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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 3 (strain Philippines/H87/1956) (DENV-3)
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 sitei1524Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1548Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1608Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Binding sitei2504mRNA capPROSITE-ProRule annotation1
Binding sitei2507mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2508mRNA capPROSITE-ProRule annotation1
Binding sitei2510mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2515mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2519mRNA capPROSITE-ProRule annotation1
Binding sitei2546S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2551Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2576S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2577S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2594S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2595S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2621S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2622S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2636Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2637S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2640mRNA capPROSITE-ProRule annotation1
Sitei2670Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2701mRNA capPROSITE-ProRule annotation1
Binding sitei2703mRNA capPROSITE-ProRule annotation1
Sitei2706Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2708S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1667 – 1674ATPPROSITE-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

Protein family/group databases

MEROPSiS07.001.

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 3 (strain Philippines/H87/1956) (DENV-3)
Taxonomic identifieri408870 [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
  • UP000007200 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 – 100CytoplasmicSequence analysisAdd BLAST100
Transmembranei101 – 118HelicalSequence analysisAdd BLAST18
Topological domaini119 – 243ExtracellularSequence analysisAdd BLAST125
Transmembranei244 – 264HelicalSequence analysisAdd BLAST21
Topological domaini265CytoplasmicSequence analysis1
Transmembranei266 – 280HelicalSequence analysisAdd BLAST15
Topological domaini281 – 723ExtracellularSequence analysisAdd BLAST443
Intramembranei724 – 744HelicalSequence analysisAdd BLAST21
Topological domaini745 – 750ExtracellularSequence analysis6
Intramembranei751 – 771HelicalSequence analysisAdd BLAST21
Topological domaini772 – 1123ExtracellularSequence analysisAdd BLAST352
Transmembranei1124 – 1144HelicalSequence analysisAdd BLAST21
Topological domaini1145 – 1154CytoplasmicSequence analysis10
Transmembranei1155 – 1175HelicalSequence analysisAdd BLAST21
Topological domaini1176 – 1196LumenalSequence analysisAdd BLAST21
Transmembranei1197 – 1217HelicalSequence analysisAdd BLAST21
Topological domaini1218 – 1282CytoplasmicSequence analysisAdd BLAST65
Transmembranei1283 – 1303HelicalSequence analysisAdd BLAST21
Topological domaini1304 – 1315LumenalSequence analysisAdd BLAST12
Transmembranei1316 – 1336HelicalSequence analysisAdd BLAST21
Topological domaini1337 – 1344CytoplasmicSequence analysis8
Transmembranei1345 – 1365HelicalSequence analysisAdd BLAST21
Topological domaini1366 – 1368LumenalSequence analysis3
Transmembranei1369 – 1389HelicalSequence analysisAdd BLAST21
Topological domaini1390 – 1443CytoplasmicSequence analysisAdd BLAST54
Intramembranei1444 – 1464HelicalSequence analysisAdd BLAST21
Topological domaini1465 – 2146CytoplasmicSequence analysisAdd BLAST682
Transmembranei2147 – 2167HelicalSequence analysisAdd BLAST21
Topological domaini2168 – 2169LumenalSequence analysis2
Intramembranei2170 – 2190HelicalSequence analysisAdd BLAST21
Topological domaini2191LumenalSequence analysis1
Transmembranei2192 – 2212HelicalSequence analysisAdd BLAST21
Topological domaini2213 – 2227CytoplasmicSequence analysisAdd BLAST15
Transmembranei2228 – 2248Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2249 – 2273LumenalSequence analysisAdd BLAST25
Intramembranei2274 – 2294HelicalSequence analysisAdd BLAST21
Topological domaini2295 – 2305LumenalSequence analysisAdd BLAST11
Intramembranei2306 – 2326HelicalSequence analysisAdd BLAST21
Topological domaini2327 – 2346LumenalSequence analysisAdd BLAST20
Transmembranei2347 – 2367HelicalSequence analysisAdd BLAST21
Topological domaini2368 – 2412CytoplasmicSequence analysisAdd BLAST45
Transmembranei2413 – 2433HelicalSequence analysisAdd BLAST21
Topological domaini2434 – 2458LumenalSequence analysisAdd BLAST25
Transmembranei2459 – 2479HelicalSequence analysisAdd BLAST21
Topological domaini2480 – 3390CytoplasmicSequence analysisAdd BLAST911

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_00004052211 – 3390Genome polyproteinAdd BLAST3390
ChainiPRO_00000379891 – 100Protein CBy similarityAdd BLAST100
PropeptideiPRO_0000037990101 – 114ER anchor for the protein C, removed in mature form by serine protease NS3By similarityAdd BLAST14
ChainiPRO_0000308293115 – 280prMBy similarityAdd BLAST166
ChainiPRO_0000308294115 – 205Peptide prBy similarityAdd BLAST91
ChainiPRO_0000037991206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037992281 – 773Envelope protein EBy similarityAdd BLAST493
ChainiPRO_0000037993774 – 1125Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000379941126 – 1343Non-structural protein 2ABy similarityAdd BLAST218
ChainiPRO_00003082951126 – 1313Non-structural protein 2A-alphaBy similarityAdd BLAST188
ChainiPRO_00000379951344 – 1473Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00000379961474 – 2092Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00000379972093 – 2219Non-structural protein 4ABy similarityAdd BLAST127
PeptideiPRO_00003082962220 – 2242Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000379982243 – 2490Non-structural protein 4BBy similarityAdd BLAST248
ChainiPRO_00000379992491 – 3390RNA-directed RNA polymerase NS5By similarityAdd BLAST900

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 bondi463 ↔ 563By similarity
Disulfide bondi580 ↔ 611By similarity
Disulfide bondi777 ↔ 788By similarity
Disulfide bondi828 ↔ 916By similarity
Glycosylationi903N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi952 ↔ 996By similarity
Glycosylationi980N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi1053 ↔ 1102By similarity
Disulfide bondi1064 ↔ 1086By similarity
Disulfide bondi1085 ↔ 1089By similarity
Glycosylationi2300N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2304N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2456N-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
Sitei773 – 774Cleavage; by host signal peptidaseSequence analysis2
Sitei1125 – 1126Cleavage; by hostBy similarity2
Sitei1343 – 1344Cleavage; by viral protease NS3Sequence analysis2
Sitei1473 – 1474Cleavage; by autolysisSequence analysis2
Sitei2092 – 2093Cleavage; by autolysisSequence analysis2
Sitei2219 – 2220Cleavage; by viral protease NS3Sequence analysis2
Sitei2242 – 2243Cleavage; by host signal peptidaseSequence analysis2
Sitei2490 – 2491Cleavage; 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

13390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni282 – 285Combined sources4
Beta strandi287 – 293Combined sources7
Beta strandi301 – 305Combined sources5
Beta strandi310 – 315Combined sources6
Beta strandi318 – 327Combined sources10
Beta strandi334 – 337Combined sources4
Beta strandi343 – 351Combined sources9
Helixi363 – 366Combined sources4
Beta strandi368 – 379Combined sources12
Turni381 – 384Combined sources4
Beta strandi389 – 404Combined sources16
Beta strandi406 – 409Combined sources4
Beta strandi415 – 423Combined sources9
Beta strandi434 – 436Combined sources3
Beta strandi438 – 443Combined sources6
Beta strandi448 – 453Combined sources6
Turni454 – 456Combined sources3
Beta strandi457 – 462Combined sources6
Beta strandi473 – 479Combined sources7
Beta strandi482 – 487Combined sources6
Helixi488 – 493Combined sources6
Beta strandi503 – 505Combined sources3
Helixi512 – 514Combined sources3
Beta strandi517 – 519Combined sources3
Beta strandi521 – 524Combined sources4
Beta strandi527 – 529Combined sources3
Helixi535 – 541Combined sources7
Beta strandi543 – 545Combined sources3
Beta strandi561 – 566Combined sources6
Beta strandi577 – 579Combined sources3
Beta strandi584 – 586Combined sources3
Beta strandi594 – 596Combined sources3
Beta strandi598 – 604Combined sources7
Beta strandi610 – 612Combined sources3
Beta strandi615 – 618Combined sources4
Beta strandi628 – 631Combined sources4
Beta strandi635 – 637Combined sources3
Beta strandi643 – 648Combined sources6
Beta strandi651 – 661Combined sources11
Beta strandi665 – 671Combined sources7
Helixi2499 – 2509Combined sources11
Helixi2512 – 2519Combined sources8
Turni2520 – 2522Combined sources3
Beta strandi2524 – 2527Combined sources4
Helixi2529 – 2536Combined sources8
Helixi2548 – 2557Combined sources10
Beta strandi2565 – 2571Combined sources7
Helixi2576 – 2582Combined sources7
Beta strandi2587 – 2593Combined sources7
Turni2609 – 2612Combined sources4
Beta strandi2613 – 2617Combined sources5
Helixi2622 – 2624Combined sources3
Beta strandi2631 – 2635Combined sources5
Helixi2644 – 2658Combined sources15
Helixi2659 – 2661Combined sources3
Beta strandi2666 – 2672Combined sources7
Helixi2677 – 2690Combined sources14
Beta strandi2693 – 2695Combined sources3
Beta strandi2707 – 2712Combined sources6
Helixi2717 – 2730Combined sources14
Beta strandi2733 – 2735Combined sources3
Beta strandi2740 – 2743Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UZGX-ray3.60A/B281-672[»]
2J7UX-ray1.85A2762-3390[»]
2J7WX-ray2.60A2762-3390[»]
3P8ZX-ray1.70A/C2491-2752[»]
3P97X-ray1.70A/C2491-2752[»]
3UZEX-ray2.04C/D573-673[»]
3VTTX-ray1.70A/B574-678[»]
5CCVX-ray3.60A/B/C/D/E/F/G/H2491-3390[»]
ProteinModelPortaliP27915.
SMRiP27915.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27915.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1474 – 1651Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1654 – 1810Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1821 – 1986Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2492 – 2753mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST262
Domaini3018 – 3168RdRp catalyticPROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 74Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST42
Regioni1396 – 1435Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1758 – 1761DEAH 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.

P27915-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSRGLLNG QGPMKLVMAF
60 70 80 90 100
IAFLRFLAIP PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK
110 120 130 140 150
TSLCLMMMLP ATLAFHLTSR DGEPRMIVGK NERGKSLLFK TASGINMCTL
160 170 180 190 200
IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC WCNLTSTWVT YGTCNQAGEH
210 220 230 240 250
RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW ALRHPGFTIL
260 270 280 290 300
ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW
310 320 330 340 350
VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT
360 370 380 390 400
DSRCPTQGEA ILPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ
410 420 430 440 450
CLESIEGKVV QHENLKYTVI ITVHTGDQHQ VGNETQGVTA EITSQASTAE
460 470 480 490 500
AILPEYGTLG LECSPRTGLD FNEMILLTMK NKAWMVHRQW FFDLPLPWTS
510 520 530 540 550
GATTKTPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT ALTGATEIQT
560 570 580 590 600
SGGTSIFAGH LKCRLKMDKL KLKGMSYAMC LNTFVLKKEV SETQHGTILI
610 620 630 640 650
KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP
660 670 680 690 700
FGESNIVIGI GDKALKINWY RKGSSIGKMF EATARGARRM AILGDTAWDF
710 720 730 740 750
GSVGGVLNSL GKMVHQIFGS AYTALFSGVS WIMKIGIGVL LTWIGLNSKN
760 770 780 790 800
TSMSFSCIAI GIITLYLGVV VQADMGCVIN WKGKELKCGS GIFVTNEVHT
810 820 830 840 850
WTEQYKFQAD SPKRVATAIA GAWENGVCGI RSTTRMENLL WKQIANELNY
860 870 880 890 900
ILWENDIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGLAKIVTAE
910 920 930 940 950
TQNSSFIIDG PSTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ
960 970 980 990 1000
LCDHRLMSAA VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK
1010 1020 1030 1040 1050
SHTLWSNGVL ESDMIIPKSL AGPISQHNHR PGYHTQTAGP WHLGKLELDF
1060 1070 1080 1090 1100
NYCEGTTVVI SENCGTRGPS LRTTTVSGKL IHEWCCRSCT LPPLRYMGED
1110 1120 1130 1140 1150
GCWYGMEIRP INEKEENMVK SLASAGSGKV DNFTMGVLCL AILFEEVMRG
1160 1170 1180 1190 1200
KFGKKHMIAG VLFTFVLLLS GQITWRGMAH TLIMIGSNAS DRMGMGVTYL
1210 1220 1230 1240 1250
ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMAATLR LPEDIEQMAN
1260 1270 1280 1290 1300
GIALGLMALK LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGI
1310 1320 1330 1340 1350
SLLPVCQSSS MRKTDWLPMT VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG
1360 1370 1380 1390 1400
VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL LIACYVITGT SADLTVEKAA
1410 1420 1430 1440 1450
DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV LLKTALLIVS
1460 1470 1480 1490 1500
GIFPYSIPAT MLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ
1510 1520 1530 1540 1550
QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI
1560 1570 1580 1590 1600
SYGGGWRLSA QWQKGEEVQV IAVEPGKNPK NFQTMPGIFQ TTTGEIGAIA
1610 1620 1630 1640 1650
LDFKPGTSGS PIINREGKVV GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP
1660 1670 1680 1690 1700
ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA IVREAIKRRL RTLILAPTRV
1710 1720 1730 1740 1750
VAAEMEEAMK GLPIRYQTTA TKSEHTGREI VDLMCHATFT MRLLSPVRVP
1760 1770 1780 1790 1800
NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP
1810 1820 1830 1840 1850
QSNAPIQDEE RDIPERSWNS GNEWITDFVG KTVWFVPSIK AGNVIANCLR
1860 1870 1880 1890 1900
KNGKKVIQLS RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FIADRVIDPR
1910 1920 1930 1940 1950
RCLKPVILTD GPERVILAGP MPVTVASAAQ RRGRVGRNPQ KENDQYIFMG
1960 1970 1980 1990 2000
QPLNKDEDHA HWTEAKMLLD NINTPEGIIP ALFEPEREKS AAIDGEYRLK
2010 2020 2030 2040 2050
GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG ERNNQILEEN
2060 2070 2080 2090 2100
MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT
2110 2120 2130 2140 2150
EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL
2160 2170 2180 2190 2200
GLMILLTGGA MLFLISGKGI GKTSIGLICV IASSGMLWMA DVPLQWIASA
2210 2220 2230 2240 2250
IVLEFFMMVL LIPEPEKQRT PQDNQLAYVV IGILTLAAIV AANEMGLLET
2260 2270 2280 2290 2300
TKRDLGMSKE PGVVSPTSYL DVDLHPASAW TLYAVATTVI TPMLRHTIEN
2310 2320 2330 2340 2350
STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC YSQVNPLTLI
2360 2370 2380 2390 2400
AAVLLLVTHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV
2410 2420 2430 2440 2450
IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEVLTLAT GPITTLWEGS
2460 2470 2480 2490 2500
PGKFWNTTIA VSMANIFRGS YLAGAGLALS IMKSVGTGKR GTGSQGETLG
2510 2520 2530 2540 2550
EKWKKKLNQL SRKEFDLYKK SGITEVDRTE AKEGLKRGEI THHAVSRGSA
2560 2570 2580 2590 2600
KLQWFVERNM VIPEGRVIDL GCGRGGWSYY CAGLKKVTEV RGYTKGGPGH
2610 2620 2630 2640 2650
EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES SPSPTVEESR
2660 2670 2680 2690 2700
TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS
2710 2720 2730 2740 2750
RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG
2760 2770 2780 2790 2800
TRHVNAEPET PNMDVIGERI KRIKEEHSST WHYDDENPYK TWAYHGSYEV
2810 2820 2830 2840 2850
KATGSASSMI NGVVKLLTKP WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT
2860 2870 2880 2890 2900
RTPRPMPGTR KVMEITAEWL WRTLGRNKRP RLCTREEFTK KVRTNAAMGA
2910 2920 2930 2940 2950
VFTEENQWDS ARAAVEDEEF WKLVDREREL HKLGKCGSCV YNMMGKREKK
2960 2970 2980 2990 3000
LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG
3010 3020 3030 3040 3050
LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH
3060 3070 3080 3090 3100
RQLANAIFKL TYQNKVVKVQ RPTPKGTVMD IISRKDQRGS GQVGTYGLNT
3110 3120 3130 3140 3150
FTNMEAQLIR QMEGEGVLSK ADLENPHPLE KKITQWLETK GVERLKRMAI
3160 3170 3180 3190 3200
SGDDCVVKPI DDRFANALLA LNDMGKVRKD IPQWQPSKGW HDWQQVPFCS
3210 3220 3230 3240 3250
HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE TACLGKAYAQ
3260 3270 3280 3290 3300
MWTLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML
3310 3320 3330 3340 3350
TVWNRVWIED NPWMEDKTPV TTWEDVPYLG KREDQWCGSL IGLTSRATWA
3360 3370 3380 3390
QNILTAIQQV RSLIGNEEFL DYMPSMKRFR KEEESEGAIW
Length:3,390
Mass (Da):378,063
Last modified:August 1, 1992 - v1
Checksum:i666E8F70F1E1756E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93130 Genomic RNA. Translation: AAA99437.1.
PIRiA34774. GNWVD3.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93130 Genomic RNA. Translation: AAA99437.1.
PIRiA34774. GNWVD3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UZGX-ray3.60A/B281-672[»]
2J7UX-ray1.85A2762-3390[»]
2J7WX-ray2.60A2762-3390[»]
3P8ZX-ray1.70A/C2491-2752[»]
3P97X-ray1.70A/C2491-2752[»]
3UZEX-ray2.04C/D573-673[»]
3VTTX-ray1.70A/B574-678[»]
5CCVX-ray3.60A/B/C/D/E/F/G/H2491-3390[»]
ProteinModelPortaliP27915.
SMRiP27915.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP27915.
PROiP27915.

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_DEN3P
AccessioniPrimary (citable) accession number: P27915
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 30, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.