Skip Header

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

Genome polyprotein

Gene
N/A
Organism
Yellow fever virus (strain Trinidad/TRINID79A/1979) (YFV)
Status
Reviewed-Annotation score: -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.By similarity
Peptide pr: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Protein prM: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network 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 similarity
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity).PROSITE-ProRule annotationBy similarity
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.By similarity
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). 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. 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.By similarity

Catalytic activityi

Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1537Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1561Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1622Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1945Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1948Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2519mRNA capPROSITE-ProRule annotation1
Binding sitei2522mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2523mRNA capPROSITE-ProRule annotation1
Binding sitei2525mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2530mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2534mRNA capPROSITE-ProRule annotation1
Binding sitei2562S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2567For 2'-O-MTase activityBy similarity1
Sitei2567Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2592S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2593S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2610S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2637S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2638S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2652For 2'-O-MTase activityBy similarity1
Sitei2652Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2653S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2656mRNA capPROSITE-ProRule annotation1
Active sitei2688For 2'-O-MTase activityBy similarity1
Sitei2688Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2719mRNA capPROSITE-ProRule annotation1
Binding sitei2721mRNA capPROSITE-ProRule annotation1
Active sitei2724For 2'-O-MTase activityBy similarity1
Sitei2724Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2726S-adenosyl-L-methioninePROSITE-ProRule annotation1
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 – 1689ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, 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

Protein family/group databases

MEROPSiS07.001

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 14 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Non-structural protein 2A-alpha
Short name:
NS2A-alpha
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 5
OrganismiYellow fever virus (strain Trinidad/TRINID79A/1979) (YFV)
Taxonomic identifieri407137 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
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
  • UP000008608 Componenti: Genome

Subcellular locationi

Capsid protein C :
Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :

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 – 757CytoplasmicSequence analysis6
Transmembranei758 – 778HelicalSequence analysisAdd BLAST21
Topological domaini779 – 1132ExtracellularBy similarityAdd BLAST354
Transmembranei1133 – 1153HelicalBy similarityAdd BLAST21
Topological domaini1154 – 1201CytoplasmicBy similarityAdd BLAST48
Transmembranei1202 – 1222HelicalBy similarityAdd BLAST21
Topological domaini1223 – 1287LumenalBy similarityAdd BLAST65
Transmembranei1288 – 1308HelicalBy similarityAdd BLAST21
Topological domaini1309 – 1355CytoplasmicBy similarityAdd BLAST47
Transmembranei1356 – 1376HelicalBy similarityAdd BLAST21
Topological domaini1377 – 1378LumenalBy similarity2
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 – 2256Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2257 – 2293LumenalSequence analysisAdd BLAST37
Intramembranei2294 – 2314HelicalSequence analysisAdd BLAST21
Topological domaini2315 – 2360LumenalSequence analysisAdd BLAST46
Transmembranei2361 – 2380HelicalSequence analysisAdd BLAST20
Topological domaini2381 – 2421CytoplasmicSequence analysisAdd BLAST41
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004051571 – 3411Genome polyproteinAdd BLAST3411
ChainiPRO_00002614851 – 101Capsid protein CBy similarityAdd BLAST101
PropeptideiPRO_0000261486102 – 121ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST20
ChainiPRO_0000261487122 – 285Protein prMBy similarityAdd BLAST164
ChainiPRO_0000261488122 – 210Peptide pr1 PublicationAdd BLAST89
ChainiPRO_0000261489211 – 285Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000261490286 – 778Envelope protein EBy similarityAdd BLAST493
ChainiPRO_0000261491779 – 1130Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00002614921131 – 1354Non-structural protein 2ABy similarityAdd BLAST224
ChainiPRO_00002614931131 – 1320Non-structural protein 2A-alphaBy similarityAdd BLAST190
ChainiPRO_00002614941355 – 1484Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00002614951485 – 2107Serine protease NS3By similarityAdd BLAST623
ChainiPRO_00002614962108 – 2233Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00002614972234 – 2256Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00002614982257 – 2506Non-structural protein 4BBy similarityAdd BLAST250
ChainiPRO_00002614992507 – 3411RNA-directed RNA polymerase NS5By similarityAdd 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 residuei2562PhosphoserineBy similarity1

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.By similarity1 Publication
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 similarity1 Publication
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.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei101 – 102Cleavage; by viral protease NS3By similarity2
Sitei121 – 122Cleavage; by host signal peptidaseBy similarity2
Sitei210 – 211Cleavage; by host furinSequence analysis1 Publication2
Sitei285 – 286Cleavage; by host signal peptidaseBy similarity2
Sitei778 – 779Cleavage; by host signal peptidaseBy similarity2
Sitei1130 – 1131Cleavage; by hostBy similarity2
Sitei1354 – 1355Cleavage; by viral protease NS3By similarity2
Sitei1484 – 1485Cleavage; by autolysisBy similarity2
Sitei2107 – 2108Cleavage; by autolysisBy similarity2
Sitei2233 – 2234Cleavage; by viral protease NS3By similarity2
Sitei2256 – 2257Cleavage; by host signal peptidaseBy similarity2
Sitei2506 – 2507Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRIDEiQ9YRV3

Interactioni

Subunit structurei

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

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ9YRV3
SMRiQ9YRV3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1485 – 1665Peptidase S7PROSITE-ProRule annotationAdd BLAST181
Domaini1669 – 1825Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1820 – 1997Helicase C-terminalAdd BLAST178
Domaini2507 – 2771mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3035 – 3187RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1773 – 1776DEAH boxPROSITE-ProRule annotation4
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.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900007N

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
cd00079 HELICc, 1 hit
Gene3Di1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 3 hits
3.30.387.10, 2 hits
3.30.67.10, 4 hits
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
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
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.

Q9YRV3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF
60 70 80 90 100
FLFNILTGKK ITAQLKRLWK MLDPRQGLAA LRKVKRVVAG LMRGLSSRKR
110 120 130 140 150
RSHDVLTVQF LILGMLLMTG GVTLMRKNRW LLLNVTSEDL GKTFSIGTGN
160 170 180 190 200
CTTNILEAKY WCPDSMEYNC PNLSPREEPD DIDCWCYGVE NVRVTYGKCD
210 220 230 240 250
SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ KIERWFVRNP
260 270 280 290 300
FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG VADRDFIEGV
310 320 330 340 350
HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPVE ARKVCYNAVL
360 370 380 390 400
THVKIDDKCP STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA
410 420 430 440 450
CAKFTCAKSM SLFEVDQTKI QYVIKAQLHV GAKQEDWKTD IKTLKFDVLS
460 470 480 490 500
GSQEAEFTGY GKVTLECQVQ TAVDFGNSYI AEMEKESWIV DRQWAQDLTL
510 520 530 540 550
PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGDQEGSLK TALTGAMRVT
560 570 580 590 600
KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH
610 620 630 640 650
GTVVMQVKVP KGAPCKIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI
660 670 680 690 700
EVNPPFGDSY IIIGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD
710 720 730 740 750
AAWDFSSAGG FFTSVGKGIH TVFGSAFQGL FGGLNWITKV IMGAVLIWVG
760 770 780 790 800
FNTRNMTMSM SMILVGVIMM FLSLGVGADQ GCAINFGKRE LKCGDGIFIF
810 820 830 840 850
RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS LEHEMWRSRA
860 870 880 890 900
DEINAILEEN 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 DSGKIIPEWC CRSCTMPPVS
1110 1120 1130 1140 1150
FHGSDGCWYP MEIRPMKTHE SHLVRSWVTA GEIHAVPFGL VSMMIAMEVV
1160 1170 1180 1190 1200
LRKRQGPKQV LVGGVVLLGA MLVGQVTLLD LLELTVAVGL HFHEMNNGGD
1210 1220 1230 1240 1250
AMYMALIAAF SVRPGLLIGF GLRTLWSPRE RLVLALGAAM VEIALGGMMG
1260 1270 1280 1290 1300
GLWKYLNAVS LCILTINAVA SRKASNAILP LMALLTPVTM AEVRLATMLF
1310 1320 1330 1340 1350
CTVVIIGVLH QNSKDTSMQK TIPLVALTLT SYLGLTQPFL GLCAFLATRI
1360 1370 1380 1390 1400
FGRRSIPVNE ALAATGLVGV LAGLAFQEME NFLGPIAVGG ILMMLVSVAG
1410 1420 1430 1440 1450
RVDGLELKKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL LSEEKVPWDQ
1460 1470 1480 1490 1500
VVMTSLALVG AAIHPFALLL VLAGWLFHVR RARRSGDVLW DIPTPKIIEE
1510 1520 1530 1540 1550
CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVWNGKK
1560 1570 1580 1590 1600
LIPSWASVKE DLVAYGGSWK LEGRWDGEEE VQLIAAAPGK NVVNVQTKPS
1610 1620 1630 1640 1650
LFKVRNGGEI GAVALDYPSG TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS
1660 1670 1680 1690 1700
AISQTEVKEE GKEELQEIPT MLKKGKTTIL DFHPGAGKTR RFLPQILAEC
1710 1720 1730 1740 1750
ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG SGREVIDVMC
1760 1770 1780 1790 1800
HATLTYRMLE PTRIVNWEVI 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 YYSEPTSEDN AHHVCWLEAS MLLDNMEVRG GMVAPLYGVE
2010 2020 2030 2040 2050
GIKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK AGLKTNDRKW
2060 2070 2080 2090 2100
CFEGPEEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALSEFI
2110 2120 2130 2140 2150
KFAEGRRGAA DVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA
2160 2170 2180 2190 2200
LSMMPEAMTI VMLFLLAGLL TSGMVIFFMS PKGISRMSMA KGTMAGCGYL
2210 2220 2230 2240 2250
MFLGGVEPTH ISYIMLIFFV LMVVVIPEPG QQRSIQDNQV AFLIIGILTL
2260 2270 2280 2290 2300
VSVVAANELG MLEKTKEDLF GKKNLIPSGA 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
KNPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLD
2460 2470 2480 2490 2500
EGIVLASAAL GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVAYNLWK
2510 2520 2530 2540 2550
MKTARRGTAN GKTLGEVWKR ELNLLDKQQF ELYKRTDIVE VDRDTARRHL
2560 2570 2580 2590 2600
AEGKVDTGVA VSRGTAKLRW FHERGYVKLE GRVIDLGCGR GGWCYYAAAQ
2610 2620 2630 2640 2650
KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDVHP LEPVKCDTLL
2660 2670 2680 2690 2700
CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMRDVLEK
2710 2720 2730 2740 2750
LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM
2760 2770 2780 2790 2800
RRPTGKVTLE ADVTLPIGTR SVETDKGPLD KEAIKERVER IKSEYMTSWF
2810 2820 2830 2840 2850
YDNDNPYRTW HYCGSYVTKT SGSAASMVNG VIKLLTYPWD KIEEVTRMAM
2860 2870 2880 2890 2900
TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI MKVVNRWLFR HLAREKNPRL
2910 2920 2930 2940 2950
CTKEEFIAKV RSHAAIGAYL EEQDQWKTAN EAVQDPKFWE LVDEERKLHQ
2960 2970 2980 2990 3000
QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN
3010 3020 3030 3040 3050
EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGLYAD 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 GCDRLRRMAV 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 GEWMTTEDRL EVWNRVWITN NPHMQDKTMV KEWRDVPYLT
3360 3370 3380 3390 3400
KRQDKLCGSL IGMTNRATWA SNIHLVIHRI RTLVGQEKYT DYLTVMDRYS
3410
VDADLQPGEL I
Length:3,411
Mass (Da):379,223
Last modified:May 1, 1999 - v1
Checksum:i005E37E8E79AE4BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF094612 Genomic RNA Translation: AAC72235.1

Similar proteinsi

Entry informationi

Entry nameiPOLG_YEFVT
AccessioniPrimary (citable) accession number: Q9YRV3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 1, 1999
Last modified: June 20, 2018
This is version 128 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

Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again