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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 1 (strain Brazil/97-11/1997) (DENV-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein C: Plays a role in virus budding by binding to 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 in host cytoplasm after hemifusion induced by surface proteins. Can migrate tot cell nucleus where it modulates host functions.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. Presumably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is ineficient, 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 extodomain. 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 particule 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 ineficient, 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. May plays a role in viral genome replication. Assist membrane bending and envelopment of genomic RNA at the endoplasmic reticulum. Excreted as a hexameric lipoparticle that plays a role against host immune responce.By similarity
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.By similarity
Non-structural protein 2B: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
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.PROSITE-ProRule annotation
Non-structural protein 4A: Induces host endoplasmic 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

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)DescriptionActionsGraphical viewLength
Active sitei1526Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1550Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1610Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Binding sitei2507mRNA capPROSITE-ProRule annotation1
Binding sitei2510mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2511mRNA capPROSITE-ProRule annotation1
Binding sitei2513mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2518mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2522mRNA capPROSITE-ProRule annotation1
Binding sitei2549S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2554Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2579S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2580S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2597S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2598S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2624S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2625S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2639Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2640S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2643mRNA capPROSITE-ProRule annotation1
Sitei2673Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2704mRNA capPROSITE-ProRule annotation1
Binding sitei2706mRNA capPROSITE-ProRule annotation1
Sitei2709Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2711S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1669 – 1676ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase, Viral ion channel

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, Ion transport, mRNA capping, mRNA processing, Transcription, Transcription regulation, Transport, 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 1 (strain Brazil/97-11/1997) (DENV-1)
Taxonomic identifieri408685 [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]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007764 Componenti: Genome

Subcellular locationi

Protein C :
  • Virion By similarity
  • Host nucleus By similarity
Peptide pr :
  • Secreted By similarity
Small envelope protein M :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotationBy similarity; Multi-pass membrane protein By similarity
Envelope protein E :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotationBy similarity; Multi-pass membrane protein By similarity
Non-structural protein 1 :
  • Secreted By similarity
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Lumenal side By similarity
Non-structural protein 2A-alpha :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
Non-structural protein 2A :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
Serine protease subunit NS2B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotationBy similarity
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 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.By similarity
Non-structural protein 4B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
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.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 101CytoplasmicSequence analysisAdd BLAST101
Transmembranei102 – 119HelicalSequence analysisAdd BLAST18
Topological domaini120 – 242ExtracellularSequence analysisAdd BLAST123
Transmembranei243 – 260HelicalSequence analysisAdd BLAST18
Topological domaini261CytoplasmicSequence analysis1
Transmembranei262 – 280HelicalSequence analysisAdd BLAST19
Topological domaini281 – 725ExtracellularSequence analysisAdd BLAST445
Intramembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 752ExtracellularSequence analysis6
Intramembranei753 – 775HelicalSequence analysisAdd BLAST23
Topological domaini776 – 1125ExtracellularSequence analysisAdd BLAST350
Transmembranei1126 – 1146HelicalSequence analysisAdd BLAST21
Topological domaini1147 – 1157CytoplasmicSequence analysisAdd BLAST11
Transmembranei1158 – 1178HelicalSequence analysisAdd BLAST21
Topological domaini1179 – 1199LumenalSequence analysisAdd BLAST21
Transmembranei1200 – 1220HelicalSequence analysisAdd BLAST21
Topological domaini1221 – 1289CytoplasmicSequence analysisAdd BLAST69
Transmembranei1290 – 1310HelicalSequence analysisAdd BLAST21
Topological domaini1311 – 1315LumenalSequence analysis5
Transmembranei1316 – 1336HelicalSequence analysisAdd BLAST21
Topological domaini1337 – 1346CytoplasmicSequence analysis10
Transmembranei1347 – 1367HelicalSequence analysisAdd BLAST21
Topological domaini1368 – 1370LumenalSequence analysis3
Transmembranei1371 – 1391HelicalSequence analysisAdd BLAST21
Topological domaini1392 – 1447CytoplasmicSequence analysisAdd BLAST56
Intramembranei1448 – 1468HelicalSequence analysisAdd BLAST21
Topological domaini1469 – 2148CytoplasmicSequence analysisAdd BLAST680
Transmembranei2149 – 2169HelicalSequence analysisAdd BLAST21
Topological domaini2170 – 2171LumenalSequence analysis2
Intramembranei2172 – 2192HelicalSequence analysisAdd BLAST21
Topological domaini2193LumenalSequence analysis1
Transmembranei2194 – 2214HelicalSequence analysisAdd BLAST21
Topological domaini2215 – 2229CytoplasmicSequence analysisAdd BLAST15
Transmembranei2230 – 2250Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2251 – 2276LumenalSequence analysisAdd BLAST26
Intramembranei2277 – 2297HelicalSequence analysisAdd BLAST21
Topological domaini2298 – 2349LumenalSequence analysisAdd BLAST52
Transmembranei2350 – 2370HelicalSequence analysisAdd BLAST21
Topological domaini2371 – 2415CytoplasmicSequence analysisAdd BLAST45
Transmembranei2416 – 2436HelicalSequence analysisAdd BLAST21
Topological domaini2437 – 2461LumenalSequence analysisAdd BLAST25
Transmembranei2462 – 2482HelicalSequence analysisAdd BLAST21
Topological domaini2483 – 3392CytoplasmicSequence analysisAdd BLAST910

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004052031 – 3392Genome polyproteinAdd BLAST3392
ChainiPRO_00002646341 – 100Protein CBy similarityAdd BLAST100
PropeptideiPRO_0000264635101 – 114ER anchor for the protein C, removed in mature form by serine protease NS3Add BLAST14
ChainiPRO_0000264636115 – 280prMBy similarityAdd BLAST166
ChainiPRO_0000264637115 – 205Peptide prBy similarityAdd BLAST91
ChainiPRO_0000264638206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000264639281 – 775Envelope protein EBy similarityAdd BLAST495
ChainiPRO_0000264640776 – 1127Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00002646411128 – 1345Non-structural protein 2ABy similarityAdd BLAST218
ChainiPRO_00002646421128 – 1315Non-structural protein 2A-alphaBy similarityAdd BLAST188
ChainiPRO_00002646431346 – 1475Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00002646441476 – 2094Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00002646452095 – 2221Non-structural protein 4ABy similarityAdd BLAST127
PeptideiPRO_00002646462222 – 2244Peptide 2kAdd BLAST23
ChainiPRO_00002646472245 – 2493Non-structural protein 4BBy similarityAdd BLAST249
ChainiPRO_00002646482494 – 3392RNA-directed RNA polymerase NS5By similarityAdd BLAST899

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi183N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Glycosylationi347N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 396By similarity
Glycosylationi433N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi465 ↔ 565By similarity
Disulfide bondi582 ↔ 613By similarity
Disulfide bondi779 ↔ 790By similarity
Disulfide bondi830 ↔ 918By similarity
Disulfide bondi954 ↔ 998By similarity
Glycosylationi982N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi1055 ↔ 1104By similarity
Disulfide bondi1066 ↔ 1088By similarity
Disulfide bondi1087 ↔ 1091By similarity
Glycosylationi2303N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2307N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2459N-linked (GlcNAc...); by hostSequence analysis1

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, wereas cleavages in the cytoplasmic side are performed by the Serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Non-structural protein 2A-alpha: A C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3.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
Non-structural protein 1: 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
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei100 – 101Cleavage; by viral protease NS3Sequence analysis2
Sitei114 – 115Cleavage; by host signal peptidaseBy similarity2
Sitei205 – 206Cleavage; by host furinSequence analysis2
Sitei280 – 281Cleavage; by host signal peptidaseSequence analysis2
Sitei775 – 776Cleavage; by host signal peptidaseSequence analysis2
Sitei1127 – 1128Cleavage; by hostSequence analysis2
Sitei1345 – 1346Cleavage; by viral protease NS3Sequence analysis2
Sitei1475 – 1476Cleavage; by autolysisSequence analysis2
Sitei2094 – 2095Cleavage; by autolysisSequence analysis2
Sitei2221 – 2222Cleavage; by viral protease NS3Sequence analysis2
Sitei2244 – 2245Cleavage; by host signal peptidaseSequence analysis2
Sitei2493 – 2494Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

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

Interactioni

Subunit structurei

Protein C: Homodimerizes. Protein prM: Forms homodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Forms homodimers with envelope protein E in the endoplasmic reticulum and Golgi. Non-structural protein 1: Forms homodimers as well as homohexamers. NS1 may interact with NS4A. Non-structural protein 2B: Forms a heterodimer with Non-structural protein 3. May form homooligomers. Non-structural protein 3: Forms a heterodimer with Non-structural protein 2B. Interacts with Non-structural protein 4B. Interacts with unphosphorylated Non-structural protein 5; this interaction stimulates Non-structural protein 5 guanylyltransferase activity. Non-structural protein 4B: Interacts with non-structural protein 3. Non-structural protein 5: 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

13392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi586 – 590Combined sources5
Beta strandi600 – 606Combined sources7
Beta strandi612 – 614Combined sources3
Beta strandi617 – 621Combined sources5
Beta strandi633 – 635Combined sources3
Beta strandi637 – 639Combined sources3
Beta strandi645 – 649Combined sources5
Beta strandi653 – 663Combined sources11
Beta strandi666 – 673Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UZQX-ray1.60B578-680[»]
ProteinModelPortaliP27909.
SMRiP27909.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1476 – 1653Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1656 – 1812Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1822 – 1989Helicase C-terminalPROSITE-ProRule annotationAdd BLAST168
Domaini2495 – 2756mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST262
Domaini3021 – 3170RdRp catalyticPROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 74Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST42
Regioni1398 – 1437Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1760 – 1763DEAH box4

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.

P27909-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNQRKKTGR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF
60 70 80 90 100
IAFLRFLAIP PTAGILARWS SFKKNGAIKV LRGFKKEISS MLNIMNRRKR
110 120 130 140 150
SVTMLLMLLP TALAFHLTTR GGEPHMIVSK QERGKSLLFK TSAGVNMCTL
160 170 180 190 200
IAMDLGELCE DTMTYKCPRI TEAEPDDVDC WCNATDTWVT YGTCSQTGEH
210 220 230 240 250
RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW ALRHPGFTVI
260 270 280 290 300
ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW
310 320 330 340 350
VDVVLEHGSC VTTMAKNKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT
360 370 380 390 400
DSRCPTQGEA TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLLTCAKFK
410 420 430 440 450
CVTKLEGKIV QYENLKYSVI VTVHTGDQHQ VGNETTEHGT IATITPQAPT
460 470 480 490 500
SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT MKEKSWLVHK QWFLDLPLPW
510 520 530 540 550
TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM HTALTGATEI
560 570 580 590 600
QTSGTTTIFA GHLKCRLKMD KLTLKGTSYV MCTGSFKLEK EVAETQHGTV
610 620 630 640 650
LVQVKYEGTD APCKIPFSTQ DEKGVTQNGR LITANPIVTD KEKPVNIETE
660 670 680 690 700
PPFGESYIVV GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW
710 720 730 740 750
DFGSIGGVFT SVGKLVHQVF GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS
760 770 780 790 800
RSTSLSMTCI AVGMVTLYLG VMVQADSGCV INWKGRELKC GSGIFVTNEV
810 820 830 840 850
HTWTEQYKFQ ADSPKRLSAA IGRAWEEGVC GIRSATRLEN IMWKQISNEL
860 870 880 890 900
NHILLENDIK FTVVVGNANG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG
910 920 930 940 950
ADIQNTTFII DGPDTPECPD EQRAWNIWEV EDYGFGIFTT NIWLKLRDSY
960 970 980 990 1000
TQMCDHRLMS AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW
1010 1020 1030 1040 1050
PKSHTLWSNG VLESEMIIPK MYGGPISQHN YRPGYFTQTA GPWHLGKLEL
1060 1070 1080 1090 1100
DFDLCEGTTV VVDEHCGSRG PSLRTTTVTG KIIHEWCCRS CTLPPLRFRG
1110 1120 1130 1140 1150
EDGCWYGMEI RPVKEKEENL VRSMVSAGSG EVDSFSLGIL CVSIMIEEVM
1160 1170 1180 1190 1200
RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMVGAN ASDKMGMGTT
1210 1220 1230 1240 1250
YLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLVAS VELPNSLEEL
1260 1270 1280 1290 1300
GDGLAMGIMM LKLLTEFQPH QLWTTLLSLT FIKTTLSLDY AWKTTAMVLS
1310 1320 1330 1340 1350
IVSLFPLCLS TTSQKTTWLP VLLGSFGCKP LTMFLITENE IWGRKSWPLN
1360 1370 1380 1390 1400
EGIMAIGIVS ILLSSLLKND VPLAGPLIAG GMLIACYVIS GSSADLSLEK
1410 1420 1430 1440 1450
AAEVSWEEEA EHSGTSHNIL VEVQDDGTMK IKDEERDDTL TILLKATLLA
1460 1470 1480 1490 1500
VSGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI
1510 1520 1530 1540 1550
LQRGLLGRSQ VGVGVFQDGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD
1560 1570 1580 1590 1600
LISYGGGWRF QGSWNTGEEV QVIAVEPGKN PKNVQTTPGT FKTPEGEVGA
1610 1620 1630 1640 1650
IALDFKPGTS GSPIVNREGK IVGLYGNGVV TTSGTYVSAI AQAKASQEGP
1660 1670 1680 1690 1700
LPEIEDEVFK KRNLTIMDLH PGSGKTRRYL PAIVREAIKR KLRTLILAPT
1710 1720 1730 1740 1750
RVVASEMAEA LKGMPIRYQT TAVKSEHTGR EIVDLMCHAT FTMRLLSPVR
1760 1770 1780 1790 1800
VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA
1810 1820 1830 1840 1850
FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC
1860 1870 1880 1890 1900
LRKNGKRVIQ LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID
1910 1920 1930 1940 1950
PRRCLKPVIL KDGPERVILA GPMPVTVASA AQRRGRIGRN QNKEGDQYVY
1960 1970 1980 1990 2000
MGQPLNNDED HAHWTEAKML LDNINTPEGI IPALFEPERE KSAAIDGEYR
2010 2020 2030 2040 2050
LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF DGERNNQVLE
2060 2070 2080 2090 2100
ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL
2110 2120 2130 2140 2150
ILEIGKLPQH LTLRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM
2160 2170 2180 2190 2200
LLALIAVLTG GVTLFFLSGK GLGKTSIGLL CVTASSALLW MASVEPHWIA
2210 2220 2230 2240 2250
ASIILEFFLM VLLIPEPDRQ RTPQDNQLAY VVIGLLFMIL TVAANEMGLL
2260 2270 2280 2290 2300
ETTKKDLGIG HVAAENHQHA TILDVDLHPA SAWTLYAVAT TVITPMMRHT
2310 2320 2330 2340 2350
IENTTANISL TAIANQAAIL MGLDKGWPIS KMDLGVPLLA LGCYSQVNPL
2360 2370 2380 2390 2400
TLTAAVLMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL
2410 2420 2430 2440 2450
DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW
2460 2470 2480 2490 2500
EGSPGKFWNT TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE
2510 2520 2530 2540 2550
TLGEKWKRQL NQLSKSEFNT YKRSGIMEVD RSEAKEGLKR GETTKHAVSR
2560 2570 2580 2590 2600
GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW SYYCAGLKKV TEVKGYTKGG
2610 2620 2630 2640 2650
PGHEEPIPMA TYGWNLVKLH SGKDVFFMPP EKCDTLLCDI GESSPNPTIE
2660 2670 2680 2690 2700
EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN
2710 2720 2730 2740 2750
PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL
2760 2770 2780 2790 2800
GAGTRHVAVE PEVANLDIIG QRIENIKNEH KSTWHYDEDN PYKTWAYHGS
2810 2820 2830 2840 2850
YEVKPSGSAS SMVNGVVRLL TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK
2860 2870 2880 2890 2900
VDTRTPRAKR GTAQIMEVTA KWLWGFLSRN KKPRICTREE FTRKVRSNAA
2910 2920 2930 2940 2950
IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA TCVYNMMGKR
2960 2970 2980 2990 3000
EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE
3010 3020 3030 3040 3050
GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME
3060 3070 3080 3090 3100
PEHALLATSI FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG
3110 3120 3130 3140 3150
LNTFTNMEVQ LIRQMESEGI FFPSELESPN LAERVLDWLE KHGAERLKRM
3160 3170 3180 3190 3200
AISGDDCVVK PIDDRFATAL IALNDMGKVR KDIPQWEPSK GWNDWQQVPF
3210 3220 3230 3240 3250
CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL RETACLGKSY
3260 3270 3280 3290 3300
AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED
3310 3320 3330 3340 3350
MLSVWNRVWI EENPWMEDKT HVSSWEEVPY LGKREDQWCG SLIGLTARAT
3360 3370 3380 3390
WATNIQVAIN QVRRLIGNEN YLDYMTSMKR FKNESDPEGA LW
Length:3,392
Mass (Da):378,905
Last modified:December 12, 2006 - v2
Checksum:iBBD894175578E164
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti394L → I in strain: Isolate Thailand/TH-Sman/1958. 1
Natural varianti402V → A in strain: Isolate Thailand/TH-Sman/1958. 1
Natural varianti441I → T in strain: Isolate Thailand/TH-Sman/1958. 1
Natural varianti475 – 476EM → RV in strain: Isolate 924-1. 2
Natural varianti483E → K in strain: Isolate 924-1. 1
Natural varianti531V → A in strain: Isolate 924-1 and Isolate Thailand/TH-Sman/1958. 1
Natural varianti577T → M in strain: Isolate 924-1 and Isolate Thailand/TH-Sman/1958. 1
Natural varianti619T → S in strain: Isolate 924-1. 1
Natural varianti649T → E in strain: Isolate 924-1 and Isolate Thailand/TH-Sman/1958. 1
Natural varianti677S → I in strain: Isolate Thailand/TH-Sman/1958n. 1
Natural varianti712V → M in strain: Isolate Thailand/TH-Sman/1958. 1
Natural varianti716V → I in strain: Isolate 924-1. 1
Natural varianti719V → I in strain: Isolate 924-1. 1
Natural varianti752S → N in strain: Isolate Thailand/TH-Sman/1958. 1
Natural varianti758T → M in strain: Isolate Thailand/TH-Sman/1958. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00504 Genomic RNA. Translation: BAA00396.1.
D10513 Genomic RNA. Translation: BAA01388.1.
AF311956 Genomic RNA. Translation: AAN60368.1.
PIRiJQ1405.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00504 Genomic RNA. Translation: BAA00396.1.
D10513 Genomic RNA. Translation: BAA01388.1.
AF311956 Genomic RNA. Translation: AAN60368.1.
PIRiJQ1405.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UZQX-ray1.60B578-680[»]
ProteinModelPortaliP27909.
SMRiP27909.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

PROiP27909.

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_DEN1B
AccessioniPrimary (citable) accession number: P27909
Secondary accession number(s): P29983, Q8B648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 12, 2006
Last modified: November 30, 2016
This is version 126 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.