Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 4 (strain Dominica/814669/1981) (DENV-4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA.By similarity
prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated.By similarity
Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes.By similarity
Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome.By similarity
Non-structural protein 2A may be involved viral RNA replication and capsid assembly.Curated
Non-structural protein 2B is a required cofactor for the serine protease function of NS3.PROSITE-ProRule annotation
Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).PROSITE-ProRule annotation
Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase.By similarity
Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.By similarity
RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).PROSITE-ProRule annotation

Catalytic activityi

Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1525 – 15251Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1549 – 15491Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1609 – 16091Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Binding sitei2501 – 25011mRNA capPROSITE-ProRule annotation
Binding sitei2504 – 25041mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2505 – 25051mRNA capPROSITE-ProRule annotation
Binding sitei2507 – 25071mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2512 – 25121mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2516 – 25161mRNA capPROSITE-ProRule annotation
Binding sitei2543 – 25431S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2548 – 25481Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2573 – 25731S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2574 – 25741S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2591 – 25911S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2592 – 25921S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2618 – 26181S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2619 – 26191S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2633 – 26331Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2634 – 26341S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2637 – 26371mRNA capPROSITE-ProRule annotation
Sitei2668 – 26681Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2699 – 26991mRNA capPROSITE-ProRule annotation
Binding sitei2701 – 27011mRNA capPROSITE-ProRule annotation
Sitei2704 – 27041Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2706 – 27061S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1667 – 16748ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase

Keywords - Biological processi

Activation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host 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

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 14 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Non-structural protein 2A-alpha
Short name:
NS2A-alpha
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Alternative name(s):
Non-structural protein 5
OrganismiDengue virus type 4 (strain Dominica/814669/1981) (DENV-4)
Taxonomic identifieri408871 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000000274 Componenti: Genome

Subcellular locationi

Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A-alpha :
Non-structural protein 2A :
Serine protease subunit NS2B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
Serine protease NS3 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation

  • Note: Remains non-covalently associated to NS3 protease.PROSITE-ProRule annotation
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Host nucleus By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 100100CytoplasmicSequence analysisAdd
BLAST
Transmembranei101 – 11717HelicalSequence analysisAdd
BLAST
Topological domaini118 – 237120ExtracellularSequence analysisAdd
BLAST
Transmembranei238 – 25821HelicalSequence analysisAdd
BLAST
Topological domaini259 – 2657CytoplasmicSequence analysis
Transmembranei266 – 27914HelicalSequence analysisAdd
BLAST
Topological domaini280 – 725446ExtracellularSequence analysisAdd
BLAST
Intramembranei726 – 74621HelicalSequence analysisAdd
BLAST
Topological domaini747 – 7515ExtracellularSequence analysis
Intramembranei752 – 77221HelicalSequence analysisAdd
BLAST
Topological domaini773 – 1156384ExtracellularSequence analysisAdd
BLAST
Transmembranei1157 – 117721HelicalSequence analysisAdd
BLAST
Topological domaini1178 – 119720CytoplasmicSequence analysisAdd
BLAST
Transmembranei1198 – 121821HelicalSequence analysisAdd
BLAST
Topological domaini1219 – 124426LumenalSequence analysisAdd
BLAST
Transmembranei1245 – 126521HelicalSequence analysisAdd
BLAST
Topological domaini1266 – 128520CytoplasmicSequence analysisAdd
BLAST
Transmembranei1286 – 130621HelicalSequence analysisAdd
BLAST
Topological domaini1307 – 131610LumenalSequence analysis
Transmembranei1317 – 133721HelicalSequence analysisAdd
BLAST
Topological domaini1338 – 13458CytoplasmicSequence analysis
Transmembranei1346 – 136621HelicalSequence analysisAdd
BLAST
Topological domaini1367 – 13693LumenalSequence analysis
Transmembranei1370 – 139021HelicalSequence analysisAdd
BLAST
Topological domaini1391 – 143747CytoplasmicSequence analysisAdd
BLAST
Intramembranei1438 – 145821HelicalSequence analysisAdd
BLAST
Topological domaini1459 – 2143685CytoplasmicSequence analysisAdd
BLAST
Transmembranei2144 – 216421HelicalSequence analysisAdd
BLAST
Topological domaini2165 – 21695LumenalSequence analysis
Intramembranei2170 – 219021HelicalSequence analysisAdd
BLAST
Topological domaini2191 – 21911LumenalSequence analysis
Transmembranei2192 – 221221HelicalSequence analysisAdd
BLAST
Topological domaini2213 – 222513CytoplasmicSequence analysisAdd
BLAST
Transmembranei2226 – 224621Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2247 – 227327LumenalSequence analysisAdd
BLAST
Intramembranei2274 – 229118HelicalSequence analysisAdd
BLAST
Topological domaini2292 – 230110LumenalSequence analysis
Intramembranei2302 – 232221HelicalSequence analysisAdd
BLAST
Topological domaini2323 – 234321LumenalSequence analysisAdd
BLAST
Transmembranei2344 – 236421HelicalSequence analysisAdd
BLAST
Topological domaini2365 – 240945CytoplasmicSequence analysisAdd
BLAST
Transmembranei2410 – 243021HelicalSequence analysisAdd
BLAST
Topological domaini2431 – 245525LumenalSequence analysisAdd
BLAST
Transmembranei2456 – 247621HelicalSequence analysisAdd
BLAST
Topological domaini2477 – 3387911CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 33863386Genome polyproteinPRO_0000405226Add
BLAST
Chaini1 – 9999Capsid protein CBy similarityPRO_0000038000Add
BLAST
Propeptidei100 – 11314ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000038001Add
BLAST
Chaini114 – 279166prMBy similarityPRO_0000308297Add
BLAST
Chaini114 – 20491Peptide prBy similarityPRO_0000308298Add
BLAST
Chaini205 – 27975Small envelope protein MBy similarityPRO_0000038002Add
BLAST
Chaini280 – 774495Envelope protein EBy similarityPRO_0000038003Add
BLAST
Chaini775 – 1126352Non-structural protein 1By similarityPRO_0000038004Add
BLAST
Chaini1127 – 1344218Non-structural protein 2ABy similarityPRO_0000038005Add
BLAST
Chaini1127 – ?Non-structural protein 2A-alphaBy similarityPRO_0000308299
Chaini1345 – 1474130Serine protease subunit NS2BBy similarityPRO_0000038006Add
BLAST
Chaini1475 – 2092618Serine protease NS3By similarityPRO_0000038007Add
BLAST
Chaini2093 – 2219127Non-structural protein 4ABy similarityPRO_0000038008Add
BLAST
Peptidei2220 – 224223Peptide 2kBy similarityPRO_0000308300Add
BLAST
Chaini2243 – 2487245Non-structural protein 4BBy similarityPRO_0000038009Add
BLAST
Chaini2488 – 3387900RNA-directed RNA polymerase NS5By similarityPRO_0000038010Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi182 – 1821N-linked (GlcNAc...); by host
Disulfide bondi282 ↔ 309By similarity
Disulfide bondi339 ↔ 400By similarity
Glycosylationi346 – 3461N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi353 ↔ 384By similarity
Disulfide bondi371 ↔ 395By similarity
Glycosylationi432 – 4321N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi464 ↔ 564By similarity
Disulfide bondi581 ↔ 612By similarity
Glycosylationi904 – 9041N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi981 – 9811N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2297 – 22971N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2301 – 23011N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2453 – 24531N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

Specific enzymatic cleavages in vivo 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 protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. 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
Envelope protein E and non-structural protein 1 are N-glycosylated.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei99 – 1002Cleavage; by viral protease NS3Sequence analysis
Sitei113 – 1142Cleavage; by host signal peptidaseBy similarity
Sitei204 – 2052Cleavage; by host furinSequence analysis
Sitei279 – 2802Cleavage; by host signal peptidaseSequence analysis
Sitei774 – 7752Cleavage; by host signal peptidaseSequence analysis
Sitei1126 – 11272Cleavage; by hostBy similarity
Sitei1344 – 13452Cleavage; by viral protease NS3Sequence analysis
Sitei1474 – 14752Cleavage; by autolysisSequence analysis
Sitei2092 – 20932Cleavage; by autolysisSequence analysis
Sitei2219 – 22202Cleavage; by viral protease NS3Sequence analysis
Sitei2242 – 22432Cleavage; by host signal peptidaseSequence analysis
Sitei2487 – 24882Cleavage; by viral protease NS3Sequence analysis

Keywords - PTMi

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

Interactioni

Subunit structurei

Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity. NS5 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

Protein-protein interaction databases

MINTiMINT-8373716.

Structurei

Secondary structure

1
3387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi283 – 2864Combined sources
Turni292 – 2943Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi300 – 3067Combined sources
Beta strandi309 – 3146Combined sources
Beta strandi317 – 32711Combined sources
Beta strandi333 – 35119Combined sources
Helixi362 – 3643Combined sources
Beta strandi369 – 37911Combined sources
Turni380 – 3834Combined sources
Beta strandi388 – 40821Combined sources
Beta strandi411 – 4133Combined sources
Beta strandi416 – 4227Combined sources
Beta strandi439 – 4435Combined sources
Beta strandi449 – 4546Combined sources
Turni455 – 4573Combined sources
Beta strandi458 – 4658Combined sources
Helixi472 – 4743Combined sources
Beta strandi475 – 4806Combined sources
Beta strandi483 – 4886Combined sources
Helixi489 – 4935Combined sources
Helixi513 – 5153Combined sources
Beta strandi517 – 5193Combined sources
Beta strandi529 – 5313Combined sources
Helixi536 – 5427Combined sources
Beta strandi544 – 5463Combined sources
Beta strandi548 – 5503Combined sources
Beta strandi552 – 5543Combined sources
Beta strandi560 – 5678Combined sources
Beta strandi570 – 5723Combined sources
Turni574 – 5774Combined sources
Beta strandi585 – 5939Combined sources
Beta strandi595 – 5973Combined sources
Beta strandi599 – 6057Combined sources
Beta strandi607 – 6093Combined sources
Beta strandi611 – 6133Combined sources
Beta strandi616 – 6194Combined sources
Beta strandi621 – 6233Combined sources
Beta strandi632 – 6343Combined sources
Beta strandi636 – 6394Combined sources
Beta strandi643 – 6486Combined sources
Beta strandi652 – 66110Combined sources
Helixi662 – 6643Combined sources
Beta strandi666 – 6727Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0PNMR-A568-679[»]
3UAJX-ray3.23A/B280-674[»]
3UC0X-ray2.71A/B280-329[»]
A/B414-469[»]
A/B560-577[»]
3WE1X-ray2.28A/B575-679[»]
4X42X-ray2.78A/B/C/D/E/F575-679[»]
5B1CX-ray2.00A/B/C575-679[»]
ProteinModelPortaliP09866.
SMRiP09866. Positions 20-99, 114-194, 280-679, 1493-2092, 2494-2755, 2761-3371.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09866.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1475 – 1652178Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1654 – 1810157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1820 – 1987168Helicase C-terminalAdd
BLAST
Domaini2489 – 2751263mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3016 – 3166151RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 7342Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni1397 – 143640Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1758 – 17614DEAH box

Domaini

Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals.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
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.Curated
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

CDDicd12149. Flavi_E_C. 1 hit.
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.
IPR027287. Flavi_E_Ig-like.
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.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR026490. mRNA_cap_0/1_MeTrfase.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
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.

P09866-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI
60 70 80 90 100
TFLRVLSIPP TAGILKRWGQ LKKNKAIKIL IGFRKEIGRM LNILNGRKRS
110 120 130 140 150
TITLLCLIPT VMAFSLSTRD GEPLMIVAKH ERGRPLLFKT TEGINKCTLI
160 170 180 190 200
AMDLGEMCED TVTYKCPLLV NTEPEDIDCW CNLTSTWVMY GTCTQSGERR
210 220 230 240 250
REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI LRNPGFALLA
260 270 280 290 300
GFMAYMIGQT GIQRTVFFVL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV
310 320 330 340 350
DLVLEHGGCV TTMAQGKPTL DFELTKTTAK EVALLRTYCI EASISNITTA
360 370 380 390 400
TRCPTQGEPY LKEEQDQQYI CRRDVVDRGW GNGCGLFGKG GVVTCAKFSC
410 420 430 440 450
SGKITGNLVQ IENLEYTVVV TVHNGDTHAV GNDTSNHGVT AMITPRSPSV
460 470 480 490 500
EVKLPDYGEL TLDCEPRSGI DFNEMILMKM KKKTWLVHKQ WFLDLPLPWT
510 520 530 540 550
AGADTSEVHW NYKERMVTFK VPHAKRQDVT VLGSQEGAMH SALAGATEVD
560 570 580 590 600
SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV
610 620 630 640 650
VKVKYEGAGA PCKVPIEIRD VNKEKVVGRI ISSTPLAENT NSVTNIELEP
660 670 680 690 700
PFGDSYIVIG VGNSALTLHW FRKGSSIGKM FESTYRGAKR MAILGETAWD
710 720 730 740 750
FGSVGGLFTS LGKAVHQVFG SVYTTMFGGV SWMIRILIGF LVLWIGTNSR
760 770 780 790 800
NTSMAMTCIA VGGITLFLGF TVQADMGCVA SWSGKELKCG SGIFVVDNVH
810 820 830 840 850
TWTEQYKFQP ESPARLASAI LNAHKDGVCG IRSTTRLENV MWKQITNELN
860 870 880 890 900
YVLWEGGHDL TVVAGDVKGV LTKGKRALTP PVSDLKYSWK TWGKAKIFTP
910 920 930 940 950
EARNSTFLID GPDTSECPNE RRAWNSLEVE DYGFGMFTTN IWMKFREGSS
960 970 980 990 1000
EVCDHRLMSA AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP
1010 1020 1030 1040 1050
KTHTLWSNGV LESQMLIPKS YAGPFSQHNY RQGYATQTVG PWHLGKLEID
1060 1070 1080 1090 1100
FGECPGTTVT IQEDCDHRGP SLRTTTASGK LVTQWCCRSC TMPPLRFLGE
1110 1120 1130 1140 1150
DGCWYGMEIR PLSEKEENMV KSQVTAGQGT SETFSMGLLC LTLFVEECLR
1160 1170 1180 1190 1200
RRVTRKHMIL VVVITLCAII LGGLTWMDLL RALIMLGDTM SGRIGGQIHL
1210 1220 1230 1240 1250
AIMAVFKMSP GYVLGVFLRK LTSRETALMV IGMAMTTVLS IPHDLMELID
1260 1270 1280 1290 1300
GISLGLILLK IVTQFDNTQV GTLALSLTFI RSTMPLVMAW RTIMAVLFVV
1310 1320 1330 1340 1350
TLIPLCRTSC LQKQSHWVEI TALILGAQAL PVYLMTLMKG ASRRSWPLNE
1360 1370 1380 1390 1400
GIMAVGLVSL LGSALLKNDV PLAGPMVAGG LLLAAYVMSG SSADLSLEKA
1410 1420 1430 1440 1450
ANVQWDEMAD ITGSSPIIEV KQDEDGSFSI RDVEETNMIT LLVKLALITV
1460 1470 1480 1490 1500
SGLYPLAIPV TMTLWYMWQV KTQRSGALWD VPSPAATKKA ALSEGVYRIM
1510 1520 1530 1540 1550
QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHETGRLE PSWADVRNDM
1560 1570 1580 1590 1600
ISYGGGWRLG DKWDKEEDVQ VLAIEPGKNP KHVQTKPGLF KTLTGEIGAV
1610 1620 1630 1640 1650
TLDFKPGTSG SPIINRKGKV IGLYGNGVVT KSGDYVSAIT QAERIGEPDY
1660 1670 1680 1690 1700
EVDEDIFRKK RLTIMDLHPG AGKTKRILPS IVREALKRRL RTLILAPTRV
1710 1720 1730 1740 1750
VAAEMEEALR GLPIRYQTPA VKSEHTGREI VDLMCHATFT TRLLSSTRVP
1760 1770 1780 1790 1800
NYNLIVMDEA HFTDPSSVAA RGYISTRVEM GEAAAIFMTA TPPGATDPFP
1810 1820 1830 1840 1850
QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR
1860 1870 1880 1890 1900
KSGKKVIQLS RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR
1910 1920 1930 1940 1950
RCLKPVILPD GPERVILAGP IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG
1960 1970 1980 1990 2000
DPLKNDEDHA HWTEAKMLLD NIYTPEGIIP TLFGPEREKT QAIDGEFRLR
2010 2020 2030 2040 2050
GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG ERNNQILEEN
2060 2070 2080 2090 2100
MEVEIWTREG EKKKLRPRWL DARVYADPMA LKDFKEFASG RKSITLDILT
2110 2120 2130 2140 2150
EIASLPTYLS SRAKLALDNI VMLHTTERGG RAYQHALNEL PESLETLMLV
2160 2170 2180 2190 2200
ALLGAMTAGI FLFFMQGKGI GKLSMGLITI AVASGLLWVA EIQPQWIAAS
2210 2220 2230 2240 2250
IILEFFLMVL LIPEPEKQRT PQDNQLIYVI LTILTIIGLI AANEMGLIEK
2260 2270 2280 2290 2300
TKTDFGFYQV KTETTILDVD LRPASAWTLY AVATTILTPM LRHTIENTSA
2310 2320 2330 2340 2350
NLSLAAIANQ AAVLMGLGKG WPLHRMDLGV PLLAMGCYSQ VNPTTLTASL
2360 2370 2380 2390 2400
VMLLVHYAII GPGLQAKATR EAQKRTAAGI MKNPTVDGIT VIDLEPISYD
2410 2420 2430 2440 2450
PKFEKQLGQV MLLVLCAGQL LLMRTTWAFC EVLTLATGPI LTLWEGNPGR
2460 2470 2480 2490 2500
FWNTTIAVST ANIFRGSYLA GAGLAFSLIK NAQTPRRGTG TTGETLGEKW
2510 2520 2530 2540 2550
KRQLNSLDRK EFEEYKRSGI LEVDRTEAKS ALKDGSKIKH AVSRGSSKIR
2560 2570 2580 2590 2600
WIVERGMVKP KGKVVDLGCG RGGWSYYMAT LKNVTEVKGY TKGGPGHEEP
2610 2620 2630 2640 2650
IPMATYGWNL VKLHSGVDVF YKPTEQVDTL LCDIGESSSN PTIEEGRTLR
2660 2670 2680 2690 2700
VLKMVEPWLS SKPEFCIKVL NPYMPTVIEE LEKLQRKHGG NLVRCPLSRN
2710 2720 2730 2740 2750
STHEMYWVSG ASGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDVDLGAGTR
2760 2770 2780 2790 2800
SVSTETEKPD MTIIGRRLQR LQEEHKETWH YDQENPYRTW AYHGSYEAPS
2810 2820 2830 2840 2850
TGSASSMVNG VVKLLTKPWD VIPMVTQLAM TDTTPFGQQR VFKEKVDTRT
2860 2870 2880 2890 2900
PQPKPGTRMV MTTTANWLWA LLGKKKNPRL CTREEFISKV RSNAAIGAVF
2910 2920 2930 2940 2950
QEEQGWTSAS EAVNDSRFWE LVDKERALHQ EGKCESCVYN MMGKREKKLG
2960 2970 2980 2990 3000
EFGRAKGSRA IWYMWLGARF LEFEALGFLN EDHWFGRENS WSGVEGEGLH
3010 3020 3030 3040 3050
RLGYILEEID KKDGDLMYAD DTAGWDTRIT EDDLQNEELI TEQMAPHHKI
3060 3070 3080 3090 3100
LAKAIFKLTY QNKVVKVLRP TPRGAVMDII SRKDQRGSGQ VGTYGLNTFT
3110 3120 3130 3140 3150
NMEVQLIRQM EAEGVITQDD MQNPKGLKER VEKWLKECGV DRLKRMAISG
3160 3170 3180 3190 3200
DDCVVKPLDE RFGTSLLFLN DMGKVRKDIP QWEPSKGWKN WQEVPFCSHH
3210 3220 3230 3240 3250
FHKIFMKDGR SLVVPCRNQD ELIGRARISQ GAGWSLRETA CLGKAYAQMW
3260 3270 3280 3290 3300
SLMYFHRRDL RLASMAICSA VPTEWFPTSR TTWSIHAHHQ WMTTEDMLKV
3310 3320 3330 3340 3350
WNRVWIEDNP NMTDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN
3360 3370 3380
IHTAITQVRN LIGKEEYVDY MPVMKRYSAP SESEGVL
Length:3,387
Mass (Da):378,385
Last modified:January 16, 2004 - v2
Checksum:i0CE81B6E7DEFDB5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti780 – 7801A → V in AAG45436 (Ref. 2) Curated
Sequence conflicti780 – 7801A → V in AAK01233 (Ref. 2) Curated
Sequence conflicti1418 – 14181I → V in AAG45435 (Ref. 2) Curated
Sequence conflicti1909 – 19091P → T in AAK01233 (Ref. 2) Curated
Sequence conflicti2032 – 20321K → E in AAG45435 (Ref. 2) Curated
Sequence conflicti2351 – 23511V → A in AAG45436 (Ref. 2) Curated
Sequence conflicti2354 – 23541L → F in AAG45437 (Ref. 2) Curated
Sequence conflicti2510 – 25101K → R in AAK01233 (Ref. 2) Curated
Sequence conflicti2736 – 27361K → R in AAG45436 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14931 Genomic RNA. Translation: AAA42964.2.
AF326825 Genomic RNA. Translation: AAG45435.1.
AF326826 Genomic RNA. Translation: AAG45436.1.
AF326827 Genomic RNA. Translation: AAG45437.1.
AF326573 Genomic RNA. Translation: AAK01233.1.
RefSeqiNP_073286.1. NC_002640.1.

Genome annotation databases

GeneIDi5075729.
KEGGivg:5075729.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14931 Genomic RNA. Translation: AAA42964.2.
AF326825 Genomic RNA. Translation: AAG45435.1.
AF326826 Genomic RNA. Translation: AAG45436.1.
AF326827 Genomic RNA. Translation: AAG45437.1.
AF326573 Genomic RNA. Translation: AAK01233.1.
RefSeqiNP_073286.1. NC_002640.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0PNMR-A568-679[»]
3UAJX-ray3.23A/B280-674[»]
3UC0X-ray2.71A/B280-329[»]
A/B414-469[»]
A/B560-577[»]
3WE1X-ray2.28A/B575-679[»]
4X42X-ray2.78A/B/C/D/E/F575-679[»]
5B1CX-ray2.00A/B/C575-679[»]
ProteinModelPortaliP09866.
SMRiP09866. Positions 20-99, 114-194, 280-679, 1493-2092, 2494-2755, 2761-3371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8373716.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5075729.
KEGGivg:5075729.

Miscellaneous databases

EvolutionaryTraceiP09866.
PROiP09866.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
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.
IPR027287. Flavi_E_Ig-like.
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.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR026490. mRNA_cap_0/1_MeTrfase.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_DEN4D
AccessioniPrimary (citable) accession number: P09866
Secondary accession number(s): Q88661
, Q88662, Q88663, Q88664, Q88665, Q88666, Q88667, Q88668, Q88669, Q88670, Q88671, Q99BK4, Q9DKQ5, Q9DKQ6, Q9DKQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 16, 2004
Last modified: September 7, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.