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P14335

- POLG_KUNJM

UniProt

P14335 - POLG_KUNJM

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Protein

Genome polyprotein

Gene
N/A
Organism
Kunjin virus (strain MRM61C)
Status
Reviewed - 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).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
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

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

        10         20         30         40         50
MSKKPGGPGK SRAVNMLKRG MPRVLSLTGL KRAMLSLIDG RGPTRFVLAL
60 70 80 90 100
LAFFRFTAIA PTRAVLDRWR SVNKQTAMKH LLSFKKELGT LTSAINRRSS
110 120 130 140 150
KQKKRGGKTG IAFMIGLIAG VGAVTLSNFQ GKVMMTVNAT DVTDIITIPP
160 170 180 190 200
AAGKNLCIVR AMDVGHMCDD TITYECPVLS AGNDPEDIDC WCTKLAVYVR
210 220 230 240 250
YGRCTKTRHS RRSRRSLTVQ THGESTLSNK KGAWMDSTKA TRYLVKTESW
260 270 280 290 300
ILRNPGYALV AAVIGWMLGS NTMQRVVFAV LLLLVAPAYS FNCLGMSNRD
310 320 330 340 350
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC
360 370 380 390 400
YLATVSELST KAACPTMGEA HNDKRADPSF VCKQGVVDRG WGNGCGLFGK
410 420 430 440 450
GSIDTCAKFA CSTKATGRTI LKENIKYEVA IFVHGPTTVE SHGNYFTQTG
460 470 480 490 500
AAQAGRFSIT PAAPSYTLKL GEYGEVTVDC EPRSGIDTSA YYVMTVGTKT
510 520 530 540 550
FLVHREWFMD LNLPWSSAES NVWRNRETLM EFEEPHATKQ SVIALGSQEG
560 570 580 590 600
ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFR
610 620 630 640 650
FLGTPADTGH GTVVLELQYT GTDGPCKIPI SSVASLNDLT PVGRLVTVNP
660 670 680 690 700
FVSVSTANAK VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTA
710 720 730 740 750
TLKGAQRLAA LGDTAWDFGS VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI
760 770 780 790 800
TQGLLGALLL WMGINARDRS IALTFLAVGG VLLFLSVNVH ADTGCAIDIS
810 820 830 840 850
RQELRCGSGV FIHNDVEAWI DRYKYYPETP QGLAKIIQKA HKEGVCGLRS
860 870 880 890 900
VSRLEHQMWE AVKDELNTLL KENGVDLSIV VEKQEGMYKS APRRLTATTE
910 920 930 940 950
KLEIGWKAWG KSILFAPELA NNTFVIDGPE TKECPTQNRA WNNLEVEDFG
960 970 980 990 1000
FGLTSTRMFL RVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRFNDT
1010 1020 1030 1040 1050
WKLERAVLGE VKSCTWPETH TLWGDGVLES DLIIPITLAG PRSNHNRRPG
1060 1070 1080 1090 1100
YKTQSQGPWD EGRVEIDFDY CPGTTVTLSE SCGHRGPATR TTTESGKLIT
1110 1120 1130 1140 1150
DWCCRSCTLP PLRYQTDNGC WYGMEIRPQR HDEKTLVQSQ VNAYNADMID
1160 1170 1180 1190 1200
PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY
1210 1220 1230 1240 1250
VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL
1260 1270 1280 1290 1300
MLAAAFFQMA YYDARQILLW EMPDVLNSLA VAWMILRAIT FTTTSNVVVP
1310 1320 1330 1340 1350
LLALLTPGLR CLNLDVYRIL LLMVGIGSLI REKRSAAAKK KGASLLCLAL
1360 1370 1380 1390 1400
ASTGFFNPMI LAAGLVACDP NRKRGWPATE VMTAVGLMFA IVGGLAELDI
1410 1420 1430 1440 1450
DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWEGDA EITGSSERVD
1460 1470 1480 1490 1500
VRLDDDGNFQ LMNDPGAPWK IWMLRMACLA ISAYTPWAIL PSVVGFWITL
1510 1520 1530 1540 1550
QYTKRGGVLW DTPSPKEYKR GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV
1560 1570 1580 1590 1600
FHTLWHTTKG AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV
1610 1620 1630 1640 1650
QMIVVEPGKN VKNVQTKPGV FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD
1660 1670 1680 1690 1700
VIGLYGNGVI MPNGSYISAI VQGERMDEPV PAGFEPEMLR KKQITVLDLH
1710 1720 1730 1740 1750
PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA LRGLPIRYQT
1760 1770 1780 1790 1800
SAVAREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI
1810 1820 1830 1840 1850
AARGYISTRV ELGEAAAIFM TATPPGTSDP FPESNAPISD LQTEIPDRAW
1860 1870 1880 1890 1900
NSGYEWITEY IGKTVWFVPS VKMGNEIALC LQRAGKKVIQ LNRKSYETEY
1910 1920 1930 1940 1950
PKCKNDDWDF VVTTDISEMG ANFKASRVID SRKSVKPTII TEGEGRVILG
1960 1970 1980 1990 2000
EPSAVTAASA AQRRGRTGRN PSQAGDEYCY GGHTNEDDSN CAHWTEARIM
2010 2020 2030 2040 2050
LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL ELLRTADLPV
2060 2070 2080 2090 2100
WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR
2110 2120 2130 2140 2150
WIDARVYSDH QALKSFKDFA SGKRSQIGFI EVLGKMPEHF MGKTWEALDT
2160 2170 2180 2190 2200
MYVVATAEKG GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG
2210 2220 2230 2240 2250
IGKIGLGGVV LGAATFFCWM AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR
2260 2270 2280 2290 2300
SQTDNQLAVF LICVLTLVGA VAANEMGWLD KTKSDISGLF GQRIETKENF
2310 2320 2330 2340 2350
SIGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYITT SLTSINVQAS
2360 2370 2380 2390 2400
ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTSATL LFCHYAYMVP
2410 2420 2430 2440 2450
GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQVM
2460 2470 2480 2490 2500
LILVSLAALV VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC
2510 2520 2530 2540 2550
HIMRGGWLSC LSITWTLVKN MEKPGLKRGG AKGRTLGEVW KERLNQMTKE
2560 2570 2580 2590 2600
EFIRYRKEAI TEVDRSAAKH ARKERNITGG HPVSRGTAKL RWLVERRFLE
2610 2620 2630 2640 2650
PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE PQLVQSYGWN
2660 2670 2680 2690 2700
IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTL RVLEMVEDWL
2710 2720 2730 2740 2750
HRGPKEFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV
2760 2770 2780 2790 2800
SRASGNVVHS VNMTSQVLLG RMEKKTWKGP QYEEDVNLGS GTRAVGKPLL
2810 2820 2830 2840 2850
NSDTSKIKNR IERLRREYSS TWHHDENHPY RTWNYHGSYE VKPTGSASSL
2860 2870 2880 2890 2900
VNGVVRLLSK PWDTITNVTT MAMTDTTPFG QQRVFKEKVD TKAPEPPEGV
2910 2920 2930 2940 2950
KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG AMFEEQNQWR
2960 2970 2980 2990 3000
SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG
3010 3020 3030 3040 3050
SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR
3060 3070 3080 3090 3100
EVGTRPGGRI YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE
3110 3120 3130 3140 3150
LTYRHKVVKV MRPAADGRTV MDVISREDQR GSGQVVTYAL NTFTNLAVQL
3160 3170 3180 3190 3200
VRMMEGEGVI GPDDVEKLTK GKGPKVRTWL SENGEERLSR MAVSGDDCVV
3210 3220 3230 3240 3250
KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP FCSNHFTELI
3260 3270 3280 3290 3300
MKDGRTLVTP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF
3310 3320 3330 3340 3350
HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW
3360 3370 3380 3390 3400
IEENEWMEDK TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI
3410 3420 3430
NQVRSIIGDE KYVDYMSSLK RYEDTTLVED TVL
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 29, 2014
This is version 144 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