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Protein

Genome polyprotein

Gene
N/A
Organism
Zika virus (strain Mr 766) (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: 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 alpha/beta interferon antiviral response.By similarity
Non-structural protein 2B: Required cofactor for the serine protease function of NS3.PROSITE-ProRule annotation
Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.PROSITE-ProRule annotation
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. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.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. 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

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.By similarity
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 sitei1549Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1573Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1633Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1954Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1957Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2529mRNA capPROSITE-ProRule annotation1
Binding sitei2532mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2533mRNA capPROSITE-ProRule annotation1
Binding sitei2535mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2540mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2544mRNA capPROSITE-ProRule annotation1
Binding sitei2572S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2577For 2'-O-MTase activityBy similarity1
Sitei2577Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2602S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2603S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2620S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2621S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2647S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2648S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2662For 2'-O-MTase activityBy similarity1
Sitei2662Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2663S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2666mRNA capPROSITE-ProRule annotation1
Active sitei2698For 2'-O-MTase activityBy similarity1
Sitei2698Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2729mRNA capPROSITE-ProRule annotation1
Binding sitei2731mRNA capPROSITE-ProRule annotation1
Active sitei2734For 2'-O-MTase activityBy similarity1
Sitei2734Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2736S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2955Zinc 11 Publication1
Metal bindingi2959Zinc 1; via tele nitrogen1 Publication1
Metal bindingi2964Zinc 11 Publication1
Metal bindingi2967Zinc 11 Publication1
Metal bindingi3230Zinc 2; via tele nitrogen1 Publication1
Metal bindingi3246Zinc 21 Publication1
Metal bindingi3365Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1692 – 1699ATPPROSITE-ProRule annotation8

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
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPSiS07.003.

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 subunit 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:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
NS5
OrganismiZika virus (strain Mr 766) (ZIKV)
Taxonomic identifieri64320 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Homo sapiens (Human) [TaxID: 9606]
Macaca mulatta (Rhesus macaque) [TaxID: 9544]
Proteomesi
  • UP000054557 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 ; 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 PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Note: Remains non-covalently associated to serine protease subunit NS2B.PROSITE-ProRule annotation
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
Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Transmembranei250 – 269HelicalSequence analysisAdd BLAST20
Transmembranei275 – 290HelicalCuratedAdd BLAST16
Transmembranei742 – 763HelicalSequence analysisAdd BLAST22
Transmembranei770 – 790HelicalSequence analysisAdd BLAST21
Transmembranei1174 – 1194HelicalSequence analysisAdd BLAST21
Transmembranei1217 – 1237HelicalSequence analysisAdd BLAST21
Transmembranei1267 – 1287HelicalSequence analysisAdd BLAST21
Transmembranei1292 – 1312HelicalSequence analysisAdd BLAST21
Transmembranei1342 – 1362HelicalSequence analysisAdd BLAST21
Transmembranei1370 – 1390HelicalSequence analysisAdd BLAST21
Transmembranei1394 – 1414HelicalSequence analysisAdd BLAST21
Intramembranei1469 – 1489HelicalSequence analysisAdd BLAST21
Transmembranei2167 – 2187HelicalSequence analysisAdd BLAST21
Intramembranei2192 – 2212HelicalSequence analysisAdd BLAST21
Transmembranei2215 – 2235HelicalSequence analysisAdd BLAST21
Transmembranei2251 – 2265Helical; Note=Signal for NS4BCuratedAdd BLAST15
Intramembranei2304 – 2324HelicalSequence analysisAdd BLAST21
Transmembranei2341 – 2361HelicalSequence analysisAdd BLAST21
Transmembranei2372 – 2392HelicalSequence analysisAdd BLAST21
Transmembranei2438 – 2458HelicalSequence analysisAdd BLAST21

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_00004358281 – 3419Genome polyproteinBy similarityAdd BLAST3419
ChainiPRO_00004358291 – 104Capsid protein CBy similarityAdd BLAST104
PropeptideiPRO_0000435830105 – 122ER anchor for capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000435831123 – 290Protein prMBy similarityAdd BLAST168
ChainiPRO_0000435832123 – 215Peptide prBy similarityAdd BLAST93
ChainiPRO_0000435833216 – 290Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000435834291 – 790Envelope protein EBy similarityAdd BLAST500
ChainiPRO_0000435835791 – 1142Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00004358361143 – 1368Non-structural protein 2ABy similarityAdd BLAST226
ChainiPRO_00004358371369 – 1498Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00004358381499 – 2115Serine protease NS3By similarityAdd BLAST617
ChainiPRO_00004358392116 – 2242Non-structural protein 4ABy similarityAdd BLAST127
PeptideiPRO_00004358402243 – 2265Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004358412266 – 2516Non-structural protein 4BBy similarityAdd BLAST251
ChainiPRO_00004358422517 – 3419RNA-directed RNA polymerase NS5By similarityAdd BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi192N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi293 ↔ 320By similarity
Disulfide bondi350 ↔ 411By similarity
Disulfide bondi350 ↔ 406By similarity
Disulfide bondi364 ↔ 395By similarity
Disulfide bondi382 ↔ 411By similarity
Disulfide bondi382 ↔ 406By similarity
Disulfide bondi476 ↔ 577By similarity
Disulfide bondi594 ↔ 625By similarity
Disulfide bondi794 ↔ 805By similarity
Disulfide bondi845 ↔ 933By similarity
Glycosylationi920N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi969 ↔ 1013By similarity
Glycosylationi997N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1070 ↔ 1119By similarity
Disulfide bondi1081 ↔ 1102By similarity
Disulfide bondi1103 ↔ 1106By similarity
Modified residuei2572PhosphoserineBy 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-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
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 NS31 Publication2
Sitei122 – 123Cleavage; by host signal peptidase1 Publication2
Sitei215 – 216Cleavage; by host furin1 Publication2
Sitei290 – 291Cleavage; by host signal peptidaseBy similarity2
Sitei790 – 791Cleavage; by host signal peptidaseBy similarity2
Sitei1142 – 1143Cleavage; by hostBy similarity2
Sitei1368 – 1369Cleavage; by viral protease NS3By similarity2
Sitei1498 – 1499Cleavage; by autolysisBy similarity2
Sitei2115 – 2116Cleavage; by autolysisBy similarity2
Sitei2242 – 2243Cleavage; by viral protease NS3By similarity2
Sitei2265 – 2266Cleavage; by host signal peptidaseBy similarity2
Sitei2516 – 2517Cleavage; 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

Secondary structure

13419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi791 – 797Combined sources7
Turni798 – 801Combined sources4
Beta strandi802 – 812Combined sources11
Beta strandi815 – 819Combined sources5
Beta strandi822 – 827Combined sources6
Helixi829 – 841Combined sources13
Helixi852 – 871Combined sources20
Beta strandi877 – 880Combined sources4
Beta strandi885 – 887Combined sources3
Beta strandi922 – 928Combined sources7
Turni930 – 932Combined sources3
Helixi935 – 937Combined sources3
Beta strandi943 – 949Combined sources7
Beta strandi952 – 961Combined sources10
Helixi971 – 973Combined sources3
Beta strandi975 – 979Combined sources5
Beta strandi982 – 986Combined sources5
Beta strandi988 – 1008Combined sources21
Helixi1017 – 1019Combined sources3
Helixi1028 – 1030Combined sources3
Helixi1035 – 1037Combined sources3
Helixi1043 – 1045Combined sources3
Beta strandi1060 – 1068Combined sources9
Beta strandi1074 – 1077Combined sources4
Beta strandi1088 – 1091Combined sources4
Beta strandi1100 – 1105Combined sources6
Beta strandi1111 – 1115Combined sources5
Beta strandi1118 – 1121Combined sources4
Beta strandi1126 – 1130Combined sources5
Helixi1132 – 1134Combined sources3
Beta strandi1420 – 1425Combined sources6
Beta strandi1431 – 1434Combined sources4
Beta strandi1441 – 1446Combined sources6
Beta strandi1452 – 1454Combined sources3
Beta strandi1519 – 1524Combined sources6
Beta strandi1528 – 1530Combined sources3
Beta strandi1533 – 1540Combined sources8
Beta strandi1543 – 1547Combined sources5
Helixi1548 – 1551Combined sources4
Beta strandi1556 – 1558Combined sources3
Beta strandi1561 – 1563Combined sources3
Beta strandi1565 – 1569Combined sources5
Turni1570 – 1573Combined sources4
Beta strandi1574 – 1580Combined sources7
Beta strandi1589 – 1591Combined sources3
Beta strandi1593 – 1597Combined sources5
Beta strandi1605 – 1609Combined sources5
Beta strandi1612 – 1616Combined sources5
Beta strandi1619 – 1624Combined sources6
Helixi1630 – 1632Combined sources3
Beta strandi1635 – 1638Combined sources4
Beta strandi1640 – 1642Combined sources3
Beta strandi1644 – 1648Combined sources5
Beta strandi1651 – 1653Combined sources3
Beta strandi1659 – 1662Combined sources4
Helixi1679 – 1682Combined sources4
Beta strandi1687 – 1690Combined sources4
Turni1698 – 1701Combined sources4
Helixi1702 – 1712Combined sources11
Beta strandi1717 – 1723Combined sources7
Helixi1724 – 1733Combined sources10
Turni1734 – 1736Combined sources3
Beta strandi1739 – 1741Combined sources3
Beta strandi1756 – 1760Combined sources5
Helixi1761 – 1769Combined sources9
Beta strandi1770 – 1772Combined sources3
Beta strandi1778 – 1784Combined sources7
Helixi1790 – 1804Combined sources15
Beta strandi1809 – 1813Combined sources5
Beta strandi1831 – 1835Combined sources5
Beta strandi1844 – 1846Combined sources3
Helixi1848 – 1851Combined sources4
Beta strandi1857 – 1860Combined sources4
Helixi1864 – 1876Combined sources13
Beta strandi1881 – 1884Combined sources4
Turni1886 – 1888Combined sources3
Helixi1889 – 1898Combined sources10
Beta strandi1902 – 1906Combined sources5
Helixi1908 – 1911Combined sources4
Beta strandi1919 – 1923Combined sources5
Beta strandi1926 – 1933Combined sources8
Turni1934 – 1936Combined sources3
Beta strandi1937 – 1945Combined sources9
Helixi1948 – 1955Combined sources8
Beta strandi1967 – 1971Combined sources5
Turni1978 – 1981Combined sources4
Helixi1983 – 1992Combined sources10
Helixi2007 – 2012Combined sources6
Turni2017 – 2020Combined sources4
Helixi2024 – 2035Combined sources12
Helixi2041 – 2049Combined sources9
Helixi2058 – 2060Combined sources3
Helixi2065 – 2067Combined sources3
Beta strandi2077 – 2079Combined sources3
Beta strandi2085 – 2087Combined sources3
Beta strandi2091 – 2094Combined sources4
Helixi2095 – 2097Combined sources3
Beta strandi2098 – 2100Combined sources3
Helixi2101 – 2111Combined sources11
Helixi2524 – 2534Combined sources11
Helixi2537 – 2544Combined sources8
Turni2545 – 2547Combined sources3
Beta strandi2549 – 2551Combined sources3
Helixi2554 – 2562Combined sources9
Helixi2574 – 2583Combined sources10
Beta strandi2591 – 2596Combined sources6
Turni2599 – 2601Combined sources3
Helixi2602 – 2607Combined sources6
Beta strandi2613 – 2619Combined sources7
Beta strandi2623 – 2626Combined sources4
Helixi2637 – 2639Combined sources3
Beta strandi2640 – 2643Combined sources4
Helixi2648 – 2650Combined sources3
Beta strandi2657 – 2661Combined sources5
Helixi2670 – 2687Combined sources18
Helixi2688 – 2690Combined sources3
Beta strandi2693 – 2700Combined sources8
Helixi2705 – 2718Combined sources14
Beta strandi2721 – 2723Combined sources3
Beta strandi2726 – 2728Combined sources3
Beta strandi2735 – 2740Combined sources6
Helixi2745 – 2759Combined sources15
Beta strandi2761 – 2763Combined sources3
Beta strandi2768 – 2770Combined sources3
Turni2791 – 2793Combined sources3
Helixi2795 – 2804Combined sources10
Turni2805 – 2808Combined sources4
Beta strandi2818 – 2827Combined sources10
Helixi2840 – 2844Combined sources5
Helixi2847 – 2851Combined sources5
Turni2853 – 2855Combined sources3
Beta strandi2858 – 2860Combined sources3
Helixi2865 – 2875Combined sources11
Helixi2885 – 2902Combined sources18
Turni2903 – 2905Combined sources3
Helixi2913 – 2920Combined sources8
Turni2921 – 2923Combined sources3
Helixi2931 – 2933Combined sources3
Helixi2935 – 2944Combined sources10
Helixi2946 – 2959Combined sources14
Turni2960 – 2962Combined sources3
Beta strandi2969 – 2973Combined sources5
Beta strandi2977 – 2979Combined sources3
Helixi2989 – 3006Combined sources18
Helixi3008 – 3011Combined sources4
Turni3012 – 3015Combined sources4
Helixi3017 – 3020Combined sources4
Beta strandi3021 – 3023Combined sources3
Helixi3029 – 3041Combined sources13
Beta strandi3042 – 3045Combined sources4
Helixi3055 – 3057Combined sources3
Helixi3061 – 3067Combined sources7
Helixi3068 – 3073Combined sources6
Helixi3076 – 3091Combined sources16
Helixi3102 – 3104Combined sources3
Beta strandi3106 – 3116Combined sources11
Helixi3123 – 3143Combined sources21
Helixi3149 – 3152Combined sources4
Helixi3159 – 3173Combined sources15
Beta strandi3176 – 3179Combined sources4
Beta strandi3182 – 3185Combined sources4
Helixi3190 – 3194Combined sources5
Helixi3197 – 3201Combined sources5
Beta strandi3206 – 3209Combined sources4
Beta strandi3218 – 3220Combined sources3
Helixi3221 – 3223Combined sources3
Beta strandi3229 – 3235Combined sources7
Beta strandi3237 – 3239Combined sources3
Beta strandi3241 – 3246Combined sources6
Helixi3249 – 3256Combined sources8
Beta strandi3258 – 3261Combined sources4
Helixi3266 – 3283Combined sources18
Helixi3288 – 3300Combined sources13
Beta strandi3322 – 3325Combined sources4
Helixi3327 – 3335Combined sources9
Turni3336 – 3338Combined sources3
Helixi3351 – 3353Combined sources3
Helixi3359 – 3364Combined sources6
Beta strandi3369 – 3371Combined sources3
Helixi3372 – 3379Combined sources8
Helixi3381 – 3392Combined sources12
Beta strandi3394 – 3396Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJ4X-ray1.84A/C/E/G1414-1498[»]
B/D/F/H1499-1675[»]
5GPIX-ray1.58A/C/E/G1414-1464[»]
B/D/F/H1499-1675[»]
5GXJX-ray2.60A/B1416-1668[»]
5JPSX-ray1.78A1674-2115[»]
5JRZX-ray1.62A1669-2115[»]
5K6KX-ray1.89A/B790-1142[»]
5T1VX-ray3.10A/B1414-1467[»]
A/B1499-1685[»]
5TFRX-ray3.05A/B2517-3419[»]
5TMHX-ray3.28A/B2517-3418[»]
5U04X-ray1.90A2822-3419[»]
5U0BX-ray3.00A/B2517-3419[»]
5U0CX-ray3.00A/B/C/D/E/F/G/H2781-3419[»]
5VI7X-ray2.00A1677-2115[»]
5Y4ZX-ray1.30A1676-2115[»]
ProteinModelPortaliQ32ZE1.
SMRiQ32ZE1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1499 – 1676Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1679 – 1835Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1830 – 2009Helicase C-terminalPROSITE-ProRule annotationAdd BLAST180
Domaini2517 – 2781mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3045 – 3195RdRp catalyticPROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni388 – 401Fusion peptideBy similarityAdd BLAST14
Regioni1421 – 1460Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1683 – 1686Important for RNA-bindingBy similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1783 – 1786DEAH boxPROSITE-ProRule annotation4

Domaini

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG090001DL.

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.

Q32ZE1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNPKEEIRR IRIVNMLKRG VARVNPLGGL KRLPAGLLLG HGPIRMVLAI
60 70 80 90 100
LAFLRFTAIK PSLGLINRWG SVGKKEAMEI IKKFKKDLAA MLRIINARKE
110 120 130 140 150
RKRRGADTSI GIIGLLLTTA MAAEITRRGS AYYMYLDRSD AGKAISFATT
160 170 180 190 200
LGVNKCHVQI MDLGHMCDAT MSYECPMLDE GVEPDDVDCW CNTTSTWVVY
210 220 230 240 250
GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY TKHLIKVENW
260 270 280 290 300
IFRNPGFALV AVAIAWLLGS 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
GSLVTCAKFT CSKKMTGKSI QPENLEYRIM LSVHGSQHSG MIGYETDEDR
460 470 480 490 500
AKVEVTPNSP RAEATLGGFG SLGLDCEPRT GLDFSDLYYL TMNNKHWLVH
510 520 530 540 550
KEWFHDIPLP WHAGADTGTP HWNNKEALVE FKDAHAKRQT VVVLGSQEGA
560 570 580 590 600
VHTALAGALE AEMDGAKGRL FSGHLKCRLK MDKLRLKGVS YSLCTAAFTF
610 620 630 640 650
TKVPAETLHG TVTVEVQYAG TDGPCKIPVQ MAVDMQTLTP VGRLITANPV
660 670 680 690 700
ITESTENSKM MLELDPPFGD SYIVIGVGDK KITHHWHRSG STIGKAFEAT
710 720 730 740 750
VRGAKRMAVL GDTAWDFGSV GGVFNSLGKG IHQIFGAAFK SLFGGMSWFS
760 770 780 790 800
QILIGTLLVW LGLNTKNGSI SLTCLALGGV MIFLSTAVSA DVGCSVDFSK
810 820 830 840 850
KETRCGTGVF IYNDVEAWRD RYKYHPDSPR RLAAAVKQAW EEGICGISSV
860 870 880 890 900
SRMENIMWKS VEGELNAILE ENGVQLTVVV GSVKNPMWRG PQRLPVPVNE
910 920 930 940 950
LPHGWKAWGK SYFVRAAKTN NSFVVDGDTL KECPLEHRAW NSFLVEDHGF
960 970 980 990 1000
GVFHTSVWLK VREDYSLECD PAVIGTAVKG REAAHSDLGY WIESEKNDTW
1010 1020 1030 1040 1050
RLKRAHLIEM KTCEWPKSHT LWTDGVEESD LIIPKSLAGP LSHHNTREGY
1060 1070 1080 1090 1100
RTQVKGPWHS EELEIRFEEC PGTKVYVEET CGTRGPSLRS TTASGRVIEE
1110 1120 1130 1140 1150
WCCRECTMPP LSFRAKDGCW YGMEIRPRKE PESNLVRSMV TAGSTDHMDH
1160 1170 1180 1190 1200
FSLGVLVILL MVQEGLKKRM TTKIIMSTSM AVLVVMILGG FSMSDLAKLV
1210 1220 1230 1240 1250
ILMGATFAEM NTGGDVAHLA LVAAFKVRPA LLVSFIFRAN WTPRESMLLA
1260 1270 1280 1290 1300
LASCLLQTAI SALEGDLMVL INGFALAWLA IRAMAVPRTD NIALPILAAL
1310 1320 1330 1340 1350
TPLARGTLLV AWRAGLATCG GIMLLSLKGK GSVKKNLPFV MALGLTAVRV
1360 1370 1380 1390 1400
VDPINVVGLL LLTRSGKRSW PPSEVLTAVG LICALAGGFA KADIEMAGPM
1410 1420 1430 1440 1450
AAVGLLIVSY VVSGKSVDMY IERAGDITWE KDAEVTGNSP RLDVALDESG
1460 1470 1480 1490 1500
DFSLVEEDGP PMREIILKVV LMAICGMNPI AIPFAAGAWY VYVKTGKRSG
1510 1520 1530 1540 1550
ALWDVPAPKE VKKGETTDGV YRVMTRRLLG STQVGVGVMQ EGVFHTMWHV
1560 1570 1580 1590 1600
TKGAALRSGE GRLDPYWGDV KQDLVSYCGP WKLDAAWDGL SEVQLLAVPP
1610 1620 1630 1640 1650
GERARNIQTL PGIFKTKDGD IGAVALDYPA GTSGSPILDK CGRVIGLYGN
1660 1670 1680 1690 1700
GVVIKNGSYV SAITQGKREE ETPVECFEPS MLKKKQLTVL DLHPGAGKTR
1710 1720 1730 1740 1750
RVLPEIVREA IKKRLRTVIL APTRVVAAEM EEALRGLPVR YMTTAVNVTH
1760 1770 1780 1790 1800
SGTEIVDLMC HATFTSRLLQ PIRVPNYNLN IMDEAHFTDP SSIAARGYIS
1810 1820 1830 1840 1850
TRVEMGEAAA IFMTATPPGT RDAFPDSNSP IMDTEVEVPE RAWSSGFDWV
1860 1870 1880 1890 1900
TDHSGKTVWF VPSVRNGNEI AACLTKAGKR VIQLSRKTFE TEFQKTKNQE
1910 1920 1930 1940 1950
WDFVITTDIS EMGANFKADR VIDSRRCLKP VILDGERVIL AGPMPVTHAS
1960 1970 1980 1990 2000
AAQRRGRIGR NPNKPGDEYM YGGGCAETDE GHAHWLEARM LLDNIYLQDG
2010 2020 2030 2040 2050
LIASLYRPEA DKVAAIEGEF KLRTEQRKTF VELMKRGDLP VWLAYQVASA
2060 2070 2080 2090 2100
GITYTDRRWC FDGTTNNTIM EDSVPAEVWT KYGEKRVLKP RWMDARVCSD
2110 2120 2130 2140 2150
HAALKSFKEF AAGKRGAALG VMEALGTLPG HMTERFQEAI DNLAVLMRAE
2160 2170 2180 2190 2200
TGSRPYKAAA AQLPETLETI MLLGLLGTVS LGIFFVLMRN KGIGKMGFGM
2210 2220 2230 2240 2250
VTLGASAWLM WLSEIEPARI ACVLIVVFLL LVVLIPEPEK QRSPQDNQMA
2260 2270 2280 2290 2300
IIIMVAVGLL GLITANELGW LERTKNDIAH LMGRREEGAT MGFSMDIDLR
2310 2320 2330 2340 2350
PASAWAIYAA LTTLITPAVQ HAVTTSYNNY SLMAMATQAG VLFGMGKGMP
2360 2370 2380 2390 2400
FMHGDLGVPL LMMGCYSQLT PLTLIVAIIL LVAHYMYLIP GLQAAAARAA
2410 2420 2430 2440 2450
QKRTAAGIMK NPVVDGIVVT DIDTMTIDPQ VEKKMGQVLL IAVAISSAVL
2460 2470 2480 2490 2500
LRTAWGWGEA GALITAATST LWEGSPNKYW NSSTATSLCN IFRGSYLAGA
2510 2520 2530 2540 2550
SLIYTVTRNA GLVKRRGGGT GETLGEKWKA RLNQMSALEF YSYKKSGITE
2560 2570 2580 2590 2600
VCREEARRAL KDGVATGGHA VSRGSAKIRW LEERGYLQPY GKVVDLGCGR
2610 2620 2630 2640 2650
GGWSYYAATI RKVQEVRGYT KGGPGHEEPM LVQSYGWNIV RLKSGVDVFH
2660 2670 2680 2690 2700
MAAEPCDTLL CDIGESSSSP EVEETRTLRV LSMVGDWLEK RPGAFCIKVL
2710 2720 2730 2740 2750
CPYTSTMMET MERLQRRHGG GLVRVPLCRN STHEMYWVSG AKSNIIKSVS
2760 2770 2780 2790 2800
TTSQLLLGRM DGPRRPVKYE EDVNLGSGTR AVASCAEAPN MKIIGRRIER
2810 2820 2830 2840 2850
IRNEHAETWF LDENHPYRTW AYHGSYEAPT QGSASSLVNG VVRLLSKPWD
2860 2870 2880 2890 2900
VVTGVTGIAM TDTTPYGQQR VFKEKVDTRV PDPQEGTRQV MNIVSSWLWK
2910 2920 2930 2940 2950
ELGKRKRPRV CTKEEFINKV RSNAALGAIF EEEKEWKTAV EAVNDPRFWA
2960 2970 2980 2990 3000
LVDREREHHL RGECHSCVYN MMGKREKKQG EFGKAKGSRA IWYMWLGARF
3010 3020 3030 3040 3050
LEFEALGFLN EDHWMGRENS GGGVEGLGLQ RLGYILEEMN RAPGGKMYAD
3060 3070 3080 3090 3100
DTAGWDTRIS KFDLENEALI TNQMEEGHRT LALAVIKYTY QNKVVKVLRP
3110 3120 3130 3140 3150
AEGGKTVMDI ISRQDQRGSG QVVTYALNTF TNLVVQLIRN MEAEEVLEMQ
3160 3170 3180 3190 3200
DLWLLRKPEK VTRWLQSNGW DRLKRMAVSG DDCVVKPIDD RFAHALRFLN
3210 3220 3230 3240 3250
DMGKVRKDTQ EWKPSTGWSN WEEVPFCSHH FNKLYLKDGR SIVVPCRHQD
3260 3270 3280 3290 3300
ELIGRARVSP GAGWSIRETA CLAKSYAQMW QLLYFHRRDL RLMANAICSA
3310 3320 3330 3340 3350
VPVDWVPTGR TTWSIHGKGE WMTTEDMLMV WNRVWIEEND HMEDKTPVTK
3360 3370 3380 3390 3400
WTDIPYLGKR EDLWCGSLIG HRPRTTWAEN IKDTVNMVRR IIGDEEKYMD
3410
YLSTQVRYLG EEGSTPGVL
Length:3,419
Mass (Da):378,736
Last modified:December 6, 2005 - v1
Checksum:iB20F0526BB24B098
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY632535 Genomic RNA. Translation: AAV34151.1.
RefSeqiYP_002790881.1. NC_012532.1.

Genome annotation databases

GeneIDi7751225.
KEGGivg:7751225.

Similar proteinsi

Entry informationi

Entry nameiPOLG_ZIKV
AccessioniPrimary (citable) accession number: Q32ZE1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 16, 2016
Last sequence update: December 6, 2005
Last modified: November 22, 2017
This is version 110 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references