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P14335

- POLG_KUNJM

UniProt

P14335 - POLG_KUNJM

Protein

Genome polyprotein

Gene
N/A
Organism
Kunjin virus (strain MRM61C)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA By similarity.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.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.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.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.4 PublicationsPROSITE-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
    Sitei105 – 1062Cleavage; by viral protease NS3Sequence Analysis
    Sitei123 – 1242Cleavage; by host signal peptidaseBy similarity
    Sitei215 – 2162Cleavage; by host furinSequence Analysis
    Sitei290 – 2912Cleavage; by host signal peptidaseSequence Analysis
    Sitei791 – 7922Cleavage; by host signal peptidaseSequence Analysis
    Sitei1143 – 11442Cleavage; by hostSequence Analysis
    Sitei1374 – 13752Cleavage; by viral protease NS3Sequence Analysis
    Sitei1505 – 15062Cleavage; by autolysisSequence Analysis
    Active sitei1556 – 15561Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Active sitei1580 – 15801Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Active sitei1640 – 16401Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Sitei2124 – 21252Cleavage; by autolysisSequence Analysis
    Sitei2250 – 22512Cleavage; by viral protease NS3Sequence Analysis
    Sitei2273 – 22742Cleavage; by host signal peptidaseSequence Analysis
    Sitei2528 – 25292Cleavage; by viral protease NS3Sequence Analysis
    Binding sitei2541 – 25411mRNA capPROSITE-ProRule annotation
    Binding sitei2544 – 25441mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei2545 – 25451mRNA capPROSITE-ProRule annotation
    Binding sitei2547 – 25471mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
    Sitei2552 – 25521mRNA cap bindingPROSITE-ProRule annotation
    Binding sitei2556 – 25561mRNA capPROSITE-ProRule annotation
    Binding sitei2584 – 25841S-adenosyl-L-methioninePROSITE-ProRule annotation
    Sitei2589 – 25891Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
    Binding sitei2614 – 26141S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei2615 – 26151S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei2632 – 26321S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei2633 – 26331S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei2659 – 26591S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei2660 – 26601S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Sitei2674 – 26741Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
    Sitei2675 – 26751S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
    Binding sitei2678 – 26781mRNA capPROSITE-ProRule annotation
    Sitei2710 – 27101Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
    Binding sitei2741 – 27411mRNA capPROSITE-ProRule annotation
    Binding sitei2743 – 27431mRNA capPROSITE-ProRule annotation
    Sitei2746 – 27461Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
    Binding sitei2748 – 27481S-adenosyl-L-methioninePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1699 – 17068ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. double-stranded RNA binding Source: InterPro
    4. metal ion binding Source: UniProtKB-KW
    5. mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-EC
    6. mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB-EC
    7. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    8. RNA helicase activity Source: InterPro
    9. serine-type endopeptidase activity Source: InterPro
    10. serine-type exopeptidase activity Source: InterPro
    11. structural molecule activity Source: InterPro

    GO - Biological processi

    1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    3. induction by virus of host autophagy Source: UniProtKB-KW
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. suppression by virus of host JAK1 activity Source: UniProtKB-KW
    6. suppression by virus of host TYK2 activity Source: UniProtKB-KW
    7. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
    8. transcription, DNA-templated Source: UniProtKB-KW
    9. viral RNA genome replication Source: InterPro
    10. virion attachment to host cell Source: UniProtKB-KW

    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

    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
    OrganismiKunjin virus (strain MRM61C)
    Taxonomic identifieri11078 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
    Virus hostiCiconiiformes [TaxID: 8920]
    Culex annulirostris (Common banded mosquito) [TaxID: 162997]
    Equus caballus (Horse) [TaxID: 9796]
    Homo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008379: Genome

    Subcellular locationi

    Chain Peptide pr : Secreted By similarity
    Chain Small envelope protein M : Virion membrane By similarity; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain Envelope protein E : Virion membrane By similarity; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain Non-structural protein 1 : Secreted. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Lumenal side By similarity
    Chain Non-structural protein 2A : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein Curated
    Chain Serine protease subunit NS2B : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein Curated
    Chain 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
    Chain Non-structural protein 4A : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Note: Located in RE-associated vesicles hosting the replication complex.
    Chain Non-structural protein 4B : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain 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.

    GO - Cellular componenti

    1. host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. viral capsid Source: UniProtKB-KW
    5. viral envelope Source: UniProtKB-KW
    6. virion membrane Source: UniProtKB-SubCell

    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
    Mutagenesisi1292 – 12921T → P: Restores induction of virus-specific membrane structures; when associated with N-1202. 1 Publication
    Mutagenesisi3181 – 31811S → F: Increases STAT1 inhibitory function of NS5. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedSequence Analysis
    Chaini2 – 34333432Genome polyproteinPRO_0000405136Add
    BLAST
    Chaini2 – 105104Capsid protein CBy similarityPRO_0000037703Add
    BLAST
    Propeptidei106 – 12318ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000405137Add
    BLAST
    Chaini124 – 290167prMBy similarityPRO_0000405138Add
    BLAST
    Chaini124 – 21592Peptide prBy similarityPRO_0000037704Add
    BLAST
    Chaini216 – 29075Small envelope protein MBy similarityPRO_0000037705Add
    BLAST
    Chaini291 – 791501Envelope protein EBy similarityPRO_0000037706Add
    BLAST
    Chaini792 – 1143352Non-structural protein 1By similarityPRO_0000037707Add
    BLAST
    Chaini1144 – 1374231Non-structural protein 2ABy similarityPRO_0000037708Add
    BLAST
    Chaini1375 – 1505131Serine protease subunit NS2BBy similarityPRO_0000037709Add
    BLAST
    Chaini1506 – 2124619Serine protease NS3By similarityPRO_0000037710Add
    BLAST
    Chaini2125 – 2250126Non-structural protein 4ABy similarityPRO_0000037711Add
    BLAST
    Peptidei2251 – 227323Peptide 2kBy similarityPRO_0000405139Add
    BLAST
    Chaini2274 – 2528255Non-structural protein 4BBy similarityPRO_0000037712Add
    BLAST
    Chaini2529 – 3433905RNA-directed RNA polymerase NS5By similarityPRO_0000037713Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi138 – 1381N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi293 ↔ 320By similarity
    Disulfide bondi350 ↔ 406By similarity
    Disulfide bondi364 ↔ 395By similarity
    Disulfide bondi382 ↔ 411By similarity
    Disulfide bondi480 ↔ 578By similarity
    Disulfide bondi595 ↔ 626By similarity
    Glycosylationi921 – 9211N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi966 – 9661N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi998 – 9981N-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.By similarity
    RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization By similarity.By similarity

    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.By similarity

    Structurei

    Secondary structure

    1
    3433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 3813
    Helixi44 – 5613
    Helixi63 – 697
    Helixi74 – 9522
    Beta strandi1694 – 16974
    Turni1703 – 17086
    Helixi1709 – 171911
    Beta strandi1724 – 17307
    Helixi1731 – 174010
    Beta strandi1763 – 17675
    Helixi1768 – 17769
    Beta strandi1777 – 17793
    Beta strandi1785 – 17917
    Helixi1797 – 181115
    Beta strandi1816 – 18205
    Beta strandi1839 – 18424
    Beta strandi1851 – 18533
    Helixi1855 – 18595
    Beta strandi1864 – 18674
    Helixi1871 – 188313
    Beta strandi1888 – 18914
    Beta strandi1909 – 19146
    Beta strandi1926 – 19305
    Beta strandi1937 – 19448
    Beta strandi1946 – 19494
    Helixi1957 – 19648
    Beta strandi1977 – 19804
    Helixi1992 – 200211
    Helixi2007 – 20093
    Helixi2016 – 20216
    Turni2026 – 20294
    Helixi2034 – 204411
    Helixi2050 – 20589
    Helixi2066 – 20694
    Helixi2074 – 20763
    Beta strandi2079 – 20846
    Beta strandi2086 – 20883
    Beta strandi2094 – 20963
    Beta strandi2100 – 21034
    Helixi2104 – 21063
    Helixi2110 – 212112
    Helixi2808 – 28158
    Turni2819 – 28213
    Beta strandi2831 – 284010
    Helixi2853 – 28575
    Helixi2860 – 28623
    Turni2870 – 28723
    Helixi2878 – 28858
    Helixi2898 – 291518
    Turni2916 – 29183
    Helixi2926 – 29349
    Helixi2951 – 29577
    Helixi2959 – 297416
    Helixi3004 – 301916
    Helixi3021 – 30244
    Turni3025 – 30284
    Helixi3030 – 30334
    Beta strandi3034 – 30363
    Helixi3042 – 305211
    Beta strandi3055 – 30584
    Beta strandi3065 – 30673
    Helixi3068 – 30703
    Helixi3074 – 30807
    Helixi3081 – 30866
    Helixi3089 – 309911
    Turni3100 – 31034
    Beta strandi3104 – 311310
    Helixi3115 – 31173
    Beta strandi3119 – 312810
    Helixi3134 – 315623
    Beta strandi3164 – 31674
    Helixi3172 – 318817
    Beta strandi3191 – 31944
    Beta strandi3197 – 32004
    Helixi3205 – 32095
    Helixi3212 – 32165
    Turni3236 – 32383
    Beta strandi3244 – 32507
    Beta strandi3256 – 32616
    Helixi3264 – 32718
    Beta strandi3275 – 32784
    Helixi3282 – 329817
    Helixi3303 – 331513
    Beta strandi3338 – 33403
    Helixi3342 – 33509
    Turni3351 – 33533
    Helixi3366 – 33683
    Helixi3374 – 33796
    Helixi3387 – 33948
    Helixi3396 – 340712
    Helixi3416 – 34183

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SFKX-ray3.20A/B/C/D/E/F/G/H23-98[»]
    2HCNX-ray2.35A2846-3433[»]
    2HCSX-ray2.50A2846-3433[»]
    2HFZX-ray3.00A2802-3433[»]
    2OF6electron microscopy24.00A/B/C291-690[»]
    2QEQX-ray3.10A/B1691-2124[»]
    ProteinModelPortaliP14335.
    SMRiP14335. Positions 25-97, 291-693, 1424-1467, 1506-2124, 2534-2795, 2802-3427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14335.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 105104CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini127 – 248122ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini270 – 2734CytoplasmicSequence Analysis
    Topological domaini291 – 743453ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini764 – 7707ExtracellularSequence Analysis
    Topological domaini792 – 1142351ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1164 – 121653CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1238 – 124710LumenalSequence Analysis
    Topological domaini1269 – 129628CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1318 – 134427LumenalSequence AnalysisAdd
    BLAST
    Topological domaini1366 – 137510CytoplasmicSequence Analysis
    Topological domaini1397 – 13993LumenalSequence Analysis
    Topological domaini1421 – 147757CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1499 – 2174676CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2196 – 22005LumenalSequence Analysis
    Topological domaini2222 – 22221LumenalSequence Analysis
    Topological domaini2244 – 225815CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2280 – 231233LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2334 – 235825LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2380 – 23801LumenalSequence Analysis
    Topological domaini2402 – 244443CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2466 – 24705LumenalSequence Analysis
    Topological domaini2492 – 3433942CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei744 – 76320HelicalSequence AnalysisAdd
    BLAST
    Intramembranei771 – 79121HelicalSequence AnalysisAdd
    BLAST
    Intramembranei1478 – 149821HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2201 – 222121HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2313 – 233321HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2359 – 237921HelicalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei106 – 12621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei249 – 26921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei274 – 29017HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1143 – 116321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1217 – 123721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1248 – 126821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1297 – 131721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1345 – 136521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1376 – 139621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1400 – 142021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2259 – 227921Helical; Note=Signal for NS4BSequence AnalysisAdd
    BLAST
    Transmembranei2381 – 240121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2445 – 246521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2471 – 249121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1506 – 1683178Peptidase S7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1686 – 1842157Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1853 – 2018166Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini2529 – 2794266mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
    BLAST
    Domaini3058 – 3210153RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
    BLAST
    Regioni388 – 40114Involved in fusionAdd
    BLAST
    Regioni1428 – 146740Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1790 – 17934DEAH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi281 – 2844Poly-Leu
    Compositional biasi2678 – 26814Poly-Ser

    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.
    IPR000208. RNA-dir_pol_flavivirus.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    [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.
    PF00271. Helicase_C. 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.

    P14335-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKKPGGPGK SRAVNMLKRG MPRVLSLTGL KRAMLSLIDG RGPTRFVLAL     50
    LAFFRFTAIA PTRAVLDRWR SVNKQTAMKH LLSFKKELGT LTSAINRRSS 100
    KQKKRGGKTG IAFMIGLIAG VGAVTLSNFQ GKVMMTVNAT DVTDIITIPP 150
    AAGKNLCIVR AMDVGHMCDD TITYECPVLS AGNDPEDIDC WCTKLAVYVR 200
    YGRCTKTRHS RRSRRSLTVQ THGESTLSNK KGAWMDSTKA TRYLVKTESW 250
    ILRNPGYALV AAVIGWMLGS NTMQRVVFAV LLLLVAPAYS FNCLGMSNRD 300
    FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC 350
    YLATVSELST KAACPTMGEA HNDKRADPSF VCKQGVVDRG WGNGCGLFGK 400
    GSIDTCAKFA CSTKATGRTI LKENIKYEVA IFVHGPTTVE SHGNYFTQTG 450
    AAQAGRFSIT PAAPSYTLKL GEYGEVTVDC EPRSGIDTSA YYVMTVGTKT 500
    FLVHREWFMD LNLPWSSAES NVWRNRETLM EFEEPHATKQ SVIALGSQEG 550
    ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFR 600
    FLGTPADTGH GTVVLELQYT GTDGPCKIPI SSVASLNDLT PVGRLVTVNP 650
    FVSVSTANAK VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTA 700
    TLKGAQRLAA LGDTAWDFGS VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI 750
    TQGLLGALLL WMGINARDRS IALTFLAVGG VLLFLSVNVH ADTGCAIDIS 800
    RQELRCGSGV FIHNDVEAWI DRYKYYPETP QGLAKIIQKA HKEGVCGLRS 850
    VSRLEHQMWE AVKDELNTLL KENGVDLSIV VEKQEGMYKS APRRLTATTE 900
    KLEIGWKAWG KSILFAPELA NNTFVIDGPE TKECPTQNRA WNNLEVEDFG 950
    FGLTSTRMFL RVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRFNDT 1000
    WKLERAVLGE VKSCTWPETH TLWGDGVLES DLIIPITLAG PRSNHNRRPG 1050
    YKTQSQGPWD EGRVEIDFDY CPGTTVTLSE SCGHRGPATR TTTESGKLIT 1100
    DWCCRSCTLP PLRYQTDNGC WYGMEIRPQR HDEKTLVQSQ VNAYNADMID 1150
    PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY 1200
    VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL 1250
    MLAAAFFQMA YYDARQILLW EMPDVLNSLA VAWMILRAIT FTTTSNVVVP 1300
    LLALLTPGLR CLNLDVYRIL LLMVGIGSLI REKRSAAAKK KGASLLCLAL 1350
    ASTGFFNPMI LAAGLVACDP NRKRGWPATE VMTAVGLMFA IVGGLAELDI 1400
    DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWEGDA EITGSSERVD 1450
    VRLDDDGNFQ LMNDPGAPWK IWMLRMACLA ISAYTPWAIL PSVVGFWITL 1500
    QYTKRGGVLW DTPSPKEYKR GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV 1550
    FHTLWHTTKG AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV 1600
    QMIVVEPGKN VKNVQTKPGV FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD 1650
    VIGLYGNGVI MPNGSYISAI VQGERMDEPV PAGFEPEMLR KKQITVLDLH 1700
    PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA LRGLPIRYQT 1750
    SAVAREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI 1800
    AARGYISTRV ELGEAAAIFM TATPPGTSDP FPESNAPISD LQTEIPDRAW 1850
    NSGYEWITEY IGKTVWFVPS VKMGNEIALC LQRAGKKVIQ LNRKSYETEY 1900
    PKCKNDDWDF VVTTDISEMG ANFKASRVID SRKSVKPTII TEGEGRVILG 1950
    EPSAVTAASA AQRRGRTGRN PSQAGDEYCY GGHTNEDDSN CAHWTEARIM 2000
    LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL ELLRTADLPV 2050
    WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR 2100
    WIDARVYSDH QALKSFKDFA SGKRSQIGFI EVLGKMPEHF MGKTWEALDT 2150
    MYVVATAEKG GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG 2200
    IGKIGLGGVV LGAATFFCWM AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR 2250
    SQTDNQLAVF LICVLTLVGA VAANEMGWLD KTKSDISGLF GQRIETKENF 2300
    SIGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYITT SLTSINVQAS 2350
    ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTSATL LFCHYAYMVP 2400
    GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQVM 2450
    LILVSLAALV VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC 2500
    HIMRGGWLSC LSITWTLVKN MEKPGLKRGG AKGRTLGEVW KERLNQMTKE 2550
    EFIRYRKEAI TEVDRSAAKH ARKERNITGG HPVSRGTAKL RWLVERRFLE 2600
    PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE PQLVQSYGWN 2650
    IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTL RVLEMVEDWL 2700
    HRGPKEFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV 2750
    SRASGNVVHS VNMTSQVLLG RMEKKTWKGP QYEEDVNLGS GTRAVGKPLL 2800
    NSDTSKIKNR IERLRREYSS TWHHDENHPY RTWNYHGSYE VKPTGSASSL 2850
    VNGVVRLLSK PWDTITNVTT MAMTDTTPFG QQRVFKEKVD TKAPEPPEGV 2900
    KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG AMFEEQNQWR 2950
    SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG 3000
    SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR 3050
    EVGTRPGGRI YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE 3100
    LTYRHKVVKV MRPAADGRTV MDVISREDQR GSGQVVTYAL NTFTNLAVQL 3150
    VRMMEGEGVI GPDDVEKLTK GKGPKVRTWL SENGEERLSR MAVSGDDCVV 3200
    KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP FCSNHFTELI 3250
    MKDGRTLVTP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF 3300
    HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW 3350
    IEENEWMEDK TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI 3400
    NQVRSIIGDE KYVDYMSSLK RYEDTTLVED TVL 3433
    Length:3,433
    Mass (Da):381,369
    Last modified:January 1, 1990 - v1
    Checksum:iEE4B888A7D040B99
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501P → T in strain: Infectious clone pAKUN and Infectious clone FLSDX.
    Natural varianti820 – 8201I → M in strain: Infectious clone pAKUNa and Infectious clone FLSDX.
    Natural varianti943 – 9431N → S in strain: Infectious clone pAKUN and Infectious clone FLSDX.
    Natural varianti1041 – 10411P → L in strain: Infectious clone pAKUN and Infectious clone FLSDX.
    Natural varianti1202 – 12021I → N in strain: Infectious clone pAKUN; blocks induction of virus-specific membrane structures.
    Natural varianti1318 – 13181R → K in strain: Infectious clone pAKUN.
    Natural varianti1967 – 19671T → I in strain: Infectious clone pAKUN and Infectious clone FLSDX.
    Natural varianti1974 – 19741A → V in strain: Infectious clone pAKUN and Infectious clone FLSDX.
    Natural varianti2023 – 20231Y → H in strain: Infectious clone pAKUN.
    Natural varianti2062 – 20621S → P in strain: Infectious clone pAKUN.
    Natural varianti2339 – 23391T → N in strain: Infectious clone pAKUN and Infectious clone FLSDX.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00246 Genomic RNA. Translation: BAA00176.1.
    AY274504 Genomic RNA. Translation: AAP78941.1.
    AY274505 Genomic RNA. Translation: AAP78942.1.
    PIRiA28697. GNWVKV.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00246 Genomic RNA. Translation: BAA00176.1 .
    AY274504 Genomic RNA. Translation: AAP78941.1 .
    AY274505 Genomic RNA. Translation: AAP78942.1 .
    PIRi A28697. GNWVKV.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SFK X-ray 3.20 A/B/C/D/E/F/G/H 23-98 [» ]
    2HCN X-ray 2.35 A 2846-3433 [» ]
    2HCS X-ray 2.50 A 2846-3433 [» ]
    2HFZ X-ray 3.00 A 2802-3433 [» ]
    2OF6 electron microscopy 24.00 A/B/C 291-690 [» ]
    2QEQ X-ray 3.10 A/B 1691-2124 [» ]
    ProteinModelPortali P14335.
    SMRi P14335. Positions 25-97, 291-693, 1424-1467, 1506-2124, 2534-2795, 2802-3427.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S07.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P14335.

    Family and domain databases

    Gene3Di 2.60.40.350. 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.
    InterProi IPR011492. 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.
    IPR000208. RNA-dir_pol_flavivirus.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF01003. 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.
    PF00271. Helicase_C. 1 hit.
    PF00949. Peptidase_S7. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003817. Gen_Poly_FLV. 1 hit.
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF53335. SSF53335. 1 hit.
    SSF56983. SSF56983. 1 hit.
    SSF81296. SSF81296. 1 hit.
    TIGRFAMsi TIGR04240. flavi_E_stem. 1 hit.
    PROSITEi PS51527. FLAVIVIRUS_NS2B. 1 hit.
    PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51591. RNA_CAP01_NS5_MT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide and complete amino acid sequences of Kunjin virus: definitive gene order and characteristics of the virus-specified proteins."
      Coia G., Parker M.D., Speight G., Byrne M.E., Westaway E.G.
      J. Gen. Virol. 69:1-21(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Molecular and functional analyses of Kunjin virus infectious cDNA clones demonstrate the essential role for NS2A in virus assembly and for a nonconservative residue in NS3 in RNA replication."
      Liu W.J., Chen H.B., Khromykh A.A.
      J. Virol. 77:7804-7813(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Infectious clone FLSDX and Infectious clone pAKUN.
    3. "Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A."
      Mackenzie J.M., Khromykh A.A., Jones M.K., Westaway E.G.
      Virology 245:203-215(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION OF NON-STRUCTURAL PROTEIN 2A, NON-STRUCTURAL PROTEIN 4A.
    4. Cited for: FUNCTION OF NON-STRUCTURAL PROTEIN 2A, MUTAGENESIS OF THR-1292, CHARACTERIZATION OF VARIANT ASN-1202.
    5. "The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex."
      Gillespie L.K., Hoenen A., Morgan G., Mackenzie J.M.
      J. Virol. 84:10438-10447(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NON-STRUCTURAL PROTEIN 4A.
    6. "West Nile virus core protein; tetramer structure and ribbon formation."
      Dokland T., Walsh M., Mackenzie J.M., Khromykh A.A., Ee K.H., Wang S.
      Structure 12:1157-1163(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-98.
    7. "West Nile virus inhibits the signal transduction pathway of alpha interferon."
      Guo J.T., Hayashi J., Seeger C.
      J. Virol. 79:1343-1350(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
    8. "The NS5 protein of the virulent West Nile virus NY99 strain is a potent antagonist of type I interferon-mediated JAK-STAT signaling."
      Laurent-Rolle M., Boer E.F., Lubick K.J., Wolfinbarger J.B., Carmody A.B., Rockx B., Liu W., Ashour J., Shupert W.L., Holbrook M.R., Barrett A.D., Mason P.W., Bloom M.E., Garcia-Sastre A., Khromykh A.A., Best S.M.
      J. Virol. 84:3503-3515(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5, MUTAGENESIS OF SER-3181.

    Entry informationi

    Entry nameiPOLG_KUNJM
    AccessioniPrimary (citable) accession number: P14335
    Secondary accession number(s): Q7T4P4, Q7T4P5, Q82983
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 143 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

    External Data

    Dasty 3