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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: Plays a role in virus budding by binding to the cell 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 into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions.By similarity
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.1 Publication
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 probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, 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 ectodomain. 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 particle 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 inefficient, 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. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).By similarity1 Publication
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).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. Also plays a role in virus assembly (PubMed:18199634).1 Publication
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.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: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. 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 (PubMed:15956546).By similarity1 Publication
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:19850911). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:25211074). IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition (PubMed:25211074).2 Publications

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.1 Publication
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).1 Publication
NTP + H2O = NDP + phosphate.1 Publication
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'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

pH dependencei

Optimum pH is 9.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1537Charge relay system; for serine protease NS3 activity1
Active sitei1561Charge relay system; for serine protease NS3 activity1
Active sitei1622Charge relay system; for serine protease NS3 activity1
Sitei1945Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1948Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2519mRNA cap1 Publication1
Binding sitei2522mRNA cap; via carbonyl oxygen1 Publication1
Binding sitei2523mRNA cap1 Publication1
Binding sitei2525mRNA cap; via carbonyl oxygen1 Publication1
Sitei2530mRNA cap binding1
Binding sitei2534mRNA cap1 Publication1
Binding sitei2562S-adenosyl-L-methionine1
Active sitei2567For 2'-O-MTase activityBy similarity1
Sitei2567Essential for 2'-O-methyltransferase activity1
Binding sitei2592S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei2593S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei2610S-adenosyl-L-methionine1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei2637S-adenosyl-L-methionine1
Binding sitei2638S-adenosyl-L-methionine; via carbonyl oxygen1
Active sitei2652For 2'-O-MTase activityBy similarity1
Sitei2652Essential for 2'-O-methyltransferase and N-7 methyltransferase activity1 Publication1
Sitei2653S-adenosyl-L-methionine binding1
Binding sitei2656mRNA cap1 Publication1
Active sitei2688For 2'-O-MTase activityBy similarity1
Sitei2688Essential for 2'-O-methyltransferase activity1
Binding sitei2719mRNA cap1 Publication1
Binding sitei2721mRNA cap1 Publication1
Active sitei2724For 2'-O-MTase activityBy similarity1
Sitei2724Essential for 2'-O-methyltransferase activity1
Binding sitei2726S-adenosyl-L-methionine1
Metal bindingi2945Zinc 1By similarity1
Metal bindingi2949Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2954Zinc 1By similarity1
Metal bindingi2957Zinc 1By similarity1
Metal bindingi3222Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3238Zinc 2By similarity1
Metal bindingi3357Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1682 – 1689ATP8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation 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, 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
LigandATP-binding, GTP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

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-alpha1 Publication
Short name:
NS2A-alpha
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.911 Publication, EC:3.6.1.151 Publication, EC:3.6.4.131 Publication)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56, EC:2.1.1.57, EC:2.7.7.48)
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
  • UP000180883 Componenti: Genome
  • UP000158765 Componenti: Genome
  • UP000180940 Componenti: Genome
  • UP000119912 Componenti: Genome
  • UP000181442 Componenti: Genome
  • UP000158778 Componenti: Genome
  • UP000138083 Componenti: Genome
  • UP000000360 Componenti: Genome
  • UP000180827 Componenti: Genome
  • UP000141075 Componenti: Genome

Subcellular locationi

Capsid protein C :
  • Virion By similarity
  • Host nucleus By similarity
  • host perinuclear region By similarity
  • Host cytoplasm By similarity
Peptide pr :
  • Secreted By similarity
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
  • Secreted By similarity
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
Non-structural protein 2A :
Serine protease subunit NS2B :
Serine protease NS3 :
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Note: Remains non-covalently associated to serine protease subunit NS2B.
Non-structural protein 4A :
  • Host endoplasmic reticulum membrane By similarity; 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 By similarity; Multi-pass membrane protein By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Host nucleus By similarity
  • Note: Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 104CytoplasmicSequence analysisAdd BLAST104
Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Topological domaini126 – 244ExtracellularSequence analysisAdd BLAST119
Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Topological domaini266 – 270CytoplasmicSequence analysis5
Transmembranei271 – 285HelicalSequence analysisAdd BLAST15
Topological domaini286 – 730ExtracellularSequence analysisAdd BLAST445
Transmembranei731 – 751HelicalSequence analysisAdd BLAST21
Topological domaini752 – 757ExtracellularSequence analysis6
Transmembranei758 – 778HelicalSequence analysisAdd BLAST21
Topological domaini779 – 1132ExtracellularSequence analysisAdd BLAST354
Transmembranei1133 – 1153HelicalSequence analysisAdd BLAST21
Topological domaini1154 – 1201CytoplasmicSequence analysisAdd BLAST48
Transmembranei1202 – 1222HelicalSequence analysisAdd BLAST21
Topological domaini1223 – 1287LumenalSequence analysisAdd BLAST65
Transmembranei1288 – 1308HelicalSequence analysisAdd BLAST21
Topological domaini1309 – 1355CytoplasmicSequence analysisAdd BLAST47
Transmembranei1356 – 1376HelicalSequence analysisAdd BLAST21
Topological domaini1377 – 1378LumenalSequence analysis2
Transmembranei1379 – 1399HelicalSequence analysisAdd BLAST21
Topological domaini1400 – 1456CytoplasmicSequence analysisAdd BLAST57
Intramembranei1457 – 1477HelicalSequence analysisAdd BLAST21
Topological domaini1478 – 2157CytoplasmicSequence analysisAdd BLAST680
Transmembranei2158 – 2178HelicalSequence analysisAdd BLAST21
Topological domaini2179 – 2186LumenalSequence analysis8
Intramembranei2187 – 2207HelicalSequence analysisAdd BLAST21
Topological domaini2208 – 2209LumenalSequence analysis2
Transmembranei2210 – 2230HelicalSequence analysisAdd BLAST21
Topological domaini2231 – 2241CytoplasmicSequence analysisAdd BLAST11
Transmembranei2242 – 2262Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2263 – 2293LumenalSequence analysisAdd BLAST31
Intramembranei2294 – 2314HelicalSequence analysisAdd BLAST21
Topological domaini2315 – 2360LumenalSequence analysisAdd BLAST46
Transmembranei2361 – 2381HelicalSequence analysisAdd BLAST21
Topological domaini2382 – 2421CytoplasmicSequence analysisAdd BLAST40
Transmembranei2422 – 2442HelicalSequence analysisAdd BLAST21
Topological domaini2443 – 2445LumenalSequence analysis3
Transmembranei2446 – 2466HelicalSequence analysisAdd BLAST21
Topological domaini2467 – 3411CytoplasmicSequence analysisAdd BLAST945

GO - Cellular componenti

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi98 – 101RKRR → AAAA: Complete loss of NS2B-NS3 cleavage. 4
Mutagenesisi98 – 101RKRR → AKAA: Complete loss of NS2B-NS3 cleavage. 4
Mutagenesisi98 – 101RKRR → AKRA: Reduces NS2B-NS3 cleavage efficiency. 4
Mutagenesisi98 – 100RKR → AAA: Complete loss of NS2B-NS3 cleavage. 3
Mutagenesisi98 – 100RKR → AKA: Complete loss of NS2B-NS3 cleavage. 3
Mutagenesisi98 – 99RK → AA: Reduces NS2B-NS3 cleavage efficiency. 2
Mutagenesisi99 – 101KRR → ARA: Complete loss of NS2B-NS3 cleavage. 1 Publication3
Mutagenesisi99 – 100KR → AA: Complete loss of NS2B-NS3 cleavage. 2
Mutagenesisi100 – 101RR → AA: Reduces NS2B-NS3 cleavage efficiency. 2
Mutagenesisi116 – 121LLMTGG → VPQAQA: Complete loss of infectious virus production. Enhances signal peptidase cleavage in vitro of nascent capsid protein C. 1 Publication6
Mutagenesisi908N → A: Reduces viral RNA accumulation and NS1 secretion. 1 Publication1
Mutagenesisi910S → A: Reduces viral RNA accumulation and NS1 secretion. 1 Publication1
Mutagenesisi986N → A: No effect. 1 Publication1
Mutagenesisi988T → A: No effect. 1 Publication1
Mutagenesisi1077R → A: Blocks RNA replication. 1 Publication1
Mutagenesisi1152 – 1154RKR → AAA: Defective in infectious particle production; almost no effect on viral replication. 1 Publication3
Mutagenesisi1229 – 1231RER → AAA: Defective in infectious particle production; almost no effect on viral replication. 1 Publication3
Mutagenesisi1319 – 1321QKT → RRS: Increases NS2A-alpha processing, complete loss of NS2A. 3
Mutagenesisi1319Q → A: Almost no effect on viral replication. 1 Publication1
Mutagenesisi1319Q → S: Complete loss of cleavage and NS2A alpha. Complete loss of infectivity. 1 Publication1
Mutagenesisi1320K → E, I, Q or S: Complete loss of cleavage and NS2A-alpha processing. Complete loss of infectivity. 1 Publication1
Mutagenesisi1320K → R: No effect on NS2A-alpha processing. 1 Publication1
Mutagenesisi1321T → V: Complete loss of cleavage and NS2A alpha synthesis. Complete loss of infectivity. 1 Publication1
Mutagenesisi1351F → C, I or V: Enhances NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1351F → G: No effect on NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1352G → A or K: Enhances NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1352G → E or V: Reduces NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1353R → H, K, R or T: Reduces NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1353R → L or P: Complete loss of NS2A-NS2B cleavage. 1 Publication1
Mutagenesisi1354R → I, N, S or T: Complete loss of NS2A-NS2B cleavage. 1 Publication1
Mutagenesisi1354R → K: Reduces of NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1355S → D, K, R or V: Complete loss of NS2A-NS2B cleavage. 1 Publication1
Mutagenesisi1355S → G: Reduces of NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1406 – 1409ELKK → ALAA: Complete loss of polyprotein cleavage. 1 Publication4
Mutagenesisi1537H → A: Complete loss NS3 protease activity. 1 Publication1
Mutagenesisi1561D → A or N: Complete loss NS3 protease activity. 1 Publication1
Mutagenesisi1622S → A: Complete loss NS3 protease activity. 1 Publication1
Mutagenesisi1622S → C: Diminishes NS3 protease activity. 1 Publication1
Mutagenesisi1833W → A: Complete loss of production of infectious virus particles. 1 Publication1
Mutagenesisi2107R → A, L, M, T or V: Reduces NS4A-NS4B cleavage efficiency. 1 Publication1
Mutagenesisi2107R → E: Complete loss of NS4A-NS4B cleavage. 2 Publications1
Mutagenesisi2107R → K: No effect on NS4A-NS4B cleavage efficiency. 1 Publication1
Mutagenesisi2107R → P: Complete loss of NS4A-NS4B cleavage. 1 Publication1
Mutagenesisi2234S → A or T: No effect on NS4A-NS4B cleavage. 1 Publication1
Mutagenesisi2234S → I or P: No effect on NS4A-NS4B cleavage. 1 Publication1
Mutagenesisi2505R → A, I, L, Q, S or T: No effect on NS4B-NS5 cleavage efficiency. 1 Publication1
Mutagenesisi2505R → P: Reduces NS4B-NS5 cleavage efficiency. 1 Publication1
Mutagenesisi2506R → E: Complete loss of NS4B-NS5 cleavage. 2 Publications1
Mutagenesisi2506R → H, N or Q: Reduces NS4B-NS5 cleavage efficiency. 1 Publication1
Mutagenesisi2506R → K: No effect on NS4B-NS5 cleavage efficiency. 1 Publication1
Mutagenesisi2506R → Y: Complete loss of NS4B-NS5 cleavage. 1 Publication1
Mutagenesisi2507G → A or S: Reduces NS4B-NS5 cleavage efficiency. 1
Mutagenesisi2507G → E, K, L, M, N or V: Reduces NS4B-NS5 cleavage efficiency. 1
Mutagenesisi2512K → R: Completet loss of NS5 binding to STAT2 after IFN-I stimulation. 1 Publication1
Mutagenesisi2562S → A: Complete loss of 2'-O-MTase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004051531 – 3411Genome polyproteinAdd BLAST3411
ChainiPRO_00000377541 – 101Capsid protein C1 PublicationAdd BLAST101
PropeptideiPRO_0000261384102 – 121ER anchor for the capsid protein C, removed in mature form by serine protease NS31 PublicationAdd BLAST20
ChainiPRO_0000261385122 – 285Protein prMBy similarityAdd BLAST164
ChainiPRO_0000037755122 – 210Peptide prBy similarityAdd BLAST89
ChainiPRO_0000037756211 – 285Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037757286 – 778Envelope protein EBy similarityAdd BLAST493
ChainiPRO_0000037758779 – 1130Non-structural protein 11 PublicationAdd BLAST352
ChainiPRO_00000377591131 – 1354Non-structural protein 2ABy similarityAdd BLAST224
ChainiPRO_00002613861131 – 1320Non-structural protein 2A-alpha1 PublicationAdd BLAST190
ChainiPRO_00000377601355 – 1484Serine protease subunit NS2B1 PublicationAdd BLAST130
ChainiPRO_00000377611485 – 2107Serine protease NS32 PublicationsAdd BLAST623
ChainiPRO_00000377622108 – 2233Non-structural protein 4A1 PublicationAdd BLAST126
PeptideiPRO_00002613872234 – 2256Peptide 2k1 PublicationAdd BLAST23
ChainiPRO_00000377632257 – 2506Non-structural protein 4B1 PublicationAdd BLAST250
ChainiPRO_00000377642507 – 3411RNA-directed RNA polymerase NS52 PublicationsAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi134N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi150N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi288 ↔ 315By similarity
Disulfide bondi345 ↔ 406By similarity
Disulfide bondi345 ↔ 401By similarity
Disulfide bondi359 ↔ 390By similarity
Disulfide bondi377 ↔ 406By similarity
Disulfide bondi377 ↔ 401By similarity
Disulfide bondi467 ↔ 568By similarity
Disulfide bondi585 ↔ 615By similarity
Disulfide bondi782 ↔ 793By similarity
Disulfide bondi833 ↔ 921By similarity
Glycosylationi908N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi957 ↔ 1002By similarity
Glycosylationi986N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1058 ↔ 1107By similarity
Disulfide bondi1069 ↔ 1091By similarity
Disulfide bondi1090 ↔ 1094By similarity
Modified residuei2562Phosphoserine1 Publication1

Post-translational modificationi

Genome polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. The nascent capsid 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 capsid 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.7 Publications
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
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
Polyubiquitinated; ubiquitination is probably mediated by host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not ISGylated or sumoylated.1 Publication
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei101 – 102Cleavage; by viral protease NS31 Publication2
Sitei121 – 122Cleavage; by host signal peptidase1 Publication2
Sitei210 – 211Cleavage; by host furinBy similarity2
Sitei285 – 286Cleavage; by host signal peptidaseBy similarity2
Sitei778 – 779Cleavage; by host signal peptidase1 Publication2
Sitei1130 – 1131Cleavage; by hostBy similarity2
Sitei1320 – 1321Cleavage; by viral protease NS31 Publication2
Sitei1354 – 1355Cleavage; by viral protease NS32 Publications2
Sitei1484 – 1485Cleavage; by autolysis2 Publications2
Sitei2107 – 2108Cleavage; by autolysis3 Publications2
Sitei2233 – 2234Cleavage; by viral protease NS31 Publication2
Sitei2256 – 2257Cleavage; by host signal peptidaseBy similarity2
Sitei2506 – 2507Cleavage; by viral protease NS33 Publications2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP03314.

Interactioni

Subunit structurei

Capsid protein C: Homodimer (PubMed:12768036). Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity). Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (By similarity). Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi. Interacts with protein prM. Interacts with non-structural protein 1 (By similarity). Non-structural protein 1: Homodimer; Homohexamer when secreted. Interacts with envelope protein E (By similarity). Non-structural protein 2A: Interacts (via N-terminus) with serine protease NS3 (PubMed:25694595). Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers (By similarity). Serine protease NS3: Forms a heterodimer with NS2B (By similarity). Interacts with non-structural protein 2A (via N-terminus) (PubMed:25694595). Interacts with NS4B (By similarity). Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). NS3 interacts with host PDCD6IP; this interaction contributes to virion release (PubMed:21044891). Non-structural protein 4B: Interacts with serine protease NS3 (By similarity). RNA-directed RNA polymerase NS5: Homodimer (By similarity). Interacts with host STAT2; this interaction prevents the establishment of cellular antiviral state (PubMed:25211074). Interacts with host TRIM23; this interaction leads to NS5 ubiquitination (PubMed:25211074).By similarity4 Publications

GO - Molecular functioni

Structurei

Secondary structure

13411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1677 – 1680Combined sources4
Turni1688 – 1691Combined sources4
Helixi1692 – 1702Combined sources11
Beta strandi1707 – 1713Combined sources7
Helixi1714 – 1723Combined sources10
Turni1724 – 1726Combined sources3
Beta strandi1729 – 1731Combined sources3
Beta strandi1746 – 1750Combined sources5
Helixi1751 – 1758Combined sources8
Beta strandi1760 – 1762Combined sources3
Beta strandi1768 – 1772Combined sources5
Turni1773 – 1776Combined sources4
Helixi1780 – 1794Combined sources15
Beta strandi1799 – 1803Combined sources5
Beta strandi1821 – 1825Combined sources5
Beta strandi1834 – 1836Combined sources3
Helixi1839 – 1842Combined sources4
Beta strandi1847 – 1850Combined sources4
Helixi1854 – 1866Combined sources13
Beta strandi1871 – 1873Combined sources3
Beta strandi1876 – 1878Combined sources3
Beta strandi1892 – 1899Combined sources8
Beta strandi1909 – 1913Combined sources5
Beta strandi1916 – 1923Combined sources8
Turni1924 – 1927Combined sources4
Beta strandi1928 – 1936Combined sources9
Helixi1939 – 1946Combined sources8
Beta strandi1958 – 1962Combined sources5
Helixi1974 – 1983Combined sources10
Helixi1989 – 1991Combined sources3
Helixi2000 – 2003Combined sources4
Beta strandi2004 – 2006Combined sources3
Turni2008 – 2011Combined sources4
Helixi2015 – 2026Combined sources12
Helixi2032 – 2040Combined sources9
Helixi2049 – 2051Combined sources3
Helixi2056 – 2058Combined sources3
Beta strandi2063 – 2065Combined sources3
Beta strandi2069 – 2071Combined sources3
Beta strandi2077 – 2079Combined sources3
Beta strandi2083 – 2086Combined sources4
Helixi2087 – 2089Combined sources3
Beta strandi2090 – 2092Combined sources3
Helixi2093 – 2103Combined sources11
Turni2104 – 2106Combined sources3
Helixi2514 – 2524Combined sources11
Helixi2527 – 2534Combined sources8
Beta strandi2536 – 2541Combined sources6
Helixi2544 – 2551Combined sources8
Helixi2564 – 2573Combined sources10
Beta strandi2581 – 2586Combined sources6
Helixi2592 – 2598Combined sources7
Beta strandi2603 – 2609Combined sources7
Helixi2627 – 2629Combined sources3
Beta strandi2630 – 2633Combined sources4
Turni2638 – 2640Combined sources3
Beta strandi2647 – 2651Combined sources5
Helixi2660 – 2678Combined sources19
Turni2679 – 2681Combined sources3
Beta strandi2683 – 2690Combined sources8
Helixi2695 – 2708Combined sources14
Beta strandi2711 – 2713Combined sources3
Beta strandi2725 – 2730Combined sources6
Helixi2735 – 2751Combined sources17
Beta strandi2757 – 2760Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03314.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1485 – 1665Peptidase S7Add BLAST181
Domaini1669 – 1825Helicase ATP-bindingAdd BLAST157
Domaini1820 – 1997Helicase C-terminalAdd BLAST178
Domaini2507 – 2771mRNA cap 0-1 NS5-type MTAdd BLAST265
Domaini3035 – 3187RdRp catalyticAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST35
Regioni383 – 396Fusion peptideBy similarityAdd BLAST14
Regioni1407 – 1446Interacts with and activates NS3 proteaseAdd BLAST40
Regioni1673 – 1676Important for RNA-bindingBy similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1773 – 1776DEAH box4
Motifi2878 – 2911Nuclear localization signalBy similarityAdd BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2656 – 2660Poly-Ser5

Domaini

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.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.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900007N.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
cd00079. HELICc. 1 hit.
cd06174. MFS. 1 hit.
Gene3Di2.60.40.350. 1 hit.
3.30.387.10. 1 hit.
3.30.67.10. 1 hit.
InterProiView protein in InterPro
IPR011492. 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_sf.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR036253. Glycoprot_cen/dimer_sf.
IPR013756. GlyE_cen_dom_subdom2.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR020846. MFS_dom.
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.
PfamiView protein in Pfam
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.
PF00949. Peptidase_S7. 1 hit.
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
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.
PROSITEiView protein in PROSITE
PS51527. 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.

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)DescriptionActionsGraphical viewLength
Natural varianti341V → A in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti438N → T in strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine. 1
Natural varianti440D → S in strain: Isolate 17DD vaccine. 1
Natural varianti610S → P in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti629I → V in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti701T → V in strain: Isolate 17DD vaccine. 1
Natural varianti744A → V in strain: Isolate 17D-204-South Africa vaccine large plaque variant. 1
Natural varianti764L → M in strain: Isolate 17D-204-South Africa vaccine large plaque variant. 1
Natural varianti1299F → L in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti1666Q → R in strain: Isolate 17DD vaccine. 1
Natural varianti1669P → S in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti1679V → I in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti2214V → 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. 1
Natural varianti2277P → S in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti2401E → 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. 1
Natural varianti2460L → S in strain: Isolate 17D-204-USA HONG vaccine1, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine. 1
Natural varianti2528R → Q in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti2643P → S in strain: Isolate 17D-204-South Africa vaccine medium plaque variant. 1
Natural varianti2661V → I in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti2897N → S in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti3110G → R in strain: Isolate 17D-204-USA HONG2 vaccine. 1
Natural varianti3135M → N in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti3163D → 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. 1
Natural varianti3222H → R in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1

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.

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 22, 2017
This is version 176 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families