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Protein

Genome polyprotein

Gene
N/A
Organism
Murray valley encephalitis virus (strain MVE-1-51) (MVEV)
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. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.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
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.PROSITE-ProRule annotation1 Publication
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.By similarity
Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Non-structural protein 4B: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. 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.1 Publication
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 sitei1554Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1578Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1638Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1961Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1964Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2542mRNA capPROSITE-ProRule annotation1
Binding sitei2545mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2546mRNA capPROSITE-ProRule annotation1
Binding sitei2548mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2557mRNA capPROSITE-ProRule annotation1
Binding sitei2585S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2590For 2'-O-MTase activityBy similarity1
Sitei2590Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2615S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2616S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2633S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2634S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2660S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2661S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2675For 2'-O-MTase activityBy similarity1
Sitei2675Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2676S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2679mRNA capPROSITE-ProRule annotation1
Active sitei2711For 2'-O-MTase activityBy similarity1
Sitei2711Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2742mRNA capPROSITE-ProRule annotation1
Binding sitei2744mRNA capPROSITE-ProRule annotation1
Active sitei2747For 2'-O-MTase activityBy similarity1
Sitei2747Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2749S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2969Zinc 1By similarity1
Metal bindingi2973Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2978Zinc 1By similarity1
Metal bindingi2981Zinc 1By similarity1
Metal bindingi3246Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3262Zinc 2By similarity1
Metal bindingi3381Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1697 – 1704ATPPROSITE-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 STAT1 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, 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:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.151 Publication, EC:3.6.4.131 Publication)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 5
OrganismiMurray valley encephalitis virus (strain MVE-1-51) (MVEV)
Taxonomic identifieri301478 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus groupMurray Valley encephalitis virus
Virus hostiCulex annulirostris (Common banded mosquito) [TaxID: 162997]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008863 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 :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Note: ER membrane retention is mediated by the transmembrane domains.By similarity
Envelope protein E :
  • Virion membrane Curated; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Note: ER membrane retention is mediated by the transmembrane domains.By similarity
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
Topological domaini2 – 110CytoplasmicSequence analysisAdd BLAST109
Transmembranei111 – 131HelicalSequence analysisAdd BLAST21
Topological domaini132 – 251ExtracellularSequence analysisAdd BLAST120
Transmembranei252 – 272HelicalSequence analysisAdd BLAST21
Topological domaini273 – 277CytoplasmicSequence analysis5
Transmembranei278 – 292HelicalCuratedAdd BLAST15
Topological domaini293 – 745ExtracellularSequence analysisAdd BLAST453
Transmembranei746 – 766HelicalSequence analysisAdd BLAST21
Topological domaini767 – 772CytoplasmicSequence analysis6
Transmembranei773 – 793HelicalSequence analysisAdd BLAST21
Topological domaini794 – 1218ExtracellularSequence analysisAdd BLAST425
Transmembranei1219 – 1239HelicalSequence analysisAdd BLAST21
Topological domaini1240 – 1249CytoplasmicSequence analysis10
Transmembranei1250 – 1270HelicalSequence analysisAdd BLAST21
Topological domaini1271 – 1286LumenalSequence analysisAdd BLAST16
Transmembranei1287 – 1307HelicalSequence analysisAdd BLAST21
Topological domaini1308CytoplasmicSequence analysis1
Transmembranei1309 – 1329HelicalSequence analysisAdd BLAST21
Topological domaini1330 – 1340LumenalSequence analysisAdd BLAST11
Transmembranei1341 – 1361HelicalSequence analysisAdd BLAST21
Topological domaini1362 – 1373CytoplasmicSequence analysisAdd BLAST12
Transmembranei1374 – 1394HelicalSequence analysisAdd BLAST21
Topological domaini1395 – 1397LumenalSequence analysis3
Transmembranei1398 – 1418HelicalSequence analysisAdd BLAST21
Topological domaini1419 – 1475CytoplasmicSequence analysisAdd BLAST57
Intramembranei1476 – 1496HelicalSequence analysisAdd BLAST21
Topological domaini1497 – 2172CytoplasmicSequence analysisAdd BLAST676
Transmembranei2173 – 2193HelicalSequence analysisAdd BLAST21
Topological domaini2194 – 2197LumenalSequence analysis4
Intramembranei2198 – 2218HelicalSequence analysisAdd BLAST21
Topological domaini2219 – 2220LumenalSequence analysis2
Transmembranei2221 – 2241HelicalSequence analysisAdd BLAST21
Topological domaini2242 – 2256CytoplasmicSequence analysisAdd BLAST15
Transmembranei2257 – 2271Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2272 – 2309LumenalSequence analysisAdd BLAST38
Intramembranei2310 – 2330HelicalSequence analysisAdd BLAST21
Topological domaini2331 – 2366LumenalSequence analysisAdd BLAST36
Transmembranei2367 – 2394HelicalSequence analysisAdd BLAST28
Topological domaini2395 – 2446CytoplasmicSequence analysisAdd BLAST52
Transmembranei2447 – 2467HelicalSequence analysisAdd BLAST21
Topological domaini2468 – 2498LumenalSequence analysisAdd BLAST31
Transmembranei2499 – 2519HelicalSequence analysisAdd BLAST21
Topological domaini2520 – 3434CytoplasmicSequence analysisAdd BLAST915

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
Mutagenesisi121 – 124GFAA → PQAQ: Increased cleavage of prM. 1 Publication4

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004051631 – 3434Genome polyproteinAdd BLAST3434
ChainiPRO_00000377821 – 105Capsid protein CBy similarityAdd BLAST105
PropeptideiPRO_0000405164106 – 125ER anchor for the capsid protein C, removed in mature form by serine protease NS3Add BLAST20
ChainiPRO_0000405165126 – 292Protein prMBy similarityAdd BLAST167
ChainiPRO_0000037783126 – 217Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037784218 – 292Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037785293 – 793Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000037786794 – 1145Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000377871146 – 1372Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00000377881373 – 1503Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000377891504 – 2122Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00000377902123 – 2248Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051662249 – 2271Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000377912272 – 2529Non-structural protein 4BBy similarityAdd BLAST258
ChainiPRO_00000377922530 – 3434RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi140N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi295 ↔ 322By similarity
Disulfide bondi352 ↔ 413By similarity
Disulfide bondi352 ↔ 408By similarity
Disulfide bondi366 ↔ 397By similarity
Disulfide bondi384 ↔ 413By similarity
Disulfide bondi384 ↔ 408By similarity
Glycosylationi446N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi482 ↔ 580By similarity
Disulfide bondi597 ↔ 628By similarity
Disulfide bondi797 ↔ 8081 Publication
Disulfide bondi848 ↔ 9361 Publication
Glycosylationi923N-linked (GlcNAc...) asparagine; by host1 Publication1
Glycosylationi968N-linked (GlcNAc...) asparagine; by host1 Publication1
Disulfide bondi972 ↔ 10161 Publication
Glycosylationi1000N-linked (GlcNAc...) (high mannose) asparagine; by host1 Publication1
Disulfide bondi1073 ↔ 1122By similarity
Disulfide bondi1084 ↔ 1105By similarity
Disulfide bondi1106 ↔ 1109By similarity
Modified residuei2585PhosphoserineBy 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.5 Publications
Protein prM: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
Envelope protein E: N-glycosylated.1 Publication
Non-structural protein 1: N-glycosylated (PubMed:11514736). The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells (By similarity).By similarity1 Publication
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei105 – 106Cleavage; by viral protease NS3Sequence analysis2
Sitei125 – 126Cleavage; by host signal peptidase1 Publication2
Sitei217 – 218Cleavage; by host furinBy similarity2
Sitei292 – 293Cleavage; by host signal peptidaseSequence analysis2
Sitei793 – 794Cleavage; by host signal peptidaseSequence analysis2
Sitei1145 – 1146Cleavage; by host1 Publication2
Sitei1372 – 1373Cleavage; by viral protease NS3Sequence analysis2
Sitei1503 – 1504Cleavage; by autolysisSequence analysis2
Sitei2122 – 2123Cleavage; by autolysisSequence analysis2
Sitei2248 – 2249Cleavage; by viral protease NS3Sequence analysis2
Sitei2271 – 2272Cleavage; by host signal peptidaseSequence analysis2
Sitei2529 – 2530Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

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

Proteomic databases

PRIDEiP05769

PTM databases

iPTMnetiP05769

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: Homohexamer when secreted. NS1 interacts with NS4B. Interacts with host complement protein CFH; this interaction leads to the degradation of C3. 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 NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. Non-structural protein 4B: Interacts with serine protease NS3. RNA-directed RNA polymerase NS5: Homodimer. Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation. Interacts with serine protease NS3.By similarity

GO - Molecular functioni

Structurei

Secondary structure

13434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1423 – 1430Combined sources8
Beta strandi1436 – 1440Combined sources5
Beta strandi1523 – 1531Combined sources9
Beta strandi1536 – 1545Combined sources10
Beta strandi1548 – 1551Combined sources4
Helixi1553 – 1556Combined sources4
Beta strandi1564 – 1568Combined sources5
Beta strandi1570 – 1574Combined sources5
Turni1575 – 1578Combined sources4
Beta strandi1579 – 1585Combined sources7
Beta strandi1598 – 1602Combined sources5
Beta strandi1610 – 1614Combined sources5
Beta strandi1617 – 1619Combined sources3
Beta strandi1622 – 1624Combined sources3
Beta strandi1626 – 1629Combined sources4
Helixi1635 – 1637Combined sources3
Beta strandi1641 – 1643Combined sources3
Beta strandi1649 – 1658Combined sources10
Beta strandi1660 – 1662Combined sources3
Beta strandi1664 – 1669Combined sources6
Helixi1684 – 1687Combined sources4
Beta strandi1692 – 1695Combined sources4
Beta strandi1699 – 1701Combined sources3
Turni1703 – 1706Combined sources4
Helixi1707 – 1717Combined sources11
Beta strandi1722 – 1728Combined sources7
Helixi1729 – 1738Combined sources10
Turni1739 – 1741Combined sources3
Beta strandi1744 – 1746Combined sources3
Beta strandi1761 – 1765Combined sources5
Helixi1766 – 1773Combined sources8
Beta strandi1775 – 1777Combined sources3
Beta strandi1783 – 1789Combined sources7
Helixi1795 – 1809Combined sources15
Beta strandi1814 – 1818Combined sources5
Beta strandi1836 – 1840Combined sources5
Beta strandi1849 – 1851Combined sources3
Helixi1853 – 1857Combined sources5
Beta strandi1862 – 1865Combined sources4
Helixi1869 – 1881Combined sources13
Beta strandi1886 – 1889Combined sources4
Turni1891 – 1893Combined sources3
Helixi1894 – 1901Combined sources8
Beta strandi1907 – 1911Combined sources5
Helixi1913 – 1916Combined sources4
Beta strandi1924 – 1928Combined sources5
Beta strandi1935 – 1938Combined sources4
Beta strandi1944 – 1947Combined sources4
Beta strandi1950 – 1952Combined sources3
Helixi1955 – 1962Combined sources8
Beta strandi1974 – 1978Combined sources5
Helixi1990 – 1999Combined sources10
Turni2005 – 2007Combined sources3
Helixi2014 – 2016Combined sources3
Turni2024 – 2027Combined sources4
Helixi2031 – 2042Combined sources12
Helixi2048 – 2055Combined sources8
Turni2056 – 2058Combined sources3
Helixi2064 – 2067Combined sources4
Helixi2072 – 2074Combined sources3
Beta strandi2078 – 2081Combined sources4
Beta strandi2098 – 2101Combined sources4
Helixi2102 – 2104Combined sources3
Helixi2108 – 2118Combined sources11
Helixi2537 – 2546Combined sources10
Helixi2550 – 2557Combined sources8
Turni2558 – 2560Combined sources3
Beta strandi2562 – 2564Combined sources3
Helixi2566 – 2568Combined sources3
Turni2571 – 2576Combined sources6
Beta strandi2578 – 2580Combined sources3
Beta strandi2584 – 2586Combined sources3
Helixi2587 – 2596Combined sources10
Beta strandi2604 – 2609Combined sources6
Helixi2615 – 2620Combined sources6
Beta strandi2626 – 2632Combined sources7
Helixi2650 – 2652Combined sources3
Beta strandi2653 – 2656Combined sources4
Helixi2661 – 2663Combined sources3
Beta strandi2670 – 2674Combined sources5
Helixi2683 – 2701Combined sources19
Beta strandi2706 – 2713Combined sources8
Helixi2718 – 2731Combined sources14
Beta strandi2734 – 2736Combined sources3
Beta strandi2748 – 2751Combined sources4
Helixi2758 – 2771Combined sources14
Turni2772 – 2774Combined sources3
Beta strandi2782 – 2784Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PX2X-ray2.00A/B2530-2798[»]
2PX4X-ray2.20A2530-2798[»]
2PX5X-ray2.30A/B2530-2798[»]
2PX8X-ray2.20A/B2530-2798[»]
2PXAX-ray2.30A/B2530-2798[»]
2PXCX-ray2.80A2530-2798[»]
2V8OX-ray1.90A1681-2122[»]
2WV9X-ray2.75A1421-1465[»]
A1504-2122[»]
ProteinModelPortaliP05769
SMRiP05769
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05769

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1504 – 1681Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1684 – 1840Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1851 – 2016Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2530 – 2795mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3059 – 3211RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni390 – 403Fusion peptideBy similarityAdd BLAST14
Regioni1426 – 1465Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1688 – 1691Important for RNA-bindingBy similarity4
Regioni2167 – 2171Regulates the ATPase activity of NS3 helicaseBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1788 – 1791DEAH 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

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

OrthoDBiVOG090000B1

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
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
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.

P05769-1 [UniParc]FASTAAdd to basket

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        10         20         30         40         50
MSKKPGGPGK PRVVNMLKRG IPRVFPLVGV KRVVMNLLDG RGPIRFVLAL
60 70 80 90 100
LAFFRFTALA PTKALMRRWK SVNKTTAMKH LTSFKKELGT LIDVVNKRGK
110 120 130 140 150
KQKKRGGSET SVLMLIFMLI GFAAALKLST FQGKIMMTVN ATDIADVIAI
160 170 180 190 200
PTPKGPNQCW IRAIDIGFMC DDTITYECPK LESGNDPEDI DCWCDKQAVY
210 220 230 240 250
VNYGRCTRAR HSKRSRRSIT VQTHGESTLV NKKDAWLDST KATRYLTKTE
260 270 280 290 300
NWIIRNPGYA LVAVVLGWML GSNTGQKVIF TVLLLLVAPA YSFNCLGMSS
310 320 330 340 350
RDFIEGASGA TWVDLVLEGD SCITIMAADK PTLDIRMMNI EATNLALVRN
360 370 380 390 400
YCYAATVSDV STVSNCPTTG ESHNTKRADH NYLCKRGVTD RGWGNGCGLF
410 420 430 440 450
GKGSIDTCAK FTCSNSAAGR LILPEDIKYE VGVFVHGSTD STSHGNYSTQ
460 470 480 490 500
IGANQAVRFT ISPNAPAITA KMGDYGEVTV ECEPRSGLNT EAYYVMTIGT
510 520 530 540 550
KHFLVHREWF NDLLLPWTSP ASTEWRNREI LVEFEEPHAT KQSVVALGSQ
560 570 580 590 600
EGALHQALAG AIPVEFSSST LKLTSGHLKC RVKMEKLKLK GTTYGMCTEK
610 620 630 640 650
FTFSKNPADT GHGTVVLELQ YTGSDGPCKI PISSVASLND MTPVGRMVTA
660 670 680 690 700
NPYVASSTAN AKVLVEIEPP FGDSYIVVGR GDKQINHHWH KEGSSIGKAF
710 720 730 740 750
STTLKGAQRL AALGDTAWDF GSVGGVFNSI GKAVHQVFGG AFRTLFGGMS
760 770 780 790 800
WISPGLLGAL LLWMGVNARD KSIALAFLAT GGVLLFLATN VHADTGCAID
810 820 830 840 850
ITRRELKCGS GIFIHNDVEA WIDRYKYLPE TPKQLAKVVE NAHKSGICGI
860 870 880 890 900
RSVNRFEHQM WESVRDELNA LLKENAIDLS VVVEKQKGMY RAAPNRLRLT
910 920 930 940 950
VEELDIGWKA WGKSLLFAAE LANSTFVVDG PETAECPNSK RAWNSFEIED
960 970 980 990 1000
FGFGITSTRG WLKLREENTS ECDSTIIGTA VKGNHAVHSD LSYWIESGLN
1010 1020 1030 1040 1050
GTWKLERAIF GEVKSCTWPE THTLWGDAVE ETELIIPVTL AGPRSKHNRR
1060 1070 1080 1090 1100
EGYKVQVQGP WDEEDIKLDF DYCPGTTVTV SEHCGKRGPS VRTTTDSGKL
1110 1120 1130 1140 1150
VTDWCCRSCT LPPLRFTTAS GCWYGMEIRP MKHDESTLVK SRVQAFNGDM
1160 1170 1180 1190 1200
IDPFQLGLLV MFLATQEVLR KRWTARLTLP AAVGALLVLL LGGITYTDLV
1210 1220 1230 1240 1250
RYLILVGSAF AESNNGGDVI HLALIAVFKV QPAFLVASLT RSRWTNQENL
1260 1270 1280 1290 1300
VLVLGAAFFQ MAASDLELTI PGLLNSAATA WMVLRAMAFP STSAIAMPML
1310 1320 1330 1340 1350
AMLAPGMRML HLDTYRIVLL LIGICSLLNE RRRSVEKKKG AVLIGLALTS
1360 1370 1380 1390 1400
TGYFSPTIMA AGLMICNPNK KRGWPATEVL TAVGLMFAIV GGLAELDIDS
1410 1420 1430 1440 1450
MSVPFTIAGL MLVSYVISGK ATDMWLERAA DVSWEAGAAI TGTSERLDVQ
1460 1470 1480 1490 1500
LDDDGDFHLL NDPGVPWKIW VLRMTCLSVA AITPRAILPS AFGYWLTLKY
1510 1520 1530 1540 1550
TKRGGVFWDT PSPKVYPKGD TTPGVYRIMA RGILGRYQAG VGVMHEGVFH
1560 1570 1580 1590 1600
TLWHTTRGAA IMSGEGRLTP YWGNVKEDRV TYGGPWKLDQ KWNGVDDVQM
1610 1620 1630 1640 1650
IVVEPGKPAI NVQTKPGIFK TAHGEIGAVS LDYPIGTSGS PIVNSNGEII
1660 1670 1680 1690 1700
GLYGNGVILG NGAYVSAIVQ GERVEEPVPE AYNPEMLKKR QLTVLDLHPG
1710 1720 1730 1740 1750
AGKTRRILPQ IIKDAIQKRL RTAVLAPTRV VAAEMAEALR GLPVRYLTPA
1760 1770 1780 1790 1800
VQREHSGNEI VDVMCHATLT HRLMSPLRVP NYNLFVMDEA HFTDPASIAA
1810 1820 1830 1840 1850
RGYIATRVEA GEAAAIFMTA TPPGTSDPFP DTNSPVHDVS SEIPDRAWSS
1860 1870 1880 1890 1900
GFEWITDYAG KTVWFVASVK MSNEIAQCLQ RAGKRVIQLN RKSYDTEYPK
1910 1920 1930 1940 1950
CKNGDWDFVI TTDISEMGAN FGASRVIDCR KSVKPTILDE GEGRVILSVP
1960 1970 1980 1990 2000
SAITSASAAQ RRGRVGRNPS QIGDEYHYGG GTSEDDTMLA HWTEAKILLD
2010 2020 2030 2040 2050
NIHLPNGLVA QLYGPERDKT YTMDGEYRLR GEERKTFLEL IKTADLPVWL
2060 2070 2080 2090 2100
AYKVASNGIQ YNDRKWCFDG PRSNIILEDN NEVEIITRIG ERKVLKPRWL
2110 2120 2130 2140 2150
DARVYSDHQS LKWFKDFAAG KRSAIGFFEV LGRMPEHFAG KTREALDTMY
2160 2170 2180 2190 2200
LVATSEKGGK AHRMALEELP DALETITLIA ALGVMTAGFF LLMMQRKGIG
2210 2220 2230 2240 2250
KLGLGALVLV VATFFLWMSD VSGTKIAGVL LLALLMMVVL IPEPEKQRSQ
2260 2270 2280 2290 2300
TDNQLAVFLI CVLLVVGLVA ANEYGMLERT KTDIRNLFGK SLIEENEVHI
2310 2320 2330 2340 2350
PPFDFFTLDL KPATAWALYG GSTVVLTPLI KHLVTSQYVT TSLASINAQA
2360 2370 2380 2390 2400
GSLFTLPKGI PFTDFDLSVA LVFLGCWGQV TLTTLIMATI LVTLHYGYLL
2410 2420 2430 2440 2450
PGWQAEALRA AQKRTAAGIM KNAVVDGIVA TDVPELERTT PQMQKRLGQI
2460 2470 2480 2490 2500
LLVLASVAAV CVNPRITTIR EAGILCTAAA LTLWDNNASA AWNSTTATGL
2510 2520 2530 2540 2550
CHVMRGSWIA GASIAWTLIK NAEKPAFKRG RAGGRTLGEQ WKEKLNAMGK
2560 2570 2580 2590 2600
EEFFSYRKEA ILEVDRTEAR RARREGNKVG GHPVSRGTAK LRWLVERRFV
2610 2620 2630 2640 2650
QPIGKVVDLG CGRGGWSYYA ATMKNVQEVR GYTKGGPGHE EPMLMQSYGW
2660 2670 2680 2690 2700
NIVTMKSGVD VFYKPSEISD TLLCDIGESS PSAEIEEQRT LRILEMVSDW
2710 2720 2730 2740 2750
LSRGPKEFCI KILCPYMPKV IEKLESLQRR FGGGLVRVPL SRNSNHEMYW
2760 2770 2780 2790 2800
VSGASGNIVH AVNMTSQVLI GRMDKKIWKG PKYEEDVNLG SGTRAVGKGV
2810 2820 2830 2840 2850
QHTDYKRIKS RIEKLKEEYA ATWHTDDNHP YRTWTYHGSY EVKPSGSAST
2860 2870 2880 2890 2900
LVNGVVRLLS KPWDAITGVT TMAMTDTTPF GQQRVFKEKV DTKAPEPPQG
2910 2920 2930 2940 2950
VKTVMDETTN WLWAYLARNK KARLCTREEF VKKVNSHAAL GAMFEEQNQW
2960 2970 2980 2990 3000
KNAREAVEDP KFWEMVDEER ECHLRGECRT CIYNMMGKRE KKPGEFGKAK
3010 3020 3030 3040 3050
GSRAIWFMWL GARFLEFEAL GFLNEDHWMS RENSGGGVEG AGIQKLGYIL
3060 3070 3080 3090 3100
RDVAQKPGGK IYADDTAGWD TRITQADLEN EAKVLELMEG EQRTLARAII
3110 3120 3130 3140 3150
ELTYRHKVVK VMRPAAGGKT VMDVISREDQ RGSGQVVTYA LNTFTNIAVQ
3160 3170 3180 3190 3200
LVRLMEAEAV IGPDDIESIE RKKKFAVRTW LFENAEERVQ RMAVSGDDCV
3210 3220 3230 3240 3250
VKPLDDRFST ALHFLNAMSK VRKDIQEWKP SQGWYDWQQV PFCSNHFQEV
3260 3270 3280 3290 3300
IMKDGRTLVV PCRGQDELIG RARISPGSGW NVRDTACLAK AYAQMWLVLY
3310 3320 3330 3340 3350
FHRRDLRLMA NAICSSVPVD WVPTGRTTWS IHGKGEWMTT EDMLSVWNRV
3360 3370 3380 3390 3400
WILENEWMED KTTVSDWTEV PYVGKREDIW CGSLIGTRTR ATWAENIYAA
3410 3420 3430
INQVRSVIGK EKYVDYVQSL RRYEETHVSE DRVL
Length:3,434
Mass (Da):380,577
Last modified:December 21, 2004 - v2
Checksum:i20D7110791C567A9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115L → V in CAA27184 (PubMed:3009829).Curated1
Sequence conflicti754P → Q in CAA27184 (PubMed:3009829).Curated1
Sequence conflicti960G → V in CAA27184 (PubMed:3009829).Curated1
Sequence conflicti1485R → W in CAA27184 (PubMed:3009829).Curated1
Sequence conflicti1779V → G in CAA27184 (PubMed:3009829).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161266 Genomic RNA Translation: AAF05296.1
X03467 Unassigned RNA Translation: CAA27184.1
PIRiA24635 GNWVMV
RefSeqiNP_051124.1, NC_000943.1

Genome annotation databases

GeneIDi1489715
KEGGivg:1489715

Similar proteinsi

Entry informationi

Entry nameiPOLG_MVEV5
AccessioniPrimary (citable) accession number: P05769
Secondary accession number(s): Q9Q9F7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 21, 2004
Last modified: May 23, 2018
This is version 165 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

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

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