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Protein

Genome polyprotein

Gene
N/A
Organism
Kunjin virus (strain MRM61C)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Capsid protein C: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.By similarity
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.By similarity
Peptide pr: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Protein prM: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Small envelope protein M: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.By similarity
Envelope protein E: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Non-structural protein 1: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).By similarity
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response (PubMed:15507609, PubMed:18337583). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219).3 Publications
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219).PROSITE-ProRule annotationBy similarity1 Publication
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. NS3 supports the separation of RNA daughter and template strands during viral replication. In addition, NS3 assists the initiation of replication by unwinding the RNA secondary structure in the 3' non-translated region (NTR). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219).PROSITE-ProRule annotation1 Publication
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Induces host ER membrane rearrangements to provide a compartment where viral replication can take part (PubMed:16611922, PubMed:25771497). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219).By similarity3 Publications
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: Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity). 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 (PubMed:15650219). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219).By similarity1 Publication
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). 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 (PubMed:15650160, PubMed:20106931). Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:15650160).By similarity2 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).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.1 Publication
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'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1556Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1580Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1640Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1963Involved in NS3 ATPase and RTPase activities1 Publication1
Sitei1966Involved in NS3 ATPase and RTPase activities1 Publication1
Binding sitei2541mRNA capPROSITE-ProRule annotation1
Binding sitei2544mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2545mRNA capPROSITE-ProRule annotation1
Binding sitei2547mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2552mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2556mRNA capPROSITE-ProRule annotation1
Binding sitei2584S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2589For 2'-O-MTase activityBy similarity1
Sitei2589Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2614S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2615S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2632S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2633S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2659S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2660S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2674For 2'-O-MTase activityBy similarity1
Sitei2674Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2675S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2678mRNA capPROSITE-ProRule annotation1
Active sitei2710For 2'-O-MTase activityBy similarity1
Sitei2710Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2741mRNA capPROSITE-ProRule annotation1
Binding sitei2743mRNA capPROSITE-ProRule annotation1
Active sitei2746For 2'-O-MTase activityBy similarity1
Sitei2746Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2748S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2968Zinc 11 Publication1
Metal bindingi2972Zinc 1; via tele nitrogen1 Publication1
Metal bindingi2977Zinc 11 Publication1
Metal bindingi2980Zinc 11 Publication1
Metal bindingi3245Zinc 2; via tele nitrogen1 Publication1
Metal bindingi3261Zinc 21 Publication1
Metal bindingi3380Zinc 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1699 – 1706ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation 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 STAT1 by virus, Inhibition of host STAT2 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
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPSiS07.003
TCDBi1.G.3.1.7 the viral pore-forming membrane fusion protein-3 (vmfp3) family

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
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15, EC:3.6.4.131 Publication)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
NS5
OrganismiKunjin virus (strain MRM61C)
Taxonomic identifieri11078 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
Virus hostiCiconiiformes [TaxID: 8920]
Culex annulirostris (Common banded mosquito) [TaxID: 162997]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008379 Componenti: Genome
  • UP000138183 Componenti: Genome
  • UP000099558 Componenti: Genome

Subcellular locationi

Capsid protein C :
Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 105CytoplasmicSequence analysisAdd BLAST104
Transmembranei106 – 126HelicalSequence analysisAdd BLAST21
Topological domaini127 – 248ExtracellularSequence analysisAdd BLAST122
Transmembranei249 – 269HelicalSequence analysisAdd BLAST21
Topological domaini270 – 273CytoplasmicSequence analysis4
Transmembranei274 – 290HelicalCuratedAdd BLAST17
Topological domaini291 – 743ExtracellularSequence analysisAdd BLAST453
Transmembranei744 – 764HelicalSequence analysisAdd BLAST21
Topological domaini765 – 770CytoplasmicSequence analysis6
Transmembranei771 – 791HelicalSequence analysisAdd BLAST21
Topological domaini792 – 1216ExtracellularSequence analysisAdd BLAST425
Transmembranei1217 – 1237HelicalSequence analysisAdd BLAST21
Topological domaini1238 – 1247CytoplasmicSequence analysis10
Transmembranei1248 – 1268HelicalSequence analysisAdd BLAST21
Topological domaini1269 – 1288LumenalSequence analysisAdd BLAST20
Transmembranei1289 – 1309HelicalSequence analysisAdd BLAST21
Topological domaini1310 – 1316CytoplasmicSequence analysis7
Transmembranei1317 – 1335HelicalSequence analysisAdd BLAST19
Topological domaini1336 – 1345LumenalSequence analysis10
Transmembranei1346 – 1366HelicalSequence analysisAdd BLAST21
Topological domaini1367 – 1375CytoplasmicSequence analysis9
Transmembranei1376 – 1396HelicalSequence analysisAdd BLAST21
Topological domaini1397 – 1399LumenalSequence analysis3
Transmembranei1400 – 1420HelicalSequence analysisAdd BLAST21
Topological domaini1421 – 1477CytoplasmicSequence analysisAdd BLAST57
Intramembranei1478 – 1498HelicalSequence analysisAdd BLAST21
Topological domaini1499 – 2174CytoplasmicSequence analysisAdd BLAST676
Transmembranei2175 – 2195HelicalSequence analysisAdd BLAST21
Topological domaini2196 – 2200LumenalSequence analysis5
Intramembranei2201 – 2221HelicalSequence analysisAdd BLAST21
Topological domaini2222LumenalSequence analysis1
Transmembranei2223 – 2243HelicalSequence analysisAdd BLAST21
Topological domaini2244 – 2258CytoplasmicSequence analysisAdd BLAST15
Transmembranei2259 – 2273Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2274 – 2312LumenalSequence analysisAdd BLAST39
Intramembranei2313 – 2333HelicalSequence analysisAdd BLAST21
Topological domaini2334 – 2380LumenalSequence analysisAdd BLAST47
Transmembranei2381 – 2401HelicalSequence analysisAdd BLAST21
Topological domaini2402 – 2444CytoplasmicSequence analysisAdd BLAST43
Transmembranei2445 – 2465HelicalSequence analysisAdd BLAST21
Topological domaini2466 – 2470LumenalSequence analysis5
Transmembranei2471 – 2491HelicalSequence analysisAdd BLAST21
Topological domaini2492 – 3433CytoplasmicSequence analysisAdd BLAST942

GO - Cellular componenti

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1173A → P: No effect on viral RNA replication and packaging; drastic increase in IFN-alpha and IFN-beta host cell response. 2 Publications1
Mutagenesisi1244N → D: 28% decrease in viral RNA replication; decreased packaging efficiency. 1 Publication1
Mutagenesisi1292T → P: Restores induction of virus-specific membrane structures; when associated with N-1202. 1 Publication1
Mutagenesisi2137P → A: Complete loss of viral replication. 1 Publication1
Mutagenesisi2172P → A: Reduced membrane proliferation and efficiency of replication; no effect on replication complex formation. 1 Publication1
Mutagenesisi2173D → A: Slightly reduced membrane proliferation and efficiency of replication at early time of infection; no effect on replication complex formation. 1 Publication1
Mutagenesisi2190G → A: Reduced membrane proliferation and efficiency of replication; no effect on replication complex formation. 1 Publication1
Mutagenesisi2244P → A: Complete loss of viral replication. 1 Publication1
Mutagenesisi2245E → A: Complete loss of viral replication. 1 Publication1
Mutagenesisi2246P → A: 20% decrease in viral replication. 1 Publication1
Mutagenesisi2247E → A: Complete loss of viral replication. 1 Publication1
Mutagenesisi2798P → S: 88% decrease in viral RNA replication; decreased packaging efficiency. 1 Publication1
Mutagenesisi3181S → F: Increases STAT1 inhibitory function of NS5. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004051361 – 3433Genome polyproteinAdd BLAST3433
ChainiPRO_00000377031 – 105Capsid protein CBy similarityAdd BLAST105
PropeptideiPRO_0000405137106 – 123ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000405138124 – 290Protein prMBy similarityAdd BLAST167
ChainiPRO_0000037704124 – 215Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037705216 – 290Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037706291 – 791Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000037707792 – 1143Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000377081144 – 1374Non-structural protein 2ABy similarityAdd BLAST231
ChainiPRO_00000377091375 – 1505Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000377101506 – 2124Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00000377112125 – 2250Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051392251 – 2273Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000377122274 – 2528Non-structural protein 4BBy similarityAdd BLAST255
ChainiPRO_00000377132529 – 3433RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...) asparagine; by host1 Publication1
Disulfide bondi293 ↔ 320By similarity
Disulfide bondi350 ↔ 411By similarity
Disulfide bondi350 ↔ 406By similarity
Disulfide bondi364 ↔ 395By similarity
Disulfide bondi382 ↔ 411By similarity
Disulfide bondi382 ↔ 406By similarity
Disulfide bondi480 ↔ 578By similarity
Disulfide bondi595 ↔ 626By similarity
Disulfide bondi795 ↔ 806By similarity
Disulfide bondi846 ↔ 934By similarity
Glycosylationi921N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi966N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi970 ↔ 1014By similarity
Glycosylationi998N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1071 ↔ 1120By similarity
Disulfide bondi1082 ↔ 1103By similarity
Disulfide bondi1104 ↔ 1107By similarity
Modified residuei2584PhosphoserineBy similarity1

Post-translational modificationi

Genome polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Protein prM: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
Envelope protein E: N-glycosylated.1 Publication
Non-structural protein 1: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei105 – 106Cleavage; by viral protease NS3By similarity2
Sitei123 – 124Cleavage; by host signal peptidaseBy similarity2
Sitei215 – 216Cleavage; by host furinBy similarity2
Sitei290 – 291Cleavage; by host signal peptidaseBy similarity2
Sitei791 – 792Cleavage; by host signal peptidaseBy similarity2
Sitei1143 – 1144Cleavage; by hostBy similarity2
Sitei1374 – 1375Cleavage; by viral protease NS3Sequence analysisBy similarity2
Sitei1505 – 1506Cleavage; by autolysisBy similarity2
Sitei2124 – 2125Cleavage; by autolysisBy similarity2
Sitei2250 – 2251Cleavage; by viral protease NS3By similarity2
Sitei2273 – 2274Cleavage; by host signal peptidaseBy similarity2
Sitei2528 – 2529Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PeptideAtlasiP14335
PRIDEiP14335

Interactioni

Subunit structurei

Capsid protein C: Homodimer; further assembles as a homotetramer (PubMed:15242592). Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity). Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (By similarity). Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi (By similarity). Non-structural protein 1: Homodimer; Homohexamer when secreted (By similarity). NS1 interacts with NS4B (By similarity). Interacts with host complement protein CFH; this interaction leads to the degradation of C3 (By similarity). Non-structural protein 2A: Interacts (via N-terminus) with serine protease NS3 (By similarity). Non-structural protein 2B: Forms a heterodimer with serine protease NS3 (By similarity). May form homooligomers (By similarity). Serine protease NS3: Forms a heterodimer with NS2B (By similarity). Interacts with NS4B (By similarity). Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). Serine protease NS3: Forms a heterodimer with NS2B (By similarity). Interacts with NS4B (By similarity). Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). Non-structural protein 4B: Interacts with serine protease NS3 (By similarity). Interacts with NS1 (By similarity). RNA-directed RNA polymerase NS5: Homodimer (By similarity). Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP14335, 37 interactors

Structurei

Secondary structure

13433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP14335
SMRiP14335
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14335

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1506 – 1683Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1686 – 1842Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1853 – 2018Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2529 – 2794mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3058 – 3210RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni388 – 401Fusion peptideBy similarityAdd BLAST14
Regioni1428 – 1467Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1690 – 1693Important for RNA-bindingBy similarity4
Regioni2169 – 2173Regulates the ATPase activity of NS3 helicaseBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1790 – 1793DEAH boxPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi281 – 284Poly-Leu4
Compositional biasi2678 – 2681Poly-Ser4

Domaini

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.By similarity

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG090001DL

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR000208 RNA-dir_pol_flavivirus
IPR007094 RNA-dir_pol_PSvirus
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
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
PF00949 Peptidase_S7, 1 hit
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF101257 SSF101257, 1 hit
SSF50494 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
PROSITEiView protein in PROSITE
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

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)DescriptionActionsGraphical viewLength
Natural varianti150P → T in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti820I → M in strain: Infectious clone pAKUNa and Infectious clone FLSDX. 1
Natural varianti943N → S in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti1041P → L in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti1202I → N in strain: Infectious clone pAKUN; blocks induction of virus-specific membrane structures. 1 Publication1
Natural varianti1318R → K in strain: Infectious clone pAKUN. 1
Natural varianti1967T → I in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti1974A → V in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti2023Y → H in strain: Infectious clone pAKUN. 1
Natural varianti2062S → P in strain: Infectious clone pAKUN. 1
Natural varianti2339T → N in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00246 Genomic RNA Translation: BAA00176.1
AY274504 Genomic RNA Translation: AAP78941.1
AY274505 Genomic RNA Translation: AAP78942.1
PIRiA28697 GNWVKV

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00246 Genomic RNA Translation: BAA00176.1
AY274504 Genomic RNA Translation: AAP78941.1
AY274505 Genomic RNA Translation: AAP78942.1
PIRiA28697 GNWVKV

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP14335, 37 interactors

Protein family/group databases

MEROPSiS07.003
TCDBi1.G.3.1.7 the viral pore-forming membrane fusion protein-3 (vmfp3) family

Proteomic databases

PeptideAtlasiP14335
PRIDEiP14335

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG090001DL

Miscellaneous databases

EvolutionaryTraceiP14335

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR000208 RNA-dir_pol_flavivirus
IPR007094 RNA-dir_pol_PSvirus
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
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
PF00949 Peptidase_S7, 1 hit
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF101257 SSF101257, 1 hit
SSF50494 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
PROSITEiView protein in PROSITE
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
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_KUNJM
AccessioniPrimary (citable) accession number: P14335
Secondary accession number(s): Q7T4P4, Q7T4P5, Q82983
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 20, 2018
This is version 170 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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