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Protein

Genome polyprotein

Gene
N/A
Organism
Yellow fever virus (strain 17D vaccine) (YFV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1537 – 15371Charge relay system; for serine protease NS3 activity
Active sitei1561 – 15611Charge relay system; for serine protease NS3 activity
Active sitei1622 – 16221Charge relay system; for serine protease NS3 activity
Binding sitei2519 – 25191mRNA cap
Binding sitei2522 – 25221mRNA cap; via carbonyl oxygen
Binding sitei2523 – 25231mRNA cap
Binding sitei2525 – 25251mRNA cap; via carbonyl oxygen
Sitei2530 – 25301mRNA cap binding
Binding sitei2534 – 25341mRNA cap
Binding sitei2562 – 25621S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2567 – 25671Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2592 – 25921S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2593 – 25931S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2610 – 26101S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2611 – 26111S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2637 – 26371S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2638 – 26381S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2652 – 26521Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2653 – 26531S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2656 – 26561mRNA cap
Sitei2688 – 26881Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2719 – 27191mRNA cap
Binding sitei2721 – 27211mRNA cap
Sitei2724 – 27241Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2726 – 27261S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1682 – 16898ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Activation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, mRNA capping, mRNA processing, Transcription, Transcription regulation, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.7.50. 6740.
3.6.4.13. 6740.

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
OrganismiYellow fever virus (strain 17D vaccine) (YFV)
Taxonomic identifieri11090 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusYellow fever virus group
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes luteocephalus (Mosquito) [TaxID: 299629]
Aedes simpsoni [TaxID: 7161]
Homo sapiens (Human) [TaxID: 9606]
Simiiformes [TaxID: 314293]
Proteomesi
  • UP000000360 Componenti: Genome

Subcellular locationi

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

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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 104104CytoplasmicSequence analysisAdd
BLAST
Transmembranei105 – 12521HelicalSequence analysisAdd
BLAST
Topological domaini126 – 244119ExtracellularSequence analysisAdd
BLAST
Transmembranei245 – 26521HelicalSequence analysisAdd
BLAST
Topological domaini266 – 2705CytoplasmicSequence analysis
Transmembranei271 – 28515HelicalSequence analysisAdd
BLAST
Topological domaini286 – 730445ExtracellularSequence analysisAdd
BLAST
Intramembranei731 – 75121HelicalSequence analysisAdd
BLAST
Topological domaini752 – 7576ExtracellularSequence analysis
Intramembranei758 – 77821HelicalSequence analysisAdd
BLAST
Topological domaini779 – 1130352ExtracellularSequence analysisAdd
BLAST
Transmembranei1131 – 115121HelicalSequence analysisAdd
BLAST
Topological domaini1152 – 11609CytoplasmicSequence analysis
Transmembranei1161 – 118121HelicalSequence analysisAdd
BLAST
Topological domaini1182 – 120120LumenalSequence analysisAdd
BLAST
Transmembranei1202 – 122221HelicalSequence analysisAdd
BLAST
Topological domaini1223 – 12319CytoplasmicSequence analysis
Transmembranei1232 – 125221HelicalSequence analysisAdd
BLAST
Topological domaini1253 – 126210LumenalSequence analysis
Transmembranei1263 – 128523HelicalSequence analysisAdd
BLAST
Topological domaini1286 – 135570CytoplasmicSequence analysisAdd
BLAST
Transmembranei1356 – 137621HelicalSequence analysisAdd
BLAST
Topological domaini1377 – 13782LumenalSequence analysis
Transmembranei1379 – 139921HelicalSequence analysisAdd
BLAST
Topological domaini1400 – 145657CytoplasmicSequence analysisAdd
BLAST
Intramembranei1457 – 147721HelicalSequence analysisAdd
BLAST
Topological domaini1478 – 2157680CytoplasmicSequence analysisAdd
BLAST
Transmembranei2158 – 217821HelicalSequence analysisAdd
BLAST
Topological domaini2179 – 21868LumenalSequence analysis
Intramembranei2187 – 220721HelicalSequence analysisAdd
BLAST
Topological domaini2208 – 22092LumenalSequence analysis
Transmembranei2210 – 223021HelicalSequence analysisAdd
BLAST
Topological domaini2231 – 224111CytoplasmicSequence analysisAdd
BLAST
Transmembranei2242 – 226221Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2263 – 229331LumenalSequence analysisAdd
BLAST
Intramembranei2294 – 231421HelicalSequence analysisAdd
BLAST
Topological domaini2315 – 233824LumenalSequence analysisAdd
BLAST
Intramembranei2339 – 235921HelicalSequence analysisAdd
BLAST
Topological domaini2360 – 23601LumenalSequence analysis
Transmembranei2361 – 238020HelicalSequence analysisAdd
BLAST
Topological domaini2381 – 242141CytoplasmicSequence analysisAdd
BLAST
Transmembranei2422 – 244221HelicalSequence analysisAdd
BLAST
Topological domaini2443 – 24453LumenalSequence analysis
Transmembranei2446 – 246621HelicalSequence analysisAdd
BLAST
Topological domaini2467 – 3411945CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi98 – 1014RKRR → AAAA: Complete loss of NS2B-NS3 cleavage.
Mutagenesisi98 – 1014RKRR → AKAA: Complete loss of NS2B-NS3 cleavage.
Mutagenesisi98 – 1014RKRR → AKRA: Reduces NS2B-NS3 cleavage efficiency.
Mutagenesisi98 – 1003RKR → AAA: Complete loss of NS2B-NS3 cleavage.
Mutagenesisi98 – 1003RKR → AKA: Complete loss of NS2B-NS3 cleavage.
Mutagenesisi98 – 992RK → AA: Reduces NS2B-NS3 cleavage efficiency.
Mutagenesisi99 – 1013KRR → ARA: Complete loss of NS2B-NS3 cleavage. 1 Publication
Mutagenesisi99 – 1002KR → AA: Complete loss of NS2B-NS3 cleavage.
Mutagenesisi100 – 1012RR → AA: Reduces NS2B-NS3 cleavage efficiency.
Mutagenesisi116 – 1216LLMTGG → VPQAQA: Complete loss of infectious virus production. Enhances signal peptidase cleavage in vitro of nascent protein C. 1 Publication
Mutagenesisi908 – 9081N → A: Reduces viral RNA accumulation and NS1 secretion. 1 Publication
Mutagenesisi910 – 9101S → A: Reduces viral RNA accumulation and NS1 secretion. 1 Publication
Mutagenesisi986 – 9861N → A: No effect. 1 Publication
Mutagenesisi988 – 9881T → A: No effect. 1 Publication
Mutagenesisi1077 – 10771R → A: Blocks RNA replication. 1 Publication
Mutagenesisi1319 – 13213QKT → RRS: Increases NS2A-alpha processing, complete loss of NS2A.
Mutagenesisi1319 – 13191Q → S: Complete loss of cleavage and NS2A alpha. Complete loss of infectivity. 1 Publication
Mutagenesisi1320 – 13201K → E, I, Q or S: Complete loss of cleavage and NS2A-alpha processing. Complete loss of infectivity. 1 Publication
Mutagenesisi1320 – 13201K → R: No effect on NS2A-alpha processing. 1 Publication
Mutagenesisi1321 – 13211T → V: Complete loss of cleavage and NS2A alpha synthesis. Complete loss of infectivity. 1 Publication
Mutagenesisi1351 – 13511F → C, I or V: Enhances NS2A-NS2B cleavage efficiency. 1 Publication
Mutagenesisi1351 – 13511F → G: No effect on NS2A-NS2B cleavage efficiency. 1 Publication
Mutagenesisi1352 – 13521G → A or K: Enhances NS2A-NS2B cleavage efficiency. 1 Publication
Mutagenesisi1352 – 13521G → E or V: Reduces NS2A-NS2B cleavage efficiency. 1 Publication
Mutagenesisi1353 – 13531R → H, K, R or T: Reduces NS2A-NS2B cleavage efficiency. 1 Publication
Mutagenesisi1353 – 13531R → L or P: Complete loss of NS2A-NS2B cleavage. 1 Publication
Mutagenesisi1354 – 13541R → I, N, S or T: Complete loss of NS2A-NS2B cleavage. 1 Publication
Mutagenesisi1354 – 13541R → K: Reduces of NS2A-NS2B cleavage efficiency. 1 Publication
Mutagenesisi1355 – 13551S → D, K, R or V: Complete loss of NS2A-NS2B cleavage. 1 Publication
Mutagenesisi1355 – 13551S → G: Reduces of NS2A-NS2B cleavage efficiency. 1 Publication
Mutagenesisi1406 – 14094ELKK → ALAA: Complete loss of polyprotein cleavage. 1 Publication
Mutagenesisi1537 – 15371H → A: Complete loss NS3 protease activity. 1 Publication
Mutagenesisi1561 – 15611D → A or N: Complete loss NS3 protease activity. 1 Publication
Mutagenesisi1622 – 16221S → A: Complete loss NS3 protease activity. 1 Publication
Mutagenesisi1622 – 16221S → C: Diminishes NS3 protease activity. 1 Publication
Mutagenesisi2107 – 21071R → A, L, M, T or V: Reduces NS4A-NS4B cleavage efficiency. 1 Publication
Mutagenesisi2107 – 21071R → E or P: Complete loss of NS4A-NS4B cleavage. 1 Publication
Mutagenesisi2107 – 21071R → K: No effect on NS4A-NS4B cleavage efficiency. 1 Publication
Mutagenesisi2505 – 25051R → A, I, L, Q, S or T: No effect on NS4B-NS5 cleavage efficiency. 1 Publication
Mutagenesisi2505 – 25051R → P: Reduces NS4B-NS5 cleavage efficiency. 1 Publication
Mutagenesisi2506 – 25061R → E or Y: Complete loss of NS4B-NS5 cleavage. 1 Publication
Mutagenesisi2506 – 25061R → H, N or Q: Reduces NS4B-NS5 cleavage efficiency. 1 Publication
Mutagenesisi2506 – 25061R → K: No effect on NS4B-NS5 cleavage efficiency. 1 Publication
Mutagenesisi2507 – 25071G → A or S: Reduces NS4B-NS5 cleavage efficiency.
Mutagenesisi2507 – 25071G → E, K, L, M, N or V: Reduces NS4B-NS5 cleavage efficiency.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 34113411Genome polyproteinPRO_0000405153Add
BLAST
Chaini1 – 101101Capsid protein CBy similarityPRO_0000037754Add
BLAST
Propeptidei102 – 12120ER anchor for the protein C, removed in mature form by serine protease NS3PRO_0000261384Add
BLAST
Chaini122 – 285164prMBy similarityPRO_0000261385Add
BLAST
Chaini122 – 21089Peptide prBy similarityPRO_0000037755Add
BLAST
Chaini211 – 28575Small envelope protein MBy similarityPRO_0000037756Add
BLAST
Chaini286 – 778493Envelope protein EBy similarityPRO_0000037757Add
BLAST
Chaini779 – 1130352Non-structural protein 1By similarityPRO_0000037758Add
BLAST
Chaini1131 – 1354224Non-structural protein 2ABy similarityPRO_0000037759Add
BLAST
Chaini1131 – 1320190Non-structural protein 2A-alphaBy similarityPRO_0000261386Add
BLAST
Chaini1355 – 1484130Serine protease subunit NS2BBy similarityPRO_0000037760Add
BLAST
Chaini1485 – 2107623Serine protease NS3By similarityPRO_0000037761Add
BLAST
Chaini2108 – 2233126Non-structural protein 4ABy similarityPRO_0000037762Add
BLAST
Peptidei2234 – 225623Peptide 2k1 PublicationPRO_0000261387Add
BLAST
Chaini2257 – 2506250Non-structural protein 4BBy similarityPRO_0000037763Add
BLAST
Chaini2507 – 3411905RNA-directed RNA polymerase NS5By similarityPRO_0000037764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi134 – 1341N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi150 – 1501N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi288 ↔ 315By similarity
Disulfide bondi345 ↔ 401By similarity
Disulfide bondi359 ↔ 390By similarity
Disulfide bondi377 ↔ 406By similarity
Disulfide bondi467 ↔ 568By similarity
Disulfide bondi585 ↔ 615By similarity
Glycosylationi908 – 9081N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi986 – 9861N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.1 Publication
Envelope protein E and non-structural protein 1 are N-glycosylated.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei101 – 1022Cleavage; by viral protease NS3Sequence analysis
Sitei121 – 1222Cleavage; by host signal peptidaseBy similarity
Sitei210 – 2112Cleavage; by host furinSequence analysis
Sitei285 – 2862Cleavage; by host signal peptidaseSequence analysis
Sitei778 – 7792Cleavage; by host signal peptidaseSequence analysis
Sitei1130 – 11312Cleavage; by hostSequence analysis
Sitei1354 – 13552Cleavage; by viral protease NS3Sequence analysis
Sitei1484 – 14852Cleavage; by autolysisSequence analysis
Sitei2107 – 21082Cleavage; by autolysisSequence analysis
Sitei2233 – 22342Cleavage; by viral protease NS3Sequence analysis
Sitei2256 – 22572Cleavage; by host signal peptidaseSequence analysis
Sitei2506 – 25072Cleavage; by viral protease NS3Sequence analysis

Keywords - PTMi

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

Proteomic databases

PRIDEiP03314.

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.By similarity

Structurei

Secondary structure

1
3411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1677 – 16804Combined sources
Turni1688 – 16914Combined sources
Helixi1692 – 170211Combined sources
Beta strandi1707 – 17137Combined sources
Helixi1714 – 172310Combined sources
Turni1724 – 17263Combined sources
Beta strandi1729 – 17313Combined sources
Beta strandi1746 – 17505Combined sources
Helixi1751 – 17588Combined sources
Beta strandi1760 – 17623Combined sources
Beta strandi1768 – 17725Combined sources
Turni1773 – 17764Combined sources
Helixi1780 – 179415Combined sources
Beta strandi1799 – 18035Combined sources
Beta strandi1821 – 18255Combined sources
Beta strandi1834 – 18363Combined sources
Helixi1839 – 18424Combined sources
Beta strandi1847 – 18504Combined sources
Helixi1854 – 186613Combined sources
Beta strandi1871 – 18733Combined sources
Beta strandi1876 – 18783Combined sources
Beta strandi1892 – 18998Combined sources
Beta strandi1909 – 19135Combined sources
Beta strandi1916 – 19238Combined sources
Turni1924 – 19274Combined sources
Beta strandi1928 – 19369Combined sources
Helixi1939 – 19468Combined sources
Beta strandi1958 – 19625Combined sources
Helixi1974 – 198310Combined sources
Helixi1989 – 19913Combined sources
Helixi2000 – 20034Combined sources
Beta strandi2004 – 20063Combined sources
Turni2008 – 20114Combined sources
Helixi2015 – 202612Combined sources
Helixi2032 – 20409Combined sources
Helixi2049 – 20513Combined sources
Helixi2056 – 20583Combined sources
Beta strandi2063 – 20653Combined sources
Beta strandi2069 – 20713Combined sources
Beta strandi2077 – 20793Combined sources
Beta strandi2083 – 20864Combined sources
Helixi2087 – 20893Combined sources
Beta strandi2090 – 20923Combined sources
Helixi2093 – 210311Combined sources
Turni2104 – 21063Combined sources
Helixi2514 – 252411Combined sources
Helixi2527 – 25348Combined sources
Beta strandi2536 – 25416Combined sources
Helixi2544 – 25518Combined sources
Helixi2564 – 257310Combined sources
Beta strandi2581 – 25866Combined sources
Helixi2592 – 25987Combined sources
Beta strandi2603 – 26097Combined sources
Helixi2627 – 26293Combined sources
Beta strandi2630 – 26334Combined sources
Turni2638 – 26403Combined sources
Beta strandi2647 – 26515Combined sources
Helixi2660 – 267819Combined sources
Turni2679 – 26813Combined sources
Beta strandi2683 – 26908Combined sources
Helixi2695 – 270814Combined sources
Beta strandi2711 – 27133Combined sources
Beta strandi2725 – 27306Combined sources
Helixi2735 – 275117Combined sources
Beta strandi2757 – 27604Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NA4electron microscopy-
1YKSX-ray1.80A1671-2107[»]
3EVAX-ray1.50A2507-2772[»]
3EVBX-ray1.85A2507-2772[»]
3EVCX-ray1.60A2507-2772[»]
3EVDX-ray1.50A2507-2772[»]
3EVEX-ray1.70A2507-2772[»]
3EVFX-ray1.45A2507-2772[»]
5FFMX-ray2.60A1671-2107[»]
ProteinModelPortaliP03314.
SMRiP03314. Positions 572-683, 1504-1653, 1671-2107, 2512-2772, 2780-3399.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03314.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1485 – 1665181Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1669 – 1825157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1820 – 1997178Helicase C-terminalAdd
BLAST
Domaini2507 – 2771265mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3035 – 3187153RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 7445Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni383 – 39614Involved in fusionAdd
BLAST
Regioni1407 – 144640Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1773 – 17764DEAH box
Motifi2878 – 291134Nuclear localization signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2656 – 26605Poly-Ser

Domaini

Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals.

Sequence similaritiesi

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.Curated
Contains 1 mRNA cap 0-1 NS5-type MT domain.PROSITE-ProRule annotation
Contains 1 peptidase S7 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

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.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF
60 70 80 90 100
FLFNILTGKK ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR
110 120 130 140 150
RSHDVLTVQF LILGMLLMTG GVTLVRKNRW LLLNVTSEDL GKTFSVGTGN
160 170 180 190 200
CTTNILEAKY WCPDSMEYNC PNLSPREEPD DIDCWCYGVE NVRVAYGKCD
210 220 230 240 250
SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ KIERWFVRNP
260 270 280 290 300
FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
310 320 330 340 350
HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDRPAE VRKVCYNAVL
360 370 380 390 400
THVKINDKCP STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA
410 420 430 440 450
CAKFTCAKSM SLFEVDQTKI QYVIRAQLHV GAKQENWNTD IKTLKFDALS
460 470 480 490 500
GSQEVEFIGY GKATLECQVQ TAVDFGNSYI AEMETESWIV DRQWAQDLTL
510 520 530 540 550
PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK TALTGAMRVT
560 570 580 590 600
KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKICTDKMF FVKNPTDTGH
610 620 630 640 650
GTVVMQVKVS KGAPCRIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI
660 670 680 690 700
EVNPPFGDSY IIVGRGDSRL TYQWHKEGSS IGKLFTQTMK GVERLAVMGD
710 720 730 740 750
TAWDFSSAGG FFTSVGKGIH TVFGSAFQGL FGGLNWITKV IMGAVLIWVG
760 770 780 790 800
INTRNMTMSM SMILVGVIMM FLSLGVGADQ GCAINFGKRE LKCGDGIFIF
810 820 830 840 850
RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS LEHEMWRSRA
860 870 880 890 900
DEINAIFEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL
910 920 930 940 950
VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV
960 970 980 990 1000
FEYTIDCDGS ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK
1010 1020 1030 1040 1050
ECEWPLTHTI GTSVEESEMF MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP
1060 1070 1080 1090 1100
LEVKREACPG TSVIIDGNCD GRGKSTRSTT DSGKVIPEWC CRSCTMPPVS
1110 1120 1130 1140 1150
FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL VSMMIAMEVV
1160 1170 1180 1190 1200
LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD
1210 1220 1230 1240 1250
AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGVMG
1260 1270 1280 1290 1300
GLWKYLNAVS LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLAAMFF
1310 1320 1330 1340 1350
CAVVIIGVLH QNFKDTSMQK TIPLVALTLT SYLGLTQPFL GLCAFLATRI
1360 1370 1380 1390 1400
FGRRSIPVNE ALAAAGLVGV LAGLAFQEME NFLGPIAVGG LLMMLVSVAG
1410 1420 1430 1440 1450
RVDGLELKKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL LSEEKVPWDQ
1460 1470 1480 1490 1500
VVMTSLALVG AALHPFALLL VLAGWLFHVR GARRSGDVLW DIPTPKIIEE
1510 1520 1530 1540 1550
CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK
1560 1570 1580 1590 1600
LIPSWASVKE DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS
1610 1620 1630 1640 1650
LFKVRNGGEI GAVALDYPSG TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS
1660 1670 1680 1690 1700
AISQTEVKEE GKEELQEIPT MLKKGMTTVL DFHPGAGKTR RFLPQILAEC
1710 1720 1730 1740 1750
ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG SGREVIDAMC
1760 1770 1780 1790 1800
HATLTYRMLE PTRVVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT
1810 1820 1830 1840 1850
ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF
1860 1870 1880 1890 1900
LPSIRAANVM AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA
1910 1920 1930 1940 1950
EMGANLCVER VLDCRTAFKP VLVDEGRKVA IKGPLRISAS SAAQRRGRIG
1960 1970 1980 1990 2000
RNPNRDGDSY YYSEPTSENN AHHVCWLEAS MLLDNMEVRG GMVAPLYGVE
2010 2020 2030 2040 2050
GTKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK AGLKTNDRKW
2060 2070 2080 2090 2100
CFEGPEEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALSEFI
2110 2120 2130 2140 2150
KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA
2160 2170 2180 2190 2200
LSMMPEAMTI VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL
2210 2220 2230 2240 2250
MFLGGVKPTH ISYVMLIFFV LMVVVIPEPG QQRSIQDNQV AYLIIGILTL
2260 2270 2280 2290 2300
VSAVAANELG MLEKTKEDLF GKKNLIPSSA SPWSWPDLDL KPGAAWTVYV
2310 2320 2330 2340 2350
GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI PFMKMNISVI
2360 2370 2380 2390 2400
MLLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA
2410 2420 2430 2440 2450
ENPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA
2460 2470 2480 2490 2500
EGIVLASAAL GPLIEGNTSL LWNGPMAVSM TGVMRGNHYA FVGVMYNLWK
2510 2520 2530 2540 2550
MKTGRRGSAN GKTLGEVWKR ELNLLDKRQF ELYKRTDIVE VDRDTARRHL
2560 2570 2580 2590 2600
AEGKVDTGVA VSRGTAKLRW FHERGYVKLE GRVIDLGCGR GGWCYYAAAQ
2610 2620 2630 2640 2650
KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR LEPVKCDTLL
2660 2670 2680 2690 2700
CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK
2710 2720 2730 2740 2750
LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM
2760 2770 2780 2790 2800
RRPTGKVTLE ADVILPIGTR SVETDKGPLD KEAIEERVER IKSEYMTSWF
2810 2820 2830 2840 2850
YDNDNPYRTW HYCGSYVTKT SGSAASMVNG VIKILTYPWD RIEEVTRMAM
2860 2870 2880 2890 2900
TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI MKVVNRWLFR HLAREKNPRL
2910 2920 2930 2940 2950
CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE LVDEERKLHQ
2960 2970 2980 2990 3000
QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN
3010 3020 3030 3040 3050
EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT
3060 3070 3080 3090 3100
EADLDDEQEI LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV
3110 3120 3130 3140 3150
ISRRDQRGSG QVVTYALNTI TNLKVQLIRM AEAEMVIHHQ HVQDCDESVL
3160 3170 3180 3190 3200
TRLEAWLTEH GCDRLKRMAV SGDDCVVRPI DDRFGLALSH LNAMSKVRKD
3210 3220 3230 3240 3250
ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE QDELIGRGRV
3260 3270 3280 3290 3300
SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ
3310 3320 3330 3340 3350
GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTMV KKWRDVPYLT
3360 3370 3380 3390 3400
KRQDKLCGSL IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS
3410
VDADLQLGEL I
Length:3,411
Mass (Da):379,518
Last modified:July 21, 1986 - v1
Checksum:i680E0FACD23DCFA6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti341 – 3411V → A in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.
Natural varianti438 – 4381N → T in strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine.
Natural varianti440 – 4401D → S in strain: Isolate 17DD vaccine.
Natural varianti610 – 6101S → P in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.
Natural varianti629 – 6291I → V in strain: Isolate Brazil/YF-VAVD/75 vaccine.
Natural varianti701 – 7011T → V in strain: Isolate 17DD vaccine.
Natural varianti744 – 7441A → V in strain: Isolate 17D-204-South Africa vaccine large plaque variant.
Natural varianti764 – 7641L → M in strain: Isolate 17D-204-South Africa vaccine large plaque variant.
Natural varianti1299 – 12991F → L in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.
Natural varianti1666 – 16661Q → R in strain: Isolate 17DD vaccine.
Natural varianti1669 – 16691P → S in strain: Isolate Brazil/YF-VAVD/75 vaccine.
Natural varianti1679 – 16791V → I in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.
Natural varianti2214 – 22141V → I in strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine.
Natural varianti2277 – 22771P → S in strain: Isolate Brazil/YF-VAVD/75 vaccine.
Natural varianti2401 – 24011E → K in strain: Isolate 17D-204-South Africa vaccine large plaque variant, Isolate 17D-204-South Africa vaccine medium plaque variant, Isolate 17D-204-South Africa vaccine, Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine.
Natural varianti2460 – 24601L → S in strain: Isolate 17D-204-USA HONG vaccine1, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine.
Natural varianti2528 – 25281R → Q in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.
Natural varianti2643 – 26431P → S in strain: Isolate 17D-204-South Africa vaccine medium plaque variant.
Natural varianti2661 – 26611V → I in strain: Isolate Brazil/YF-VAVD/75 vaccine.
Natural varianti2897 – 28971N → S in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine.
Natural varianti3110 – 31101G → R in strain: Isolate 17D-204-USA HONG2 vaccine.
Natural varianti3135 – 31351M → N in strain: Isolate Brazil/YF-VAVD/75 vaccine.
Natural varianti3163 – 31631D → N in strain: Isolate 17D-204-South Africa vaccine large plaque variant, Isolate 17D-204-South Africa vaccine medium plaque variant, Isolate 17D-204-South Africa vaccine, Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine.
Natural varianti3222 – 32221H → R in strain: Isolate Brazil/YF-VAVD/75 vaccine.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03700 Genomic RNA. Translation: CAA27332.1.
X15062 Genomic RNA. Translation: CAB37419.1.
U17066 Genomic RNA. Translation: AAC54267.1.
U17067 Genomic RNA. Translation: AAC54268.1.
AF052437 Genomic RNA. Translation: AAC35899.1.
AF052438 Genomic RNA. Translation: AAC35900.1.
AF052439 Genomic RNA. Translation: AAC35901.1.
AF052444 Genomic RNA. Translation: AAC35906.1.
AF052445 Genomic RNA. Translation: AAC35907.1.
AF052446 Genomic RNA. Translation: AAC35908.1.
DQ118157 Genomic RNA. Translation: AAZ31436.1.
DQ100292 Genomic RNA. Translation: AAZ07885.1.
PIRiA03914. GNWVY.
S07757. GNWVYP.
RefSeqiNP_041726.1. NC_002031.1.

Genome annotation databases

GeneIDi1502173.
KEGGivg:1502173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03700 Genomic RNA. Translation: CAA27332.1.
X15062 Genomic RNA. Translation: CAB37419.1.
U17066 Genomic RNA. Translation: AAC54267.1.
U17067 Genomic RNA. Translation: AAC54268.1.
AF052437 Genomic RNA. Translation: AAC35899.1.
AF052438 Genomic RNA. Translation: AAC35900.1.
AF052439 Genomic RNA. Translation: AAC35901.1.
AF052444 Genomic RNA. Translation: AAC35906.1.
AF052445 Genomic RNA. Translation: AAC35907.1.
AF052446 Genomic RNA. Translation: AAC35908.1.
DQ118157 Genomic RNA. Translation: AAZ31436.1.
DQ100292 Genomic RNA. Translation: AAZ07885.1.
PIRiA03914. GNWVY.
S07757. GNWVYP.
RefSeqiNP_041726.1. NC_002031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NA4electron microscopy-
1YKSX-ray1.80A1671-2107[»]
3EVAX-ray1.50A2507-2772[»]
3EVBX-ray1.85A2507-2772[»]
3EVCX-ray1.60A2507-2772[»]
3EVDX-ray1.50A2507-2772[»]
3EVEX-ray1.70A2507-2772[»]
3EVFX-ray1.45A2507-2772[»]
5FFMX-ray2.60A1671-2107[»]
ProteinModelPortaliP03314.
SMRiP03314. Positions 572-683, 1504-1653, 1671-2107, 2512-2772, 2780-3399.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP03314.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1502173.
KEGGivg:1502173.

Enzyme and pathway databases

BRENDAi2.7.7.50. 6740.
3.6.4.13. 6740.

Miscellaneous databases

EvolutionaryTraceiP03314.

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.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution."
    Rice C.M., Lenches E.M., Eddy S.R., Shin S.J., Sheets R.L., Strauss J.H.
    Science 229:726-733(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Complete nucleotide sequence of yellow fever virus vaccine strains 17DD and 17D-213."
    dos Santos C.N., Post P.R., Carvalho R., Ferreira I.I., Rice C.M., Galler R.
    Virus Res. 35:35-41(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate 17D-213 vaccine and Isolate 17DD vaccine.
  3. "Yellow fever 17D vaccine virus isolated from healthy vaccinees accumulates very few mutations."
    Xie H., Cass A.R., Barrett A.D.T.
    Virus Res. 55:93-99(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine.
  4. "Nucleotide sequence comparison of the genome of two 17D-204 yellow fever vaccines."
    Dupuy A., Despres P., Cahour A., Girard M., Bouloy M.
    Nucleic Acids Res. 17:3989-3989(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Pasteur 17D-204 vaccine.
  5. "Mutation in NS5 protein attenuates mouse neurovirulence of yellow fever 17D vaccine virus."
    Xie H., Ryman K.D., Campbell G.A., Barrett A.D.T.
    J. Gen. Virol. 79:1895-1899(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate 17D-204-South Africa vaccine, Isolate 17D-204-South Africa vaccine large plaque variant and Isolate 17D-204-South Africa vaccine medium plaque variant.
  6. "Yellow fever vaccine-associated viscerotropic disease and death in Spain."
    Doblas A., Domingo C., Bae H.G., Bohorquez C.L., de Ory F., Niedrig M., Mora D., Carrasco F.J., Tenorio A.
    J. Clin. Virol. 36:156-158(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Spain/AVD2791-93F/2004 vaccine.
  7. "Characterization of a viscerotropic yellow fever vaccine variant from a patient in Brazil."
    Engel A.R., Vasconcelos P.F., McArthur M.A., Barrett A.D.
    Vaccine 24:2803-2809(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Brazil/YF-VAVD/1975 vaccine.
  8. "Partial N-terminal amino acid sequences of three nonstructural proteins of two flaviviruses."
    Rice C.M., Aebersold R., Teplow D.B., Pata J., Bell J.R., Vorndam A.V., Trent D.W., Brandriss M.W., Schlesinger J.J., Strauss J.H.
    Virology 151:1-9(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 779-798; 1485-1497 AND 2507-2510.
  9. "Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and partial N-terminal amino acid sequence analysis."
    Chambers T.J., McCourt D.W., Rice C.M.
    Virology 169:100-109(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2257-2276.
  10. "Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein."
    Chambers T.J., Weir R.C., Grakoui A., McCourt D.W., Bazan J.F., Fletterick R.J., Rice C.M.
    Proc. Natl. Acad. Sci. U.S.A. 87:8898-8902(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF NS2B-NS3 PROTEASE, MUTAGENESIS OF HIS-1537; ASP-1561 AND SER-1622.
  11. "Mutagenesis of the yellow fever virus NS2B/3 cleavage site: determinants of cleavage site specificity and effects on polyprotein processing and viral replication."
    Chambers T.J., Nestorowicz A., Rice C.M.
    J. Virol. 69:1600-1605(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF NS2B-NS3 PROTEASE.
  12. "Mutagenesis of conserved residues at the yellow fever virus 3/4A and 4B/5 dibasic cleavage sites: effects on cleavage efficiency and polyprotein processing."
    Lin C., Chambers T.J., Rice C.M.
    Virology 192:596-604(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-2107; ARG-2505 AND ARG-2506.
  13. "Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site."
    Lin C., Amberg S.M., Chambers T.J., Rice C.M.
    J. Virol. 67:2327-2335(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF NS4A/NS4B.
  14. "NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies."
    Amberg S.M., Nestorowicz A., McCourt D.W., Rice C.M.
    J. Virol. 68:3794-3802(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF NS2B-NS3 PROTEASE.
  15. "Mutagenesis of the yellow fever virus NS2A/2B cleavage site: effects on proteolytic processing, viral replication, and evidence for alternative processing of the NS2A protein."
    Nestorowicz A., Chambers T.J., Rice C.M.
    Virology 199:114-123(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-1351; GLY-1352; ARG-1353; ARG-1354 AND SER-1355.
  16. "Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effects on virus replication and mouse neurovirulence."
    Muylaert I.R., Chambers T.J., Galler R., Rice C.M.
    Virology 222:159-168(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-908; SER-910; ASN-986 AND THR-988.
  17. "Genetic analysis of the yellow fever virus NS1 protein: identification of a temperature-sensitive mutation which blocks RNA accumulation."
    Muylaert I.R., Galler R., Rice C.M.
    J. Virol. 71:291-298(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-1077.
  18. "trans-Complementation of yellow fever virus NS1 reveals a role in early RNA replication."
    Lindenbach B.D., Rice C.M.
    J. Virol. 71:9608-9617(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF NS1.
  19. "The NS5A/NS5 proteins of viruses from three genera of the family flaviviridae are phosphorylated by associated serine/threonine kinases."
    Reed K.E., Gorbalenya A.E., Rice C.M.
    J. Virol. 72:6199-6206(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF RNA-DIRECTED RNA POLYMERASE NS5.
  20. "Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a determinant of replicase function."
    Lindenbach B.D., Rice C.M.
    J. Virol. 73:4611-4621(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NS1 WITH NS4A.
  21. "Mutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus capsid protein demonstrates a requirement for coordinated processing."
    Amberg S.M., Rice C.M.
    J. Virol. 73:8083-8094(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 99-ARG--ARG-101.
  22. "Mutagenesis of the signal sequence of yellow fever virus prM protein: enhancement of signalase cleavage In vitro is lethal for virus production."
    Lee E., Stocks C.E., Amberg S.M., Rice C.M., Lobigs M.
    J. Virol. 74:24-32(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 116-LEU--GLY-121.
  23. "Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and deletion analysis define regions important for protease complex formation and function."
    Droll D.A., Krishna Murthy H.M., Chambers T.J.
    Virology 275:335-347(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 1406-GLU--LYS-1409.
  24. "Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles."
    Kummerer B.M., Rice C.M.
    J. Virol. 76:4773-4784(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLN-1319; LYS-1320 AND THR-1321.
  25. "Flavivirus capsid is a dimeric alpha-helical protein."
    Jones C.T., Ma L., Burgner J.W., Groesch T.D., Post C.B., Kuhn R.J.
    J. Virol. 77:7143-7149(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  26. "The transmembrane domains of the prM and E proteins of yellow fever virus are endoplasmic reticulum localization signals."
    Op De Beeck A., Rouille Y., Caron M., Duvet S., Dubuisson J.
    J. Virol. 78:12591-12602(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF SMALL ENVELOPE PROTEIN M AND ENVELOPE PROTEIN E.
  27. "Inhibition of alpha/beta interferon signaling by the NS4B protein of flaviviruses."
    Munoz-Jordan J.L., Laurent-Rolle M., Ashour J., Martinez-Sobrido L., Ashok M., Lipkin W.I., Garcia-Sastre A.
    J. Virol. 79:8004-8013(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF NON-STRUCTURAL PROTEIN 4B.
  28. "Structure and function of flavivirus NS5 methyltransferase."
    Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y., Bernard K.A., Shi P.-Y., Li H.
    J. Virol. 81:3891-3903(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
  29. "The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure."
    Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S., Mayette J., Hobdey S.E., Bisaillon M.
    RNA 15:2340-2350(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
  30. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) OF IMMATURE PARTICLES.
  31. "Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing."
    Wu J., Bera A.K., Kuhn R.J., Smith J.L.
    J. Virol. 79:10268-10277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1671-2107.

Entry informationi

Entry nameiPOLG_YEFV1
AccessioniPrimary (citable) accession number: P03314
Secondary accession number(s): O42028
, O91857, P19901, Q102J3, Q45RQ2, Q89275, Q89276, Q9W878, Q9YWN0, Q9YWN1, Q9YWN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 16, 2016
This is version 163 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, Reference proteome

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.