Beta strandi612 – 6143Combined sources
Beta strandi616 – 6227Combined sources
Beta strandi628 – 6303Combined sources
Beta strandi633 – 6386Combined sources
Beta strandi641 – 6444Combined sources
Beta strandi646 – 6505Combined sources
Beta strandi662 – 6698Combined sources
Beta strandi672 – 68110Combined sources
Helixi682 – 6843Combined sources
Beta strandi686 – 6927Combined sources
Helixi1686 – 16883Combined sources
Beta strandi1693 – 16964Combined sources
Turni1704 – 17074Combined sources
Helixi1708 – 171811Combined sources
Beta strandi1723 – 17275Combined sources
Helixi1730 – 173910Combined sources
Turni1740 – 17423Combined sources
Beta strandi1745 – 17473Combined sources
Beta strandi1761 – 17666Combined sources
Helixi1767 – 17759Combined sources
Beta strandi1784 – 17907Combined sources
Helixi1796 – 181015Combined sources
Beta strandi1815 – 18195Combined sources
Beta strandi1837 – 18415Combined sources
Helixi1854 – 18585Combined sources
Beta strandi1863 – 18664Combined sources
Helixi1870 – 188213Combined sources
Beta strandi1887 – 18915Combined sources
Helixi1894 – 18985Combined sources
Helixi1899 – 19013Combined sources
Beta strandi1902 – 19043Combined sources
Beta strandi1908 – 19147Combined sources
Beta strandi1925 – 19295Combined sources
Beta strandi1936 – 19394Combined sources
Beta strandi1941 – 19433Combined sources
Beta strandi1945 – 19484Combined sources
Helixi1956 – 19638Combined sources
Beta strandi1975 – 19795Combined sources
Helixi1991 – 200111Combined sources
Helixi2015 – 20206Combined sources
Turni2025 – 20284Combined sources
Helixi2032 – 204312Combined sources
Helixi2049 – 20579Combined sources
Helixi2066 – 20683Combined sources
Helixi2073 – 20753Combined sources
Beta strandi2085 – 20873Combined sources
Beta strandi2093 – 20953Combined sources
Beta strandi2099 – 21024Combined sources
Helixi2103 – 21064Combined sources
Helixi2109 – 212012Combined sources
Helixi2535 – 254410Combined sources
Helixi2548 – 25547Combined sources
Turni2555 – 25584Combined sources
Beta strandi2560 – 25623Combined sources
Helixi2565 – 25728Combined sources
Helixi2585 – 25939Combined sources
Turni2594 – 25963Combined sources
Beta strandi2602 – 26076Combined sources
Helixi2613 – 26197Combined sources
Beta strandi2624 – 26307Combined sources
Helixi2648 – 26503Combined sources
Beta strandi2651 – 26544Combined sources
Helixi2659 – 26613Combined sources
Beta strandi2668 – 26725Combined sources
Helixi2681 – 269919Combined sources
Beta strandi2704 – 27118Combined sources
Helixi2716 – 272914Combined sources
Beta strandi2732 – 27343Combined sources
Beta strandi2746 – 27494Combined sources
Helixi2756 – 277015Combined sources
Beta strandi2780 – 27823Combined sources
Helixi2802 – 281615Combined sources
Turni2817 – 28204Combined sources
Beta strandi2830 – 283910Combined sources
Helixi2852 – 28565Combined sources
Helixi2859 – 28635Combined sources
Helixi2865 – 28684Combined sources
Beta strandi2870 – 28723Combined sources
Helixi2877 – 288711Combined sources
Helixi2897 – 291418Combined sources
Turni2915 – 29173Combined sources
Helixi2925 – 29328Combined sources
Turni2933 – 29353Combined sources
Helixi2943 – 29453Combined sources
Turni2946 – 29483Combined sources
Helixi2951 – 29566Combined sources
Helixi2958 – 297215Combined sources
Beta strandi2981 – 29877Combined sources
Beta strandi2989 – 29913Combined sources
Turni2994 – 29963Combined sources
Beta strandi3001 – 30055Combined sources
Helixi3008 – 301811Combined sources
Helixi3020 – 30234Combined sources
Turni3024 – 30274Combined sources
Helixi3029 – 30324Combined sources
Beta strandi3033 – 30353Combined sources
Helixi3041 – 305313Combined sources
Beta strandi3054 – 30574Combined sources
Helixi3067 – 30693Combined sources
Helixi3073 – 30797Combined sources
Helixi3080 – 30856Combined sources
Helixi3088 – 310013Combined sources
Turni3101 – 31033Combined sources
Beta strandi3104 – 311310Combined sources
Turni3114 – 31163Combined sources
Beta strandi3117 – 312610Combined sources
Helixi3136 – 315520Combined sources
Helixi3161 – 31633Combined sources
Helixi3169 – 318719Combined sources
Beta strandi3190 – 31934Combined sources
Beta strandi3196 – 31994Combined sources
Helixi3204 – 32085Combined sources
Helixi3211 – 32155Combined sources
Beta strandi3220 – 32234Combined sources
Beta strandi3232 – 32343Combined sources
Helixi3235 – 32373Combined sources
Beta strandi3243 – 32497Combined sources
Beta strandi3255 – 32606Combined sources
Helixi3263 – 32708Combined sources
Beta strandi3272 – 32754Combined sources
Helixi3280 – 329718Combined sources
Helixi3302 – 331413Combined sources
Beta strandi3336 – 33394Combined sources
Helixi3341 – 33499Combined sources
Turni3350 – 33523Combined sources
Helixi3365 – 33673Combined sources
Helixi3373 – 33786Combined sources
Helixi3386 – 340621Combined sources
Helixi3415 – 34173Combined sources
Helixi3419 – 34213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z83X-ray1.80A1685-2123[»]
3P54X-ray2.10A295-700[»]
4HDGX-ray2.38A/B2799-3432[»]
4HDHX-ray2.28A/B2799-3432[»]
4K6MX-ray2.60A/B2528-3432[»]
4MTPX-ray3.65A/B/C/D2799-3432[»]
ProteinModelPortaliP27395.
SMRiP27395. Positions 27-97, 295-693, 1423-1465, 1505-2123, 2533-2794, 2801-3426.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27395.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1505 – 1682178Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1685 – 1841157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1852 – 2017166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2528 – 2793266mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3057 – 3209153RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni1427 – 146640Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1789 – 17924DEAH box

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

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.
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.
IPR027287. Flavovir_Ig-like.
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.

P27395-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL
60 70 80 90 100
ITFFKFTALA PTKALLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR
110 120 130 140 150
KQNKRGGNEG SIMWLASLAV VIACAGAMKL SNFQGKLLMT INNTDIADVI
160 170 180 190 200
VIPTSKGENR CWVRAIDVGY MCEDTITYEC PKLTMGNDPE DVDCWCDNQE
210 220 230 240 250
VYVQYGRCTR TRHSKRSRRS VSVQTHGESS LVNKKEAWLD STKATRYLMK
260 270 280 290 300
TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM
310 320 330 340 350
GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV
360 370 380 390 400
RSYCYHASVT DISTVARCPT TGEAHNEKRA DSSYVCKQGF TDRGWGNGCG
410 420 430 440 450
LFGKGSIDTC AKFSCTSKAI GRTIQPENIK YEVGIFVHGT TTSENHGNYS
460 470 480 490 500
AQVGASQAAK FTVTPNAPSI TLKLGDYGEV TLDCEPRSGL NTEAFYVMTV
510 520 530 540 550
GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEGAH ATKQSVVALG
560 570 580 590 600
SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE
610 620 630 640 650
KFSFAKNPVD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT
660 670 680 690 700
VNPFVATSSA NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA
710 720 730 740 750
FSTTLKGAQR LAALGDTAWD FGSIGGVFNS IGRAVHQVFG GAFRTLFGGM
760 770 780 790 800
SWITQGLMGA LLLWMGVNAR DRSIALAFLA TGGVLVFLAT NVHADTGCAI
810 820 830 840 850
DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV HKAHKEGVCG
860 870 880 890 900
VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM
910 920 930 940 950
TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE
960 970 980 990 1000
DFGFGITSTR VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY
1010 1020 1030 1040 1050
NDTWKLERAV FGEVKSCTWP ETHTLWGDDV EESELIIPHT IAGPKSKHNR
1060 1070 1080 1090 1100
REGYKTQNQG PWDENGIVLD FDYCPGTKVT ITEDCSKRGP SVRTTTDSGK
1110 1120 1130 1140 1150
LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVMHDETTLV RSQVDAFKGE
1160 1170 1180 1190 1200
MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGVLLVL MLGGITYTDL
1210 1220 1230 1240 1250
ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN
1260 1270 1280 1290 1300
VILVLGAAFF QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV
1310 1320 1330 1340 1350
LALLTPGMRA LYLDTYRIIL LVIGICSLLH ERKKTMAKKK GAVLLGLALT
1360 1370 1380 1390 1400
STGWFSPTTI AAGLMVCNPN KKRGWPATEF LSAVGLMFAI VGGLAELDIE
1410 1420 1430 1440 1450
SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA ITGSSRRLDV
1460 1470 1480 1490 1500
KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK
1510 1520 1530 1540 1550
TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF
1560 1570 1580 1590 1600
HTLWHTTRGA AIMSGEGKLT PYWGSVREDR IAYGGPWRFD RKWNGTDDVQ
1610 1620 1630 1640 1650
VIVVEPGKAA VNIQTKPGVF RTPFGEVGAV SLDYPRGTSG SPILDSNGDI
1660 1670 1680 1690 1700
IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP EAYTPNMLRK RQMTVLDLHP
1710 1720 1730 1740 1750
GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL RGLPVRYQTS
1760 1770 1780 1790 1800
AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA
1810 1820 1830 1840 1850
ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS
1860 1870 1880 1890 1900
SGYEWITEYA GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP
1910 1920 1930 1940 1950
KCKNGDWDFV ITTDISEMGA NFGASRVIDC RKSVKPTILE EGEGRVILGN
1960 1970 1980 1990 2000
PSPITSASAA QRRGRVGRNP NQVGDEYHYG GATSEDDSNL AHWTEAKIML
2010 2020 2030 2040 2050
DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE LLRTADLPVW
2060 2070 2080 2090 2100
LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW
2110 2120 2130 2140 2150
LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM
2160 2170 2180 2190 2200
YLVATAEKGG KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI
2210 2220 2230 2240 2250
GKMGLGALVL TLATFFLWAA EVPGTKIAGT LLIALLLMVV LIPEPEKQRS
2260 2270 2280 2290 2300
QTDNQLAVFL ICVLTVVGVV AANEYGMLEK TKADLKSMFG GKTQASGLTG
2310 2320 2330 2340 2350
LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS LASINSQAGS
2360 2370 2380 2390 2400
LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG
2410 2420 2430 2440 2450
WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL
2460 2470 2480 2490 2500
IGVSVAAFLV NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH
2510 2520 2530 2540 2550
VMRGSYLAGG SIAWTLIKNA DKPSLKRGRP GGRTLGEQWK EKLNAMSREE
2560 2570 2580 2590 2600
FFKYRREAII EVDRTEARRA RRENNIVGGH PVSRGSAKLR WLVEKGFVSP
2610 2620 2630 2640 2650
IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP MLMQSYGWNL
2660 2670 2680 2690 2700
VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH
2710 2720 2730 2740 2750
RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS
2760 2770 2780 2790 2800
GAAGNVVHAV NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH
2810 2820 2830 2840 2850
SNQEKIKKRI QKLKEEFATT WHKDPEHPYR TWTYHGSYEV KATGSASSLV
2860 2870 2880 2890 2900
NGVVELMSKP WDAIANVTTM AMTDTTPFGQ QRVFKEKVDT KAPEPPAGAK
2910 2920 2930 2940 2950
EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA VFAEQNQWST
2960 2970 2980 2990 3000
AREAVDDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS
3010 3020 3030 3040 3050
RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD
3060 3070 3080 3090 3100
IAGKQGGKMY ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL
3110 3120 3130 3140 3150
TYRHKVVKVM RPAAEGKTVM DVISREDQRG SGQVVTYALN TFTNIAVQLV
3160 3170 3180 3190 3200
RLMEAEGVIG PQHLEQLPRK TKIAVRTWLF ENGEERVTRM AISGDDCVVK
3210 3220 3230 3240 3250
PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF CSNHFQEIVM
3260 3270 3280 3290 3300
KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH
3310 3320 3330 3340 3350
RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLQVWNRVWI
3360 3370 3380 3390 3400
EENEWMMDKT PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN
3410 3420 3430
QVRAVIGKEN YVDYMTSLRR YEDVLIQEDR VI
Length:3,432
Mass (Da):380,211
Last modified:August 1, 1992 - v1
Checksum:i11B9423735B1B5FE
GO

Sequence cautioni

The sequence AAA46249.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55506 Genomic RNA. Translation: AAA46248.1.
M55506 Genomic RNA. Translation: AAA46249.1. Different initiation.
PIRiA35519. GNWVJS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55506 Genomic RNA. Translation: AAA46248.1.
M55506 Genomic RNA. Translation: AAA46249.1. Different initiation.
PIRiA35519. GNWVJS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z83X-ray1.80A1685-2123[»]
3P54X-ray2.10A295-700[»]
4HDGX-ray2.38A/B2799-3432[»]
4HDHX-ray2.28A/B2799-3432[»]
4K6MX-ray2.60A/B2528-3432[»]
4MTPX-ray3.65A/B/C/D2799-3432[»]
ProteinModelPortaliP27395.
SMRiP27395. Positions 27-97, 295-693, 1423-1465, 1505-2123, 2533-2794, 2801-3426.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.6.4.12. 2787.
3.6.4.13. 2787.

Miscellaneous databases

EvolutionaryTraceiP27395.

Family and domain databases

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.
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.
IPR027287. Flavovir_Ig-like.
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...

Publicationsi

  1. "Nucleotide sequence of the virulent SA-14 strain of Japanese encephalitis virus and its attenuated vaccine derivative, SA-14-14-2."
    Nitayaphan S., Grant J.A., Chang G.J.J., Trent D.W.
    Virology 177:541-552(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Nuclear localization of flavivirus RNA synthesis in infected cells."
    Uchil P.D., Kumar A.V., Satchidanandam V.
    J. Virol. 80:5451-5464(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF SERINE PROTEASE NS3, SUBCELLULAR LOCATION OF RNA-DIRECTED RNA POLYMERASE NS5.
    Strain: P20778.
  3. "Interferon antagonist function of Japanese encephalitis virus NS4A and its interaction with DEAD-box RNA helicase DDX42."
    Lin C.-W., Cheng C.W., Yang T.-C., Li S.-W., Cheng M.-H., Wan L., Lin Y.-J., Lai C.H., Lin W.-Y., Kao M.-C.
    Virus Res. 137:49-55(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF NON-STRUCTURAL PROTEIN 4A.
  4. "Blocking of interferon-induced Jak-Stat signaling by Japanese encephalitis virus NS5 through a protein tyrosine phosphatase-mediated mechanism."
    Lin R.J., Chang B.L., Yu H.P., Liao C.L., Lin Y.L.
    J. Virol. 80:5908-5918(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
  5. "Involvement of ceramide in the propagation of Japanese encephalitis virus."
    Tani H., Shiokawa M., Kaname Y., Kambara H., Mori Y., Abe T., Moriishi K., Matsuura Y.
    J. Virol. 84:2798-2807(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF ENVELOPE PROTEIN E.
    Strain: AT31.
  6. "Crystal structure of the catalytic domain of Japanese encephalitis virus NS3 helicase/nucleoside triphosphatase at a resolution of 1.8 A."
    Yamashita T., Unno H., Mori Y., Tani H., Moriishi K., Takamizawa A., Agoh M., Tsukihara T., Matsuura Y.
    Virology 373:426-436(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1685-2123, MUTAGENESIS OF GLY-1703; LYS-1704; THR-1705; GLN-1961; ARG-1962; ARG-1965 AND ARG-1968.

Entry informationi

Entry nameiPOLG_JAEV1
AccessioniPrimary (citable) accession number: P27395
Secondary accession number(s): Q82920
, Q82921, Q82922, Q82923, Q82924, Q82925, Q82926, Q82927, Q82928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: December 9, 2015
This is version 137 of the entry and version 1 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.