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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.4 Publications
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.4 Publications
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.4 Publications
Non-structural protein 1 is involved in virus replication and regulation of the innate immune response By similarity.4 Publications
Non-structural protein 2A may be involved viral RNA replication and capsid assembly Reviewed prediction.4 Publications
Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity.4 Publications
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.4 Publications
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.4 Publications
Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter By similarity.4 Publications
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.4 Publications
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 Publications

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).
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
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 NS3 Reviewed prediction
Sitei123 – 1242Cleavage; by host signal peptidase By similarity
Sitei215 – 2162Cleavage; by host furin Reviewed prediction
Sitei290 – 2912Cleavage; by host signal peptidase Reviewed prediction
Sitei791 – 7922Cleavage; by host signal peptidase Reviewed prediction
Sitei1143 – 11442Cleavage; by host Reviewed prediction
Sitei1374 – 13752Cleavage; by viral protease NS3 Reviewed prediction
Sitei1505 – 15062Cleavage; by autolysis Reviewed prediction
Active sitei1556 – 15561Charge relay system; for serine protease NS3 activity By similarity
Active sitei1580 – 15801Charge relay system; for serine protease NS3 activity By similarity
Active sitei1640 – 16401Charge relay system; for serine protease NS3 activity By similarity
Sitei2124 – 21252Cleavage; by autolysis Reviewed prediction
Sitei2250 – 22512Cleavage; by viral protease NS3 Reviewed prediction
Sitei2273 – 22742Cleavage; by host signal peptidase Reviewed prediction
Sitei2528 – 25292Cleavage; by viral protease NS3 Reviewed prediction
Binding sitei2541 – 25411mRNA cap By similarity
Binding sitei2544 – 25441mRNA cap; via carbonyl oxygen By similarity
Binding sitei2545 – 25451mRNA cap By similarity
Binding sitei2547 – 25471mRNA cap; via carbonyl oxygen By similarity
Sitei2552 – 25521mRNA cap binding By similarity
Binding sitei2556 – 25561mRNA cap By similarity
Binding sitei2584 – 25841S-adenosyl-L-methionine By similarity
Sitei2589 – 25891Essential for 2'-O-methyltransferase activity By similarity
Binding sitei2614 – 26141S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei2615 – 26151S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei2632 – 26321S-adenosyl-L-methionine By similarity
Binding sitei2633 – 26331S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei2659 – 26591S-adenosyl-L-methionine By similarity
Binding sitei2660 – 26601S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Sitei2674 – 26741Essential for 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Sitei2675 – 26751S-adenosyl-L-methionine binding By similarity
Binding sitei2678 – 26781mRNA cap By similarity
Sitei2710 – 27101Essential for 2'-O-methyltransferase activity By similarity
Binding sitei2741 – 27411mRNA cap By similarity
Binding sitei2743 – 27431mRNA cap By similarity
Sitei2746 – 27461Essential for 2'-O-methyltransferase activity By similarity
Binding sitei2748 – 27481S-adenosyl-L-methionine By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1699 – 17068ATP Reviewed prediction

GO - Molecular functioni

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

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 Capsid protein C : Virion Reviewed prediction 1 Publication
Chain Peptide pr : Secreted By similarity 1 Publication
Chain Small envelope protein M : Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity 1 Publication
Chain Envelope protein E : Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity 1 Publication
Chain Non-structural protein 1 : Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity 1 Publication
Chain Non-structural protein 2A : Host endoplasmic reticulum membrane; Multi-pass membrane protein Reviewed prediction 1 Publication
Chain Serine protease subunit NS2B : Host endoplasmic reticulum membrane; Multi-pass membrane protein Reviewed prediction 1 Publication
Chain Serine protease NS3 : Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity
Note: Remains non-covalently associated to NS3 protease By similarity.1 Publication
Chain Non-structural protein 4A : Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity
Note: Located in RE-associated vesicles hosting the replication complex.1 Publication
Chain Non-structural protein 4B : Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity 1 Publication
Chain RNA-directed RNA polymerase NS5 : Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Host nucleus By similarity
Note: Located in RE-associated vesicles hosting the replication complex.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 105104Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei106 – 12621Helical; Reviewed prediction
Add
BLAST
Topological domaini127 – 248122Extracellular Reviewed prediction
Add
BLAST
Transmembranei249 – 26921Helical; Reviewed prediction
Add
BLAST
Topological domaini270 – 2734Cytoplasmic Reviewed prediction
Transmembranei274 – 29017Helical; Reviewed prediction
Add
BLAST
Topological domaini291 – 743453Extracellular Reviewed prediction
Add
BLAST
Intramembranei744 – 76320Helical; Reviewed prediction
Add
BLAST
Topological domaini764 – 7707Extracellular Reviewed prediction
Intramembranei771 – 79121Helical; Reviewed prediction
Add
BLAST
Topological domaini792 – 1142351Extracellular Reviewed prediction
Add
BLAST
Transmembranei1143 – 116321Helical; Reviewed prediction
Add
BLAST
Topological domaini1164 – 121653Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1217 – 123721Helical; Reviewed prediction
Add
BLAST
Topological domaini1238 – 124710Lumenal Reviewed prediction
Transmembranei1248 – 126821Helical; Reviewed prediction
Add
BLAST
Topological domaini1269 – 129628Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1297 – 131721Helical; Reviewed prediction
Add
BLAST
Topological domaini1318 – 134427Lumenal Reviewed prediction
Add
BLAST
Transmembranei1345 – 136521Helical; Reviewed prediction
Add
BLAST
Topological domaini1366 – 137510Cytoplasmic Reviewed prediction
Transmembranei1376 – 139621Helical; Reviewed prediction
Add
BLAST
Topological domaini1397 – 13993Lumenal Reviewed prediction
Transmembranei1400 – 142021Helical; Reviewed prediction
Add
BLAST
Topological domaini1421 – 147757Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1478 – 149821Helical; Reviewed prediction
Add
BLAST
Topological domaini1499 – 2174676Cytoplasmic Reviewed prediction
Add
BLAST
Topological domaini2196 – 22005Lumenal Reviewed prediction
Intramembranei2201 – 222121Helical; Reviewed prediction
Add
BLAST
Topological domaini2222 – 22221Lumenal Reviewed prediction
Topological domaini2244 – 225815Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2259 – 227921Helical; Note=Signal for NS4B; Reviewed prediction
Add
BLAST
Topological domaini2280 – 231233Lumenal Reviewed prediction
Add
BLAST
Intramembranei2313 – 233321Helical; Reviewed prediction
Add
BLAST
Topological domaini2334 – 235825Lumenal Reviewed prediction
Add
BLAST
Intramembranei2359 – 237921Helical; Reviewed prediction
Add
BLAST
Topological domaini2380 – 23801Lumenal Reviewed prediction
Transmembranei2381 – 240121Helical; Reviewed prediction
Add
BLAST
Topological domaini2402 – 244443Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2445 – 246521Helical; Reviewed prediction
Add
BLAST
Topological domaini2466 – 24705Lumenal Reviewed prediction
Transmembranei2471 – 249121Helical; Reviewed prediction
Add
BLAST
Topological domaini2492 – 3433942Cytoplasmic Reviewed prediction
Add
BLAST

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
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 – 11Removed Reviewed prediction
Chaini2 – 34333432Genome polyprotein
PRO_0000405136Add
BLAST
Chaini2 – 105104Capsid protein C By similarity
PRO_0000037703Add
BLAST
Propeptidei106 – 12318ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000405137Add
BLAST
Chaini124 – 290167prM By similarity
PRO_0000405138Add
BLAST
Chaini124 – 21592Peptide pr By similarity
PRO_0000037704Add
BLAST
Chaini216 – 29075Small envelope protein M By similarity
PRO_0000037705Add
BLAST
Chaini291 – 791501Envelope protein E By similarity
PRO_0000037706Add
BLAST
Chaini792 – 1143352Non-structural protein 1 By similarity
PRO_0000037707Add
BLAST
Chaini1144 – 1374231Non-structural protein 2A By similarity
PRO_0000037708Add
BLAST
Chaini1375 – 1505131Serine protease subunit NS2B By similarity
PRO_0000037709Add
BLAST
Chaini1506 – 2124619Serine protease NS3 By similarity
PRO_0000037710Add
BLAST
Chaini2125 – 2250126Non-structural protein 4A By similarity
PRO_0000037711Add
BLAST
Peptidei2251 – 227323Peptide 2k By similarity
PRO_0000405139Add
BLAST
Chaini2274 – 2528255Non-structural protein 4B By similarity
PRO_0000037712Add
BLAST
Chaini2529 – 3433905RNA-directed RNA polymerase NS5 By similarity
PRO_0000037713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi293 ↔ 320 By similarity
Disulfide bondi350 ↔ 406 By similarity
Disulfide bondi364 ↔ 395 By similarity
Disulfide bondi382 ↔ 411 By similarity
Disulfide bondi480 ↔ 578 By similarity
Disulfide bondi595 ↔ 626 By similarity
Glycosylationi921 – 9211N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi966 – 9661N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi998 – 9981N-linked (GlcNAc...); by host Reviewed prediction

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.

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.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP14335.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1506 – 1683178Peptidase S7
Add
BLAST
Domaini1686 – 1842157Helicase ATP-binding
Add
BLAST
Domaini1853 – 2018166Helicase C-terminal
Add
BLAST
Domaini2529 – 2794266mRNA cap 0-1 NS5-type MT
Add
BLAST
Domaini3058 – 3210153RdRp catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein C By similarity
Add
BLAST
Regioni388 – 40114Involved in fusion
Add
BLAST
Regioni1428 – 146740Interacts with and activates NS3 protease By similarity
Add
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

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

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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. 1 Publication
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...

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: June 11, 2014
This is version 142 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

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