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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 2 (strain Jamaica/1409/1983) (DENV-2)
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 sitei1526 – 15261Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1550 – 15501Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1610 – 16101Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Binding sitei2505 – 25051mRNA capPROSITE-ProRule annotation
Binding sitei2508 – 25081mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2509 – 25091mRNA capPROSITE-ProRule annotation
Binding sitei2511 – 25111mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2516 – 25161mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2520 – 25201mRNA capPROSITE-ProRule annotation
Binding sitei2547 – 25471S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2552 – 25521Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2577 – 25771S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2578 – 25781S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2595 – 25951S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2596 – 25961S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2622 – 26221S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2623 – 26231S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2637 – 26371Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2638 – 26381S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2641 – 26411mRNA capPROSITE-ProRule annotation
Sitei2672 – 26721Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2703 – 27031mRNA capPROSITE-ProRule annotation
Binding sitei2705 – 27051mRNA capPROSITE-ProRule annotation
Sitei2708 – 27081Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2710 – 27101S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1668 – 16758ATPPROSITE-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

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.

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 2 (strain Jamaica/1409/1983) (DENV-2)
Taxonomic identifieri11064 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostiAedimorphus [TaxID: 53540]
Diceromyia [TaxID: 53539]
Erythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
Stegomyia [TaxID: 53541]
Proteomesi
  • UP000002475 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 – 101101CytoplasmicSequence analysisAdd
BLAST
Transmembranei102 – 11918HelicalSequence analysisAdd
BLAST
Topological domaini120 – 241122ExtracellularSequence analysisAdd
BLAST
Transmembranei242 – 25918HelicalSequence analysisAdd
BLAST
Topological domaini260 – 2656CytoplasmicSequence analysis
Transmembranei266 – 28015HelicalSequence analysisAdd
BLAST
Topological domaini281 – 725445ExtracellularSequence analysisAdd
BLAST
Intramembranei726 – 74621HelicalSequence analysisAdd
BLAST
Topological domaini747 – 7526ExtracellularSequence analysis
Intramembranei753 – 77321HelicalSequence analysisAdd
BLAST
Topological domaini774 – 1124351ExtracellularSequence analysisAdd
BLAST
Transmembranei1125 – 114521HelicalSequence analysisAdd
BLAST
Topological domaini1146 – 115611CytoplasmicSequence analysisAdd
BLAST
Transmembranei1157 – 117721HelicalSequence analysisAdd
BLAST
Topological domaini1178 – 11847LumenalSequence analysis
Transmembranei1185 – 120521HelicalSequence analysisAdd
BLAST
Topological domaini1206 – 127166CytoplasmicSequence analysisAdd
BLAST
Transmembranei1272 – 129221HelicalSequence analysisAdd
BLAST
Topological domaini1293 – 131725LumenalSequence analysisAdd
BLAST
Transmembranei1318 – 133821HelicalSequence analysisAdd
BLAST
Topological domaini1339 – 13468CytoplasmicSequence analysis
Transmembranei1347 – 136721HelicalSequence analysisAdd
BLAST
Topological domaini1368 – 13703LumenalSequence analysis
Transmembranei1371 – 139121HelicalSequence analysisAdd
BLAST
Topological domaini1392 – 144756CytoplasmicSequence analysisAdd
BLAST
Intramembranei1448 – 146821HelicalSequence analysisAdd
BLAST
Topological domaini1469 – 2147679CytoplasmicSequence analysisAdd
BLAST
Transmembranei2148 – 216821HelicalSequence analysisAdd
BLAST
Topological domaini2169 – 21702LumenalSequence analysis
Intramembranei2171 – 219121HelicalSequence analysisAdd
BLAST
Topological domaini2192 – 21921LumenalSequence analysis
Transmembranei2193 – 221321HelicalSequence analysisAdd
BLAST
Topological domaini2214 – 222815CytoplasmicSequence analysisAdd
BLAST
Transmembranei2229 – 224921Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2250 – 227728LumenalSequence analysisAdd
BLAST
Intramembranei2278 – 229518HelicalSequence analysisAdd
BLAST
Topological domaini2296 – 231621LumenalSequence analysisAdd
BLAST
Intramembranei2317 – 233721HelicalSequence analysisAdd
BLAST
Topological domaini2338 – 234710LumenalSequence analysis
Transmembranei2348 – 236821HelicalSequence analysisAdd
BLAST
Topological domaini2369 – 241345CytoplasmicSequence analysisAdd
BLAST
Transmembranei2414 – 243421HelicalSequence analysisAdd
BLAST
Topological domaini2435 – 245925LumenalSequence analysisAdd
BLAST
Transmembranei2460 – 248021HelicalSequence analysisAdd
BLAST
Topological domaini2481 – 3391911CytoplasmicSequence 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 – 33913391Genome polyproteinPRO_0000405215Add
BLAST
Chaini1 – 100100Capsid protein CBy similarityPRO_0000037947Add
BLAST
Propeptidei101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000037948Add
BLAST
Chaini115 – 280166prMBy similarityPRO_0000308282Add
BLAST
Chaini115 – 20591Peptide prBy similarityPRO_0000308283Add
BLAST
Chaini206 – 28075Small envelope protein MBy similarityPRO_0000037949Add
BLAST
Chaini281 – 775495Envelope protein EBy similarityPRO_0000037950Add
BLAST
Chaini776 – 1127352Non-structural protein 1By similarityPRO_0000037951Add
BLAST
Chaini1128 – 1345218Non-structural protein 2ABy similarityPRO_0000037952Add
BLAST
Chaini1128 – 1315188Non-structural protein 2A-alphaBy similarityPRO_0000308284Add
BLAST
Chaini1346 – 1475130Serine protease subunit NS2BBy similarityPRO_0000037953Add
BLAST
Chaini1476 – 2093618Serine protease NS3By similarityPRO_0000037954Add
BLAST
Chaini2094 – 2220127Non-structural protein 4ABy similarityPRO_0000037955Add
BLAST
Peptidei2221 – 224323Peptide 2kBy similarityPRO_0000308285Add
BLAST
Chaini2244 – 2491248Non-structural protein 4BBy similarityPRO_0000037956Add
BLAST
Chaini2492 – 3391900RNA-directed RNA polymerase NS5By similarityPRO_0000037957Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Glycosylationi347 – 3471N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 396By similarity
Glycosylationi433 – 4331N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi465 ↔ 565By similarity
Disulfide bondi582 ↔ 613By similarity
Glycosylationi905 – 9051N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi982 – 9821N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2301 – 23011N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2305 – 23051N-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
Sitei100 – 1012Cleavage; by viral protease NS3Sequence analysis
Sitei114 – 1152Cleavage; by host signal peptidaseBy similarity
Sitei205 – 2062Cleavage; by host furinSequence analysis
Sitei280 – 2812Cleavage; by host signal peptidaseSequence analysis
Sitei775 – 7762Cleavage; by host signal peptidaseSequence analysis
Sitei1127 – 11282Cleavage; by hostBy similarity
Sitei1345 – 13462Cleavage; by viral protease NS3Sequence analysis
Sitei1475 – 14762Cleavage; by autolysisSequence analysis
Sitei2093 – 20942Cleavage; by autolysisSequence analysis
Sitei2220 – 22212Cleavage; by viral protease NS3Sequence analysis
Sitei2243 – 22442Cleavage; by host signal peptidaseSequence analysis
Sitei2491 – 24922Cleavage; 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

Structurei

Secondary structure

1
3391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi586 – 5883Combined sources
Beta strandi600 – 6067Combined sources
Beta strandi608 – 6103Combined sources
Beta strandi612 – 6143Combined sources
Beta strandi617 – 6204Combined sources
Beta strandi630 – 6356Combined sources
Beta strandi645 – 6506Combined sources
Beta strandi653 – 6619Combined sources
Beta strandi663 – 6653Combined sources
Beta strandi667 – 6737Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UZVX-ray2.10A576-680[»]
ProteinModelPortaliP07564.
SMRiP07564. Positions 21-100, 115-194, 281-674, 1394-1440, 1495-2093, 2498-2759, 2765-3374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1476 – 1653178Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1655 – 1811157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1821 – 1988168Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2493 – 2755263mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3020 – 3169150RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni1398 – 143740Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1759 – 17624DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi97 – 1004Poly-Arg
Compositional biasi1434 – 14374Poly-Glu
Compositional biasi2148 – 21547Poly-Leu
Compositional biasi2354 – 23574Poly-Leu
Compositional biasi3383 – 33864Poly-Glu

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.PROSITE-ProRule annotation
Contains 1 mRNA cap 0-1 NS5-type MT domain.PROSITE-ProRule annotation
Contains 1 peptidase S7 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

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.
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.

P07564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNQRKKARS TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL
60 70 80 90 100
VAFLRFLTIP PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR
110 120 130 140 150
TAGVIIMLIP TAMAFHLTTR NGEPHMIVGR QEKGKSLLFK TEDGVNMCTL
160 170 180 190 200
MAIDLGELCE DTITYKCPLL RQNEPEDIDC WCNSTSTWVT YGTCATTGEH
210 220 230 240 250
RREKRSVALV PHVGMGLETR TETWMSSEGA WKHVQRIETW ILRHPGFTIM
260 270 280 290 300
AAILAYTIGT THFQRALIFI LLTAVAPSMT MRCIGISNRD FVEGVSGGSW
310 320 330 340 350
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT
360 370 380 390 400
ESRCPTQGEP SLNEEQDKRF LCKHSMVDRG WGNGCGLFGK GGIVTCAMFT
410 420 430 440 450
CKKNMEGKVV LPENLEYTIV ITPHSGEEHA VGNDTGKHGK EIKITPQSSI
460 470 480 490 500
TEAELTGYGT VTMECSPRTG LDFNEMVLLQ MEDKAWLVHR QWFLDLPLPW
510 520 530 540 550
LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM HTALTGATEI
560 570 580 590 600
QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKIVK EIAETQHGTI
610 620 630 640 650
VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE
660 670 680 690 700
PPFGDSYIII GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW
710 720 730 740 750
DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS
760 770 780 790 800
RSTSLSVSLV LVGVVTLYLG AMVQADSGCV VSWKNKELKC GSGIFITDNV
810 820 830 840 850
HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN LMWKQITPEL
860 870 880 890 900
NHILSENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS
910 920 930 940 950
TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLREKQ
960 970 980 990 1000
DVFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKMEKA SFIEVKSCHW
1010 1020 1030 1040 1050
PKSHTLWSNG VLESEMIIPK NFAGPVSQHN YRPGYHTQTA GPWHLGKLEM
1060 1070 1080 1090 1100
DFDFCEGTTV VVTEDCGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG
1110 1120 1130 1140 1150
EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QIDNFSLGVL GMALFLEEML
1160 1170 1180 1190 1200
RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT
1210 1220 1230 1240 1250
YLALLAAFKV RPTFAAGLLL RKLTSKELMM ATIGIALLSQ STIPETILEL
1260 1270 1280 1290 1300
TDALALGMMV LKIVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA
1310 1320 1330 1340 1350
AVSVSPLLLT SSQQKADWIP LALTIKGLNP TAIFLTTLSR TSKKRSWPLN
1360 1370 1380 1390 1400
EAIMAVGMVS ILASSLLKND IPMTGPLVAG GLLTVCYVLT GRSADLELER
1410 1420 1430 1440 1450
AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL TILIRTGLLV
1460 1470 1480 1490 1500
ISGVFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPVGK AELEDGAYRI
1510 1520 1530 1540 1550
KQRGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD
1560 1570 1580 1590 1600
LISYGGGWKL EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FKTNTGTIGA
1610 1620 1630 1640 1650
VSLDFSPGTS GSPIVDRKGK VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN
1660 1670 1680 1690 1700
PEIEDDIFRK KRLTIMDLHP GAGKTKRYLP AIVREAIKRG LRTLILAPTR
1710 1720 1730 1740 1750
VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF TMRLLSPVRV
1760 1770 1780 1790 1800
PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
1810 1820 1830 1840 1850
PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL
1860 1870 1880 1890 1900
RKNGKKVIQL SRKTFDSEYV KTRANDWDFV VTTDISEMGA NFKAERVIDP
1910 1920 1930 1940 1950
RRCMKPVILT DGEERVILAG PMPVTHSSAA QRRGRIGRNP KNENDQYIYM
1960 1970 1980 1990 2000
GEPLENDEDC AHWKEAKMLL DNINTPEGII PSMFEPEREK VDAIDGEYRL
2010 2020 2030 2040 2050
RGEARKTFVD LMRRGDLPVW LAYRVAAEGI NYADRRWCFD GIKNNQILEE
2060 2070 2080 2090 2100
NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
2110 2120 2130 2140 2150
TEMGRLPTFM TQKARDALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL
2160 2170 2180 2190 2200
LTLLATVTGG IFLFLMSGKG IGKMTLGMCC IITASILLWY AQIQPHWIAA
2210 2220 2230 2240 2250
SIILEFFLIV LLIPEPEKQR TPQDNQLTYV VIAILTVVAA TMANEMGFLE
2260 2270 2280 2290 2300
KTKKDLGLGS ITTQESESNI LDIDLRPASA WTLYAVATTF VTPMLRHSIE
2310 2320 2330 2340 2350
NSSVNVSLTA IANQATVLMG LGKGWPLSKI HIGVPLLAIG CYSQVNPITL
2360 2370 2380 2390 2400
TAALLLLVAH YAIIGPGLQA KATREAQKRA AAGIMKNPTV DGITVIDLDP
2410 2420 2430 2440 2450
IPYDPKFEKQ LGQVMLLILC VTQVLMMRTT WALCEALTLA TGPISTLWEG
2460 2470 2480 2490 2500
NPGRFWNTTI AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RGTGNIGETL
2510 2520 2530 2540 2550
GEKWKSRLNA LGKSEFQIYK KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS
2560 2570 2580 2590 2600
AKLRWFVERN MVTPEGKVVD LGCGRGGWSY YCGGLKNVRE VKGLTKGGPG
2610 2620 2630 2640 2650
HEEPIPMSTY GWNLVRLQSG VDVFFTPPEK CDTLLCDIGE SSPNPTIEAG
2660 2670 2680 2690 2700
RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMETLQR KYGGALVRNP
2710 2720 2730 2740 2750
LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMKHKK ATYETDVDLG
2760 2770 2780 2790 2800
SGTRNIGIES EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY
2810 2820 2830 2840 2850
ETKQTGSASS MVNGVVRLLT KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV
2860 2870 2880 2890 2900
DTRTQEPKEG TKKLMKITAE WLWKELGKKK TPRMCTREEF TRKVRSNAAL
2910 2920 2930 2940 2950
GAIFTDENKW KSAREAVEDS RFWELVDRER NLHLEGKCET CVYNMMGKRE
2960 2970 2980 2990 3000
KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RGNSLSGVEG
3010 3020 3030 3040 3050
EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMEG
3060 3070 3080 3090 3100
EHKKLAEAIF KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL
3110 3120 3130 3140 3150
NTFTNMEAQL IRQMEGEGIF KSIQHLTVTE EIAVQNWLAR VGRERLSRMA
3160 3170 3180 3190 3200
ISGDDCVVKP LDDRFASALT ALNDMGKVRK DIQQWEPSRG WNDWTQVPFC
3210 3220 3230 3240 3250
SHHFHELVMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLK ETACLGKSYA
3260 3270 3280 3290 3300
QMWTLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
3310 3320 3330 3340 3350
LAVWNRVWIQ ENPWMEDKTP VESWEEVPYL GKREDQWCGS LIGLTSRATW
3360 3370 3380 3390
AKNIQTAINQ VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W
Length:3,391
Mass (Da):379,250
Last modified:July 1, 1989 - v2
Checksum:i3F2D1D6B8855718E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1044 – 10441H → D in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1231 – 12311A → T in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1236 – 12361A → V in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1263 – 12631I → M in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1266 – 12661N → K in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1301 – 13011A → V in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1308 – 13081L → F in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1342 – 13421S → N in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1454 – 14541V → L in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1503 – 15031R → K in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1552 – 15543ISY → VSC in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1595 – 15951T → A in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1615 – 16173VDR → IDK in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1661 – 16622KR → RK in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1685 – 16851E → G in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1820 – 18201N → S in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1846 – 18461I → T in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1858 – 18581I → T in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1874 – 18741A → T in AAA66406 (PubMed:3803928).Curated
Sequence conflicti1878 – 18781D → N in AAA66406 (PubMed:3803928).Curated
Sequence conflicti2169 – 21691K → R (PubMed:3803928).Curated
Sequence conflicti2265 – 22662ES → QP (PubMed:3803928).Curated
Sequence conflicti2330 – 23312IH → MD (PubMed:3803928).Curated
Sequence conflicti2355 – 23551L → F (PubMed:3803928).Curated
Sequence conflicti2391 – 23922DG → GR (PubMed:3803928).Curated
Sequence conflicti2418 – 24181I → V (PubMed:3803928).Curated
Sequence conflicti2647 – 26471I → V (PubMed:3803928).Curated
Sequence conflicti2687 – 26871T → A (PubMed:3803928).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20558 Genomic RNA. Translation: AAA42942.1.
M15075 Genomic RNA. Translation: AAA42961.1.
M14969 Genomic RNA. Translation: AAA66406.1.
M14970 Genomic RNA. No translation available.
PIRiA25817.
A94346. GNWVJA.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20558 Genomic RNA. Translation: AAA42942.1.
M15075 Genomic RNA. Translation: AAA42961.1.
M14969 Genomic RNA. Translation: AAA66406.1.
M14970 Genomic RNA. No translation available.
PIRiA25817.
A94346. GNWVJA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UZVX-ray2.10A576-680[»]
ProteinModelPortaliP07564.
SMRiP07564. Positions 21-100, 115-194, 281-674, 1394-1440, 1495-2093, 2498-2759, 2765-3374.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.

Miscellaneous databases

PROiP07564.

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.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_DEN2J
AccessioniPrimary (citable) accession number: P07564
Secondary accession number(s): P07565
, Q88642, Q88643, Q88644, Q88645
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 1, 1989
Last modified: September 7, 2016
This is version 154 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.