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Protein

Genome polyprotein

Gene
N/A
Organism
Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV)
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.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: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavege is inneficient, and un-matured prM-E proteins would have an activity against host immune response. The sequence of PrM contributes to fetal microcephaly in Humans. 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 similarity1 Publication
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 particule is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is 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 alpha/beta interferon antiviral response (By similarity). Disrupts adherens junction formation and thereby impairs proliferation of radial cells in both embryonic mouse cortex and human forebrain organoids (PubMed:28826723).By similarity1 Publication
Non-structural protein 2B: Required cofactor for the serine protease function of NS3.By similarity
Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Leads to translation arrest when expressed ex vivo (PubMed:28592527).By similarity1 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). Cooperatively with NS4B suppress the Akt-mTOR pathway and lead to cellular dysregulation (PubMed:27524440). Leads to translation arrest when expressed ex vivo (PubMed:28592527).By similarity2 Publications
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. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). Cooperatively with NS4A suppress the Akt-mTOR pathway and lead to cellular dysregulation (PubMed:27524440).By similarity1 Publication
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. 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. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.By similarity

Catalytic activityi

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
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
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.By similarity
NTP + H2O = NDP + phosphate.By similarity
ATP + H2O = ADP + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei139Fetal microcephaly1
Active sitei1553Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1577Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1637Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1958Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1961Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2533mRNA capPROSITE-ProRule annotation1
Binding sitei2536mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2537mRNA capPROSITE-ProRule annotation1
Binding sitei2539mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2544mRNA capCombined sources1
Binding sitei2548mRNA capPROSITE-ProRule annotation1
Binding sitei2576S-adenosyl-L-methionineCombined sources1
Active sitei2581For 2'-O-MTase activityBy similarity1
Binding sitei2651S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2652S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2666For 2'-O-MTase activityBy similarity1
Sitei2667S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2670mRNA capPROSITE-ProRule annotation1
Active sitei2702For 2'-O-MTase activityBy similarity1
Binding sitei2733mRNA capPROSITE-ProRule annotation1
Binding sitei2735mRNA capPROSITE-ProRule annotation1
Active sitei2738For 2'-O-MTase activityBy similarity1
Binding sitei2740S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2959Zinc 1By similarity1
Metal bindingi2963Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2968Zinc 1By similarity1
Metal bindingi2971Zinc 1By similarity1
Metal bindingi3234Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3250Zinc 2By similarity1
Metal bindingi3369Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1696 – 1703ATPPROSITE-ProRule annotation8
Nucleotide bindingi2533 – 2539GTPCombined sources7
Nucleotide bindingi2669 – 2675GTPCombined sources7
Nucleotide bindingi2733 – 2735GTPCombined sources3

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 STAT1 by virus, Inhibition of host STAT2 by virus, Inhibition of host TYK2 by virus, mRNA capping, mRNA processing, Transcription, Transcription regulation, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
Ligand4Fe-4S, ATP-binding, GTP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Capsid protein CBy similarity
Alternative name(s):
Capsid protein
Core protein
Protein prMBy similarity
Alternative name(s):
Precursor membrane protein
Peptide prBy similarity
Alternative name(s):
Peptide precursor
Small envelope protein MBy similarity
Alternative name(s):
Matrix protein
Envelope protein EBy similarity
Non-structural protein 1By similarity
Short name:
NS1
Non-structural protein 2ABy similarity
Short name:
NS2A
Serine protease syssubunit NS2BBy similarity
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3By similarity (EC:3.4.21.91, EC:3.6.1.15, EC:3.6.4.13)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Non-structural protein 4ABy similarity
Short name:
NS4A
Peptide 2kBy similarity
Non-structural protein 4BBy similarity
Short name:
NS4B
RNA-directed RNA polymerase NS5By similarity (EC:2.1.1.56, EC:2.1.1.57, EC:2.7.7.48)
Alternative name(s):
NS5
OrganismiZika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV)
Taxonomic identifieri2043570 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
Proteomesi
  • UP000137079 Componenti: Genome
  • UP000151151 Componenti: Genome
  • UP000112691 Componenti: Genome
  • UP000168269 Componenti: Genome

Subcellular locationi

Capsid protein C :
  • Virion By similarity
  • Host nucleus By similarity
  • Host cytoplasm By similarity
  • host perinuclear region 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 By similarity; Peripheral membrane protein By similarity; Lumenal side By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
Non-structural protein 2A :
Serine protease NS3 :
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 By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • 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 – 104CytoplasmicCuratedAdd BLAST104
Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Topological domaini126 – 249ExtracellularCuratedAdd BLAST124
Transmembranei250 – 269HelicalSequence analysisAdd BLAST20
Topological domaini270 – 274CytoplasmicCurated5
Transmembranei275 – 290HelicalCuratedAdd BLAST16
Topological domaini291 – 745ExtracellularCuratedAdd BLAST455
Transmembranei746 – 767HelicalSequence analysisAdd BLAST22
Topological domaini768 – 773CytoplasmicCurated6
Transmembranei774 – 794HelicalSequence analysisAdd BLAST21
Topological domaini795 – 1177LumenalCuratedAdd BLAST383
Transmembranei1178 – 1198HelicalSequence analysisAdd BLAST21
Topological domaini1199 – 1220CytoplasmicCuratedAdd BLAST22
Transmembranei1221 – 1241HelicalSequence analysisAdd BLAST21
Topological domaini1242 – 1270LumenalCuratedAdd BLAST29
Transmembranei1271 – 1291HelicalSequence analysisAdd BLAST21
Topological domaini1292 – 1295CytoplasmicCurated4
Transmembranei1296 – 1316HelicalSequence analysisAdd BLAST21
Topological domaini1317 – 1345LumenalCuratedAdd BLAST29
Transmembranei1346 – 1366HelicalSequence analysisAdd BLAST21
Topological domaini1367 – 1373CytoplasmicCurated7
Transmembranei1374 – 1394HelicalSequence analysisAdd BLAST21
Topological domaini1395 – 1397LumenalCurated3
Transmembranei1398 – 1418HelicalSequence analysisAdd BLAST21
Topological domaini1419 – 1472CytoplasmicCuratedAdd BLAST54
Intramembranei1473 – 1493HelicalSequence analysisAdd BLAST21
Topological domaini1494 – 2170LumenalCuratedAdd BLAST677
Transmembranei2171 – 2191HelicalSequence analysisAdd BLAST21
Topological domaini2192 – 2195LumenalCurated4
Intramembranei2196 – 2216HelicalSequence analysisAdd BLAST21
Topological domaini2217 – 2218CytoplasmicCurated2
Transmembranei2219 – 2239HelicalSequence analysisAdd BLAST21
Topological domaini2240 – 2254LumenalCuratedAdd BLAST15
Intramembranei2255 – 2269Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2268 – 2307LumenalCuratedAdd BLAST40
Intramembranei2308 – 2328HelicalSequence analysisAdd BLAST21
Topological domaini2329 – 2344LumenalCuratedAdd BLAST16
Transmembranei2345 – 2365HelicalSequence analysisAdd BLAST21
Topological domaini2366 – 2375CytoplasmicCurated10
Transmembranei2376 – 2396HelicalSequence analysisAdd BLAST21
Topological domaini2397 – 2441LumenalCuratedAdd BLAST45
Transmembranei2442 – 2462HelicalSequence analysisAdd BLAST21
Topological domaini2463 – 3423CytoplasmicCuratedAdd BLAST961

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
Mutagenesisi444N → Q: Improves attachment, assembly and infectivity in cell culture. Attenuates the virus in mouse and mosquitoes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004430181 – 3423Genome polyproteinBy similarityAdd BLAST3423
ChainiPRO_00004430191 – 104Capsid protein CBy similarityAdd BLAST104
PropeptideiPRO_0000443020105 – 122ER anchor for capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000443021123 – 290Protein prMBy similarityAdd BLAST168
ChainiPRO_0000443022123 – 215Peptide prBy similarityAdd BLAST93
ChainiPRO_0000443023216 – 290Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000443024291 – 794Envelope protein EBy similarityAdd BLAST504
ChainiPRO_0000443025795 – 1146Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00004430261147 – 1372Non-structural protein 2ABy similarityAdd BLAST226
ChainiPRO_00004430271373 – 1502Serine protease syssubunit NS2BBy similarityAdd BLAST130
ChainiPRO_00004430281503 – 2119Serine protease NS3By similarityAdd BLAST617
ChainiPRO_00004430292120 – 2246Non-structural protein 4ABy similarityAdd BLAST127
PeptideiPRO_00004430302247 – 2269Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004430312270 – 2520Non-structural protein 4BBy similarityAdd BLAST251
ChainiPRO_00004430322521 – 3423RNA-directed RNA polymerase NS5By similarityAdd BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi192N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi350 ↔ 406By similarity
Disulfide bondi382 ↔ 411By similarity
Glycosylationi444N-linked (GlcNAc...) asparagine; by hostCombined sources1 Publication1
Disulfide bondi798 ↔ 809By similarity
Disulfide bondi849 ↔ 937By similarity
Glycosylationi924N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi973 ↔ 1017By similarity
Glycosylationi1001N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1074 ↔ 1123By similarity
Disulfide bondi1085 ↔ 1106By similarity
Disulfide bondi1107 ↔ 1110By similarity
Modified residuei2576PhosphoserineBy similarity1

Post-translational modificationi

Genome polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Protein prM: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
Envelope protein E: N-glycosylation plays a role in virulence in mammal?ian and mosquito hosts, but may have no effect on neurovirulence.1 Publication
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
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei104 – 105Cleavage; by viral protease NS3By similarity2
Sitei122 – 123Cleavage; by host signal peptidaseBy similarity2
Sitei215 – 216Cleavage; by host furinBy similarity2
Sitei290 – 291Cleavage; by host signal peptidaseBy similarity2
Sitei794 – 795Cleavage; by host signal peptidaseBy similarity2
Sitei1146 – 1147Cleavage; by hostBy similarity2
Sitei1372 – 1373Cleavage; by viral protease NS3By similarity2
Sitei1502 – 1503Cleavage; by autolysisBy similarity2
Sitei2119 – 2120Cleavage; by autolysisBy similarity2
Sitei2246 – 2247Cleavage; by viral protease NS3By similarity2
Sitei2269 – 2270Cleavage; by host signal peptidaseBy similarity2
Sitei2520 – 2521Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Interactioni

Subunit structurei

Capsid protein C: Homodimer. 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 (By similarity). Interacts with host Tyro3, AXL and DC-SIGN proteins (PubMed:26085147). Non-structural protein 1: Homodimer; Homohexamer when secreted (PubMed:27455458). Interacts with envelope protein E (By similarity). Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers (By similarity). Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers (By similarity). Serine protease NS3: Forms a heterodimer with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). Non-structural protein 4B: Interacts with serine protease NS3. Interacts with NS1 (By similarity). RNA-directed RNA polymerase NS5: Homodimer (By similarity). Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (By similarity).By similarity2 Publications

GO - Molecular functioni

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GOZX-ray2.05A/B/C2524-2785[»]
5GP1X-ray2.44A/B/C2524-2785[»]
5H30electron microscopy4.40A/B/C291-794[»]
D/E/F216-290[»]
5H32electron microscopy12.00A/B/C291-693[»]
5H37electron microscopy4.00A/B/C291-794[»]
D/E/F216-290[»]
5IREelectron microscopy3.80A/C/E291-794[»]
B/D/F216-290[»]
5IZ7electron microscopy3.70A/B/C291-794[»]
D/E/F216-290[»]
5JMTX-ray1.80A1674-2119[»]
5KQRX-ray1.33A2521-2786[»]
5KQSX-ray1.50A2521-2786[»]
5KVEX-ray1.70E588-697[»]
5LBSX-ray2.41A/B291-698[»]
5LBVX-ray2.20A/B291-698[»]
5LCVX-ray2.64A/B291-698[»]
5M5BX-ray2.01A/B2525-2786[»]
5MRKX-ray1.90A/B2521-2784[»]
5U4Welectron microscopy9.10G/I/K726-791[»]
H/J/L238-290[»]
5UHYelectron microscopy6.20A/C/E291-686[»]
5ULPX-ray1.55A/B2521-2788[»]
SMRiA0A024B7W1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1503 – 1680Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1683 – 1839Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1834 – 2013Helicase C-terminalPROSITE-ProRule annotationAdd BLAST180
Domaini2521 – 2785mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3049 – 3199RdRp catalyticPROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 25DisorderedBy similarityAdd BLAST25
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni388 – 401Fusion peptideBy similarityAdd BLAST14
Regioni1425 – 1464Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1429 – 1451DisorderedBy similarityAdd BLAST23
Regioni1687 – 1690Important for RNA-bindingBy similarity4
Regioni2601 – 2607S-adenosyl-L-methionine bindingCombined sources7
Regioni2624 – 2625S-adenosyl-L-methionine bindingCombined sources2
Regioni2630 – 2631S-adenosyl-L-methionine bindingCombined sources2
Regioni2651 – 2652S-adenosyl-L-methionine bindingCombined sources2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1787 – 1790DEAH boxPROSITE-ProRule annotation4

Domaini

Small envelope protein M: The transmembrane domain contains an endoplasmic reticulum retention signal.By similarity
Envelope protein E: The transmembrane domain contains an endoplasmic reticulum retention signal.By similarity
Capsid protein C: The disordered region at the N-terminus may be involved in lipid-droplet binding.By similarity
Serine protease subunit NS2B: The central disordered region transitions to ordered by binding to NS3.1 Publication

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

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
cd00079. HELICc. 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.
IPR037172. Flavi_capsidC_sf.
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.
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.
SUPFAMiSSF101257. SSF101257. 1 hit.
SSF50494. 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.
PS51194. HELICASE_CTER. 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.

A0A024B7W1-1 [UniParc]FASTAAdd to basket

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        10         20         30         40         50
MKNPKKKSGG FRIVNMLKRG VARVSPFGGL KRLPAGLLLG HGPIRMVLAI
60 70 80 90 100
LAFLRFTAIK PSLGLINRWG SVGKKEAMEI IKKFKKDLAA MLRIINARKE
110 120 130 140 150
KKRRGADTSV GIVGLLLTTA MAAEVTRRGS AYYMYLDRND AGEAISFPTT
160 170 180 190 200
LGMNKCYIQI MDLGHMCDAT MSYECPMLDE GVEPDDVDCW CNTTSTWVVY
210 220 230 240 250
GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY TKHLIRVENW
260 270 280 290 300
IFRNPGFALA AAAIAWLLGS STSQKVIYLV MILLIAPAYS IRCIGVSNRD
310 320 330 340 350
FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC
360 370 380 390 400
YEASISDMAS DSRCPTQGEA YLDKQSDTQY VCKRTLVDRG WGNGCGLFGK
410 420 430 440 450
GSLVTCAKFA CSKKMTGKSI QPENLEYRIM LSVHGSQHSG MIVNDTGHET
460 470 480 490 500
DENRAKVEIT PNSPRAEATL GGFGSLGLDC EPRTGLDFSD LYYLTMNNKH
510 520 530 540 550
WLVHKEWFHD IPLPWHAGAD TGTPHWNNKE ALVEFKDAHA KRQTVVVLGS
560 570 580 590 600
QEGAVHTALA GALEAEMDGA KGRLSSGHLK CRLKMDKLRL KGVSYSLCTA
610 620 630 640 650
AFTFTKIPAE TLHGTVTVEV QYAGTDGPCK VPAQMAVDMQ TLTPVGRLIT
660 670 680 690 700
ANPVITESTE NSKMMLELDP PFGDSYIVIG VGEKKITHHW HRSGSTIGKA
710 720 730 740 750
FEATVRGAKR MAVLGDTAWD FGSVGGALNS LGKGIHQIFG AAFKSLFGGM
760 770 780 790 800
SWFSQILIGT LLMWLGLNTK NGSISLMCLA LGGVLIFLST AVSADVGCSV
810 820 830 840 850
DFSKKETRCG TGVFVYNDVE AWRDRYKYHP DSPRRLAAAV KQAWEDGICG
860 870 880 890 900
ISSVSRMENI MWRSVEGELN AILEENGVQL TVVVGSVKNP MWRGPQRLPV
910 920 930 940 950
PVNELPHGWK AWGKSYFVRA AKTNNSFVVD GDTLKECPLK HRAWNSFLVE
960 970 980 990 1000
DHGFGVFHTS VWLKVREDYS LECDPAVIGT AVKGKEAVHS DLGYWIESEK
1010 1020 1030 1040 1050
NDTWRLKRAH LIEMKTCEWP KSHTLWTDGI EESDLIIPKS LAGPLSHHNT
1060 1070 1080 1090 1100
REGYRTQMKG PWHSEELEIR FEECPGTKVH VEETCGTRGP SLRSTTASGR
1110 1120 1130 1140 1150
VIEEWCCREC TMPPLSFRAK DGCWYGMEIR PRKEPESNLV RSMVTAGSTD
1160 1170 1180 1190 1200
HMDHFSLGVL VILLMVQEGL KKRMTTKIII STSMAVLVAM ILGGFSMSDL
1210 1220 1230 1240 1250
AKLAILMGAT FAEMNTGGDV AHLALIAAFK VRPALLVSFI FRANWTPRES
1260 1270 1280 1290 1300
MLLALASCLL QTAISALEGD LMVLINGFAL AWLAIRAMVV PRTDNITLAI
1310 1320 1330 1340 1350
LAALTPLARG TLLVAWRAGL ATCGGFMLLS LKGKGSVKKN LPFVMALGLT
1360 1370 1380 1390 1400
AVRLVDPINV VGLLLLTRSG KRSWPPSEVL TAVGLICALA GGFAKADIEM
1410 1420 1430 1440 1450
AGPMAAVGLL IVSYVVSGKS VDMYIERAGD ITWEKDAEVT GNSPRLDVAL
1460 1470 1480 1490 1500
DESGDFSLVE DDGPPMREII LKVVLMTICG MNPIAIPFAA GAWYVYVKTG
1510 1520 1530 1540 1550
KRSGALWDVP APKEVKKGET TDGVYRVMTR RLLGSTQVGV GVMQEGVFHT
1560 1570 1580 1590 1600
MWHVTKGSAL RSGEGRLDPY WGDVKQDLVS YCGPWKLDAA WDGHSEVQLL
1610 1620 1630 1640 1650
AVPPGERARN IQTLPGIFKT KDGDIGAVAL DYPAGTSGSP ILDKCGRVIG
1660 1670 1680 1690 1700
LYGNGVVIKN GSYVSAITQG RREEETPVEC FEPSMLKKKQ LTVLDLHPGA
1710 1720 1730 1740 1750
GKTRRVLPEI VREAIKTRLR TVILAPTRVV AAEMEEALRG LPVRYMTTAV
1760 1770 1780 1790 1800
NVTHSGTEIV DLMCHATFTS RLLQPIRVPN YNLYIMDEAH FTDPSSIAAR
1810 1820 1830 1840 1850
GYISTRVEMG EAAAIFMTAT PPGTRDAFPD SNSPIMDTEV EVPERAWSSG
1860 1870 1880 1890 1900
FDWVTDHSGK TVWFVPSVRN GNEIAACLTK AGKRVIQLSR KTFETEFQKT
1910 1920 1930 1940 1950
KHQEWDFVVT TDISEMGANF KADRVIDSRR CLKPVILDGE RVILAGPMPV
1960 1970 1980 1990 2000
THASAAQRRG RIGRNPNKPG DEYLYGGGCA ETDEDHAHWL EARMLLDNIY
2010 2020 2030 2040 2050
LQDGLIASLY RPEADKVAAI EGEFKLRTEQ RKTFVELMKR GDLPVWLAYQ
2060 2070 2080 2090 2100
VASAGITYTD RRWCFDGTTN NTIMEDSVPA EVWTRHGEKR VLKPRWMDAR
2110 2120 2130 2140 2150
VCSDHAALKS FKEFAAGKRG AAFGVMEALG TLPGHMTERF QEAIDNLAVL
2160 2170 2180 2190 2200
MRAETGSRPY KAAAAQLPET LETIMLLGLL GTVSLGIFFV LMRNKGIGKM
2210 2220 2230 2240 2250
GFGMVTLGAS AWLMWLSEIE PARIACVLIV VFLLLVVLIP EPEKQRSPQD
2260 2270 2280 2290 2300
NQMAIIIMVA VGLLGLITAN ELGWLERTKS DLSHLMGRRE EGATIGFSMD
2310 2320 2330 2340 2350
IDLRPASAWA IYAALTTFIT PAVQHAVTTS YNNYSLMAMA TQAGVLFGMG
2360 2370 2380 2390 2400
KGMPFYAWDF GVPLLMIGCY SQLTPLTLIV AIILLVAHYM YLIPGLQAAA
2410 2420 2430 2440 2450
ARAAQKRTAA GIMKNPVVDG IVVTDIDTMT IDPQVEKKMG QVLLIAVAVS
2460 2470 2480 2490 2500
SAILSRTAWG WGEAGALITA ATSTLWEGSP NKYWNSSTAT SLCNIFRGSY
2510 2520 2530 2540 2550
LAGASLIYTV TRNAGLVKRR GGGTGETLGE KWKARLNQMS ALEFYSYKKS
2560 2570 2580 2590 2600
GITEVCREEA RRALKDGVAT GGHAVSRGSA KLRWLVERGY LQPYGKVIDL
2610 2620 2630 2640 2650
GCGRGGWSYY AATIRKVQEV KGYTKGGPGH EEPMLVQSYG WNIVRLKSGV
2660 2670 2680 2690 2700
DVFHMAAEPC DTLLCDIGES SSSPEVEEAR TLRVLSMVGD WLEKRPGAFC
2710 2720 2730 2740 2750
IKVLCPYTST MMETLERLQR RYGGGLVRVP LSRNSTHEMY WVSGAKSNTI
2760 2770 2780 2790 2800
KSVSTTSQLL LGRMDGPRRP VKYEEDVNLG SGTRAVVSCA EAPNMKIIGN
2810 2820 2830 2840 2850
RIERIRSEHA ETWFFDENHP YRTWAYHGSY EAPTQGSASS LINGVVRLLS
2860 2870 2880 2890 2900
KPWDVVTGVT GIAMTDTTPY GQQRVFKEKV DTRVPDPQEG TRQVMSMVSS
2910 2920 2930 2940 2950
WLWKELGKHK RPRVCTKEEF INKVRSNAAL GAIFEEEKEW KTAVEAVNDP
2960 2970 2980 2990 3000
RFWALVDKER EHHLRGECQS CVYNMMGKRE KKQGEFGKAK GSRAIWYMWL
3010 3020 3030 3040 3050
GARFLEFEAL GFLNEDHWMG RENSGGGVEG LGLQRLGYVL EEMSRIPGGR
3060 3070 3080 3090 3100
MYADDTAGWD TRISRFDLEN EALITNQMEK GHRALALAII KYTYQNKVVK
3110 3120 3130 3140 3150
VLRPAEKGKT VMDIISRQDQ RGSGQVVTYA LNTFTNLVVQ LIRNMEAEEV
3160 3170 3180 3190 3200
LEMQDLWLLR RSEKVTNWLQ SNGWDRLKRM AVSGDDCVVK PIDDRFAHAL
3210 3220 3230 3240 3250
RFLNDMGKVR KDTQEWKPST GWDNWEEVPF CSHHFNKLHL KDGRSIVVPC
3260 3270 3280 3290 3300
RHQDELIGRA RVSPGAGWSI RETACLAKSY AQMWQLLYFH RRDLRLMANA
3310 3320 3330 3340 3350
ICSSVPVDWV PTGRTTWSIH GKGEWMTTED MLVVWNRVWI EENDHMEDKT
3360 3370 3380 3390 3400
PVTKWTDIPY LGKREDLWCG SLIGHRPRTT WAENIKNTVN MVRRIIGDEE
3410 3420
KYMDYLSTQV RYLGEEGSTP GVL
Length:3,423
Mass (Da):379,113
Last modified:July 9, 2014 - v1
Checksum:i5F0E490EE43DE346
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KJ776791 Genomic RNA. Translation: AHZ13508.1.
KX447509 Genomic RNA. Translation: ANO46301.1.
KX447510 Genomic RNA. Translation: ANO46302.1.
KX447512 Genomic RNA. Translation: ANO46304.1.

Similar proteinsi

Entry informationi

Entry nameiPOLG_ZIKVF
AccessioniPrimary (citable) accession number: A0A024B7W1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 31, 2018
Last sequence update: July 9, 2014
Last modified: January 31, 2018
This is version 32 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families