SubmitCancel

Skip Header

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

P27915

- POLG_DEN3P

UniProt

P27915 - POLG_DEN3P

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Genome polyprotein
Gene
N/A
Organism
Dengue virus type 3 (strain Philippines/H87/1956) (DENV-3)
Status
Reviewed - 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 Reviewed prediction.
Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By 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 By similarity.
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.

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).
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
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
Sitei100 – 1012Cleavage; by viral protease NS3 Reviewed prediction
Sitei114 – 1152Cleavage; by host signal peptidase By similarity
Sitei205 – 2062Cleavage; by host furin Reviewed prediction
Sitei280 – 2812Cleavage; by host signal peptidase Reviewed prediction
Sitei773 – 7742Cleavage; by host signal peptidase Reviewed prediction
Sitei1125 – 11262Cleavage; by host By similarity
Sitei1343 – 13442Cleavage; by viral protease NS3 Reviewed prediction
Sitei1473 – 14742Cleavage; by autolysis Reviewed prediction
Active sitei1524 – 15241Charge relay system; for serine protease NS3 activity By similarity
Active sitei1548 – 15481Charge relay system; for serine protease NS3 activity By similarity
Active sitei1608 – 16081Charge relay system; for serine protease NS3 activity By similarity
Sitei2092 – 20932Cleavage; by autolysis Reviewed prediction
Sitei2219 – 22202Cleavage; by viral protease NS3 Reviewed prediction
Sitei2242 – 22432Cleavage; by host signal peptidase Reviewed prediction
Sitei2490 – 24912Cleavage; by viral protease NS3 Reviewed prediction
Binding sitei2504 – 25041mRNA cap By similarity
Binding sitei2507 – 25071mRNA cap; via carbonyl oxygen By similarity
Binding sitei2508 – 25081mRNA cap By similarity
Binding sitei2510 – 25101mRNA cap; via carbonyl oxygen By similarity
Sitei2515 – 25151mRNA cap binding By similarity
Binding sitei2519 – 25191mRNA cap By similarity
Binding sitei2546 – 25461S-adenosyl-L-methionine By similarity
Sitei2551 – 25511Essential for 2'-O-methyltransferase activity By similarity
Binding sitei2576 – 25761S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei2577 – 25771S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei2594 – 25941S-adenosyl-L-methionine By similarity
Binding sitei2595 – 25951S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei2621 – 26211S-adenosyl-L-methionine By similarity
Binding sitei2622 – 26221S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Sitei2636 – 26361Essential for 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Sitei2637 – 26371S-adenosyl-L-methionine binding By similarity
Binding sitei2640 – 26401mRNA cap By similarity
Sitei2670 – 26701Essential for 2'-O-methyltransferase activity By similarity
Binding sitei2701 – 27011mRNA cap By similarity
Binding sitei2703 – 27031mRNA cap By similarity
Sitei2706 – 27061Essential for 2'-O-methyltransferase activity By similarity
Binding sitei2708 – 27081S-adenosyl-L-methionine By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1667 – 16748ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. RNA helicase activity Source: InterPro
  4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  5. double-stranded RNA binding Source: InterPro
  6. mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-EC
  7. mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB-EC
  8. metal ion binding Source: UniProtKB-KW
  9. serine-type endopeptidase activity Source: InterPro
  10. serine-type exopeptidase activity Source: InterPro
  11. structural molecule activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB-KW
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. suppression by virus of host STAT2 activity Source: UniProtKB-KW
  6. suppression by virus of host TYK2 activity Source: UniProtKB-KW
  7. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
  8. transcription, DNA-templated Source: UniProtKB-KW
  9. viral RNA genome replication Source: InterPro
  10. virion attachment to host cell Source: UniProtKB-KW
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

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 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]
ProteomesiUP000007200: Genome

Subcellular locationi

Chain Capsid protein C : Virion Reviewed prediction
Chain Peptide pr : Secreted By similarity
Chain Serine protease NS3 : Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity
Note: Remains non-covalently associated to NS3 protease By similarity.
Chain Non-structural protein 4A : Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity
Note: Located in RE-associated vesicles hosting the replication complex.
Chain RNA-directed RNA polymerase NS5 : Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Host nucleus By similarity
Note: Located in RE-associated vesicles hosting the replication complex.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 100100Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei101 – 11818Helical; Reviewed prediction
Add
BLAST
Topological domaini119 – 243125Extracellular Reviewed prediction
Add
BLAST
Transmembranei244 – 26421Helical; Reviewed prediction
Add
BLAST
Topological domaini265 – 2651Cytoplasmic Reviewed prediction
Transmembranei266 – 28015Helical; Reviewed prediction
Add
BLAST
Topological domaini281 – 723443Extracellular Reviewed prediction
Add
BLAST
Intramembranei724 – 74421Helical; Reviewed prediction
Add
BLAST
Topological domaini745 – 7506Extracellular Reviewed prediction
Intramembranei751 – 77121Helical; Reviewed prediction
Add
BLAST
Topological domaini772 – 1123352Extracellular Reviewed prediction
Add
BLAST
Transmembranei1124 – 114421Helical; Reviewed prediction
Add
BLAST
Topological domaini1145 – 115410Cytoplasmic Reviewed prediction
Transmembranei1155 – 117521Helical; Reviewed prediction
Add
BLAST
Topological domaini1176 – 119621Lumenal Reviewed prediction
Add
BLAST
Transmembranei1197 – 121721Helical; Reviewed prediction
Add
BLAST
Topological domaini1218 – 128265Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1283 – 130321Helical; Reviewed prediction
Add
BLAST
Topological domaini1304 – 131512Lumenal Reviewed prediction
Add
BLAST
Transmembranei1316 – 133621Helical; Reviewed prediction
Add
BLAST
Topological domaini1337 – 13448Cytoplasmic Reviewed prediction
Transmembranei1345 – 136521Helical; Reviewed prediction
Add
BLAST
Topological domaini1366 – 13683Lumenal Reviewed prediction
Transmembranei1369 – 138921Helical; Reviewed prediction
Add
BLAST
Topological domaini1390 – 144354Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1444 – 146421Helical; Reviewed prediction
Add
BLAST
Topological domaini1465 – 2146682Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2147 – 216721Helical; Reviewed prediction
Add
BLAST
Topological domaini2168 – 21692Lumenal Reviewed prediction
Intramembranei2170 – 219021Helical; Reviewed prediction
Add
BLAST
Topological domaini2191 – 21911Lumenal Reviewed prediction
Transmembranei2192 – 221221Helical; Reviewed prediction
Add
BLAST
Topological domaini2213 – 222715Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2228 – 224821Helical; Note=Signal for NS4B; Reviewed prediction
Add
BLAST
Topological domaini2249 – 227325Lumenal Reviewed prediction
Add
BLAST
Intramembranei2274 – 229421Helical; Reviewed prediction
Add
BLAST
Topological domaini2295 – 230511Lumenal Reviewed prediction
Add
BLAST
Intramembranei2306 – 232621Helical; Reviewed prediction
Add
BLAST
Topological domaini2327 – 234620Lumenal Reviewed prediction
Add
BLAST
Transmembranei2347 – 236721Helical; Reviewed prediction
Add
BLAST
Topological domaini2368 – 241245Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2413 – 243321Helical; Reviewed prediction
Add
BLAST
Topological domaini2434 – 245825Lumenal Reviewed prediction
Add
BLAST
Transmembranei2459 – 247921Helical; Reviewed prediction
Add
BLAST
Topological domaini2480 – 3390911Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. host cell nucleus Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. viral capsid Source: UniProtKB-KW
  5. viral envelope Source: UniProtKB-KW
  6. virion membrane Source: UniProtKB-SubCell
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 – 33903390Genome polyprotein
PRO_0000405221Add
BLAST
Chaini1 – 100100Capsid protein C By similarity
PRO_0000037989Add
BLAST
Propeptidei101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000037990Add
BLAST
Chaini115 – 280166prM By similarity
PRO_0000308293Add
BLAST
Chaini115 – 20591Peptide pr By similarity
PRO_0000308294Add
BLAST
Chaini206 – 28075Small envelope protein M By similarity
PRO_0000037991Add
BLAST
Chaini281 – 773493Envelope protein E By similarity
PRO_0000037992Add
BLAST
Chaini774 – 1125352Non-structural protein 1 By similarity
PRO_0000037993Add
BLAST
Chaini1126 – 1343218Non-structural protein 2A By similarity
PRO_0000037994Add
BLAST
Chaini1126 – 1313188Non-structural protein 2A-alpha By similarity
PRO_0000308295Add
BLAST
Chaini1344 – 1473130Serine protease subunit NS2B By similarity
PRO_0000037995Add
BLAST
Chaini1474 – 2092619Serine protease NS3 By similarity
PRO_0000037996Add
BLAST
Chaini2093 – 2219127Non-structural protein 4A By similarity
PRO_0000037997Add
BLAST
Peptidei2220 – 224223Peptide 2k By similarity
PRO_0000308296Add
BLAST
Chaini2243 – 2490248Non-structural protein 4B By similarity
PRO_0000037998Add
BLAST
Chaini2491 – 3390900RNA-directed RNA polymerase NS5 By similarity
PRO_0000037999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi283 ↔ 310 By similarity
Disulfide bondi340 ↔ 401 By similarity
Glycosylationi347 – 3471N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi354 ↔ 385 By similarity
Disulfide bondi372 ↔ 396 By similarity
Glycosylationi433 – 4331N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi463 ↔ 563 By similarity
Disulfide bondi580 ↔ 611 By similarity
Glycosylationi903 – 9031N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi980 – 9801N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi2300 – 23001N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi2304 – 23041N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi2456 – 24561N-linked (GlcNAc...); by host Reviewed prediction

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.

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

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni282 – 2854
Beta strandi287 – 2937
Beta strandi301 – 3055
Beta strandi310 – 3156
Beta strandi318 – 32710
Beta strandi334 – 3374
Beta strandi343 – 3519
Helixi363 – 3664
Beta strandi368 – 37912
Turni381 – 3844
Beta strandi389 – 40416
Beta strandi406 – 4094
Beta strandi415 – 4239
Beta strandi434 – 4363
Beta strandi438 – 4436
Beta strandi448 – 4536
Turni454 – 4563
Beta strandi457 – 4626
Beta strandi473 – 4797
Beta strandi482 – 4876
Helixi488 – 4936
Beta strandi503 – 5053
Helixi512 – 5143
Beta strandi517 – 5193
Beta strandi521 – 5244
Beta strandi527 – 5293
Helixi535 – 5417
Beta strandi543 – 5453
Beta strandi561 – 5666
Beta strandi577 – 5793
Beta strandi584 – 5863
Beta strandi594 – 5963
Beta strandi598 – 6047
Beta strandi610 – 6123
Beta strandi615 – 6184
Beta strandi628 – 6314
Beta strandi635 – 6373
Beta strandi643 – 6486
Beta strandi651 – 66111
Beta strandi665 – 6717
Helixi2499 – 250911
Helixi2512 – 25198
Turni2520 – 25223
Beta strandi2524 – 25274
Helixi2529 – 25368
Helixi2548 – 255710
Beta strandi2565 – 25717
Helixi2576 – 25827
Beta strandi2587 – 25937
Turni2609 – 26124
Beta strandi2613 – 26175
Helixi2622 – 26243
Beta strandi2631 – 26355
Helixi2644 – 265815
Helixi2659 – 26613
Beta strandi2666 – 26727
Helixi2677 – 269014
Beta strandi2693 – 26953
Beta strandi2707 – 27126
Helixi2717 – 273014
Beta strandi2733 – 27353
Beta strandi2740 – 27434

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP27915.
SMRiP27915. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.

Miscellaneous databases

EvolutionaryTraceiP27915.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1474 – 1651178Peptidase S7
Add
BLAST
Domaini1654 – 1810157Helicase ATP-binding
Add
BLAST
Domaini1821 – 1986166Helicase C-terminal
Add
BLAST
Domaini2492 – 2753262mRNA cap 0-1 NS5-type MT
Add
BLAST
Domaini3018 – 3168151RdRp catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein C By similarity
Add
BLAST
Regioni1396 – 143540Interacts with and activates NS3 protease By similarity
Add
BLAST

Motif

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

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.
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.
IPR027287. Flavovir_Ig-like.
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.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
[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.
PF00271. Helicase_C. 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

MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSRGLLNG QGPMKLVMAF     50
IAFLRFLAIP PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK 100
TSLCLMMMLP ATLAFHLTSR DGEPRMIVGK NERGKSLLFK TASGINMCTL 150
IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC WCNLTSTWVT YGTCNQAGEH 200
RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW ALRHPGFTIL 250
ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW 300
VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT 350
DSRCPTQGEA ILPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ 400
CLESIEGKVV QHENLKYTVI ITVHTGDQHQ VGNETQGVTA EITSQASTAE 450
AILPEYGTLG LECSPRTGLD FNEMILLTMK NKAWMVHRQW FFDLPLPWTS 500
GATTKTPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT ALTGATEIQT 550
SGGTSIFAGH LKCRLKMDKL KLKGMSYAMC LNTFVLKKEV SETQHGTILI 600
KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP 650
FGESNIVIGI GDKALKINWY RKGSSIGKMF EATARGARRM AILGDTAWDF 700
GSVGGVLNSL GKMVHQIFGS AYTALFSGVS WIMKIGIGVL LTWIGLNSKN 750
TSMSFSCIAI GIITLYLGVV VQADMGCVIN WKGKELKCGS GIFVTNEVHT 800
WTEQYKFQAD SPKRVATAIA GAWENGVCGI RSTTRMENLL WKQIANELNY 850
ILWENDIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGLAKIVTAE 900
TQNSSFIIDG PSTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ 950
LCDHRLMSAA VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK 1000
SHTLWSNGVL ESDMIIPKSL AGPISQHNHR PGYHTQTAGP WHLGKLELDF 1050
NYCEGTTVVI SENCGTRGPS LRTTTVSGKL IHEWCCRSCT LPPLRYMGED 1100
GCWYGMEIRP INEKEENMVK SLASAGSGKV DNFTMGVLCL AILFEEVMRG 1150
KFGKKHMIAG VLFTFVLLLS GQITWRGMAH TLIMIGSNAS DRMGMGVTYL 1200
ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMAATLR LPEDIEQMAN 1250
GIALGLMALK LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGI 1300
SLLPVCQSSS MRKTDWLPMT VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG 1350
VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL LIACYVITGT SADLTVEKAA 1400
DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV LLKTALLIVS 1450
GIFPYSIPAT MLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ 1500
QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI 1550
SYGGGWRLSA QWQKGEEVQV IAVEPGKNPK NFQTMPGIFQ TTTGEIGAIA 1600
LDFKPGTSGS PIINREGKVV GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP 1650
ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA IVREAIKRRL RTLILAPTRV 1700
VAAEMEEAMK GLPIRYQTTA TKSEHTGREI VDLMCHATFT MRLLSPVRVP 1750
NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP 1800
QSNAPIQDEE RDIPERSWNS GNEWITDFVG KTVWFVPSIK AGNVIANCLR 1850
KNGKKVIQLS RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FIADRVIDPR 1900
RCLKPVILTD GPERVILAGP MPVTVASAAQ RRGRVGRNPQ KENDQYIFMG 1950
QPLNKDEDHA HWTEAKMLLD NINTPEGIIP ALFEPEREKS AAIDGEYRLK 2000
GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG ERNNQILEEN 2050
MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT 2100
EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL 2150
GLMILLTGGA MLFLISGKGI GKTSIGLICV IASSGMLWMA DVPLQWIASA 2200
IVLEFFMMVL LIPEPEKQRT PQDNQLAYVV IGILTLAAIV AANEMGLLET 2250
TKRDLGMSKE PGVVSPTSYL DVDLHPASAW TLYAVATTVI TPMLRHTIEN 2300
STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC YSQVNPLTLI 2350
AAVLLLVTHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV 2400
IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEVLTLAT GPITTLWEGS 2450
PGKFWNTTIA VSMANIFRGS YLAGAGLALS IMKSVGTGKR GTGSQGETLG 2500
EKWKKKLNQL SRKEFDLYKK SGITEVDRTE AKEGLKRGEI THHAVSRGSA 2550
KLQWFVERNM VIPEGRVIDL GCGRGGWSYY CAGLKKVTEV RGYTKGGPGH 2600
EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES SPSPTVEESR 2650
TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS 2700
RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG 2750
TRHVNAEPET PNMDVIGERI KRIKEEHSST WHYDDENPYK TWAYHGSYEV 2800
KATGSASSMI NGVVKLLTKP WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT 2850
RTPRPMPGTR KVMEITAEWL WRTLGRNKRP RLCTREEFTK KVRTNAAMGA 2900
VFTEENQWDS ARAAVEDEEF WKLVDREREL HKLGKCGSCV YNMMGKREKK 2950
LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG 3000
LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH 3050
RQLANAIFKL TYQNKVVKVQ RPTPKGTVMD IISRKDQRGS GQVGTYGLNT 3100
FTNMEAQLIR QMEGEGVLSK ADLENPHPLE KKITQWLETK GVERLKRMAI 3150
SGDDCVVKPI DDRFANALLA LNDMGKVRKD IPQWQPSKGW HDWQQVPFCS 3200
HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE TACLGKAYAQ 3250
MWTLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML 3300
TVWNRVWIED NPWMEDKTPV TTWEDVPYLG KREDQWCGSL IGLTSRATWA 3350
QNILTAIQQV RSLIGNEEFL DYMPSMKRFR KEEESEGAIW 3390
Length:3,390
Mass (Da):378,063
Last modified:August 1, 1992 - v1
Checksum:i666E8F70F1E1756E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93130 Genomic RNA. Translation: AAA99437.1.
PIRiA34774. GNWVD3.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93130 Genomic RNA. Translation: AAA99437.1 .
PIRi A34774. GNWVD3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UZG X-ray 3.60 A/B 281-672 [» ]
2J7U X-ray 1.85 A 2762-3390 [» ]
2J7W X-ray 2.60 A 2762-3390 [» ]
3P8Z X-ray 1.70 A/C 2491-2752 [» ]
3P97 X-ray 1.70 A/C 2491-2752 [» ]
3UZE X-ray 2.04 C/D 573-673 [» ]
3VTT X-ray 1.70 A/B 574-678 [» ]
ProteinModelPortali P27915.
SMRi P27915. Positions 21-100, 281-672, 1493-2092, 2497-2757, 2763-3373.
ModBasei Search...

Protein family/group databases

MEROPSi S07.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P27915.
PROi P27915.

Family and domain databases

Gene3Di 2.60.40.350. 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.
InterProi IPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
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.
IPR027287. Flavovir_Ig-like.
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.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view ]
PIRSFi PIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsi TIGR04240. flavi_E_stem. 1 hit.
PROSITEi PS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete nucleotide sequence of dengue type 3 virus genome RNA."
    Osatomi K., Sumiyoshi H.
    Virology 176:643-647(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], PARTIAL PROTEIN SEQUENCE.
  2. "Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein."
    Modis Y., Ogata S., Clements D., Harrison S.C.
    J. Virol. 79:1223-1231(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 281-672.

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: June 11, 2014
This is version 134 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

External Data

Dasty 3

Similar proteinsi