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Protein

Genome polyprotein

Gene
N/A
Organism
Japanese encephalitis virus (strain SA-14)
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 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 (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:16731929). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:16731929).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 sitei1555Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1579Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1639Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1962Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1965Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2540mRNA capPROSITE-ProRule annotation1
Binding sitei2543mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2544mRNA capPROSITE-ProRule annotation1
Binding sitei2546mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2551mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2555mRNA capPROSITE-ProRule annotation1
Binding sitei2583S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2588For 2'-O-MTase activityBy similarity1
Sitei2588Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2613S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2614S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2631S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2632S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2658S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2659S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2673For 2'-O-MTase activityBy similarity1
Sitei2673Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2674S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2677mRNA capPROSITE-ProRule annotation1
Active sitei2709For 2'-O-MTase activityBy similarity1
Sitei2709Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2740mRNA capPROSITE-ProRule annotation1
Binding sitei2742mRNA capPROSITE-ProRule annotation1
Active sitei2745For 2'-O-MTase activityBy similarity1
Sitei2745Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2747S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2967Zinc 11 Publication1
Metal bindingi2971Zinc 1; via tele nitrogen1 Publication1
Metal bindingi2976Zinc 11 Publication1
Metal bindingi2979Zinc 11 Publication1
Metal bindingi3244Zinc 2; via tele nitrogen1 Publication1
Metal bindingi3260Zinc 21 Publication1
Metal bindingi3379Zinc 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1698 – 1705ATPPROSITE-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, 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

Enzyme and pathway databases

BRENDAi3.6.4.12 2787
3.6.4.13 2787

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
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
OrganismiJapanese encephalitis virus (strain SA-14)
Taxonomic identifieri11073 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Virus hostiArdeidae (herons) [TaxID: 8899]
Bos taurus (Bovine) [TaxID: 9913]
Culex gelidus [TaxID: 308713]
Culex tritaeniorhynchus (Mosquito) [TaxID: 7178]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000008380 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 By similarity
  • Host nucleus 1 Publication
  • 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 – 109CytoplasmicSequence analysisAdd BLAST108
Transmembranei110 – 130HelicalSequence analysisAdd BLAST21
Topological domaini131 – 253ExtracellularSequence analysisAdd BLAST123
Transmembranei254 – 274HelicalSequence analysisAdd BLAST21
Topological domaini275 – 279CytoplasmicSequence analysis5
Transmembranei280 – 294HelicalCuratedAdd BLAST15
Topological domaini295 – 746ExtracellularSequence analysisAdd BLAST452
Transmembranei747 – 767HelicalSequence analysisAdd BLAST21
Topological domaini768 – 773CytoplasmicSequence analysis6
Transmembranei774 – 794HelicalSequence analysisAdd BLAST21
Topological domaini795 – 1219ExtracellularSequence analysisAdd BLAST425
Transmembranei1220 – 1240HelicalSequence analysisAdd BLAST21
Topological domaini1241 – 1250CytoplasmicSequence analysis10
Transmembranei1251 – 1271HelicalSequence analysisAdd BLAST21
Topological domaini1272LumenalSequence analysis1
Transmembranei1273 – 1293HelicalSequence analysisAdd BLAST21
Topological domaini1294 – 1309CytoplasmicSequence analysisAdd BLAST16
Transmembranei1310 – 1330HelicalSequence analysisAdd BLAST21
Topological domaini1331 – 1341LumenalSequence analysisAdd BLAST11
Transmembranei1342 – 1362HelicalSequence analysisAdd BLAST21
Topological domaini1363 – 1374CytoplasmicSequence analysisAdd BLAST12
Transmembranei1375 – 1395HelicalSequence analysisAdd BLAST21
Topological domaini1396 – 1398LumenalSequence analysis3
Transmembranei1399 – 1419HelicalSequence analysisAdd BLAST21
Topological domaini1420 – 1476CytoplasmicSequence analysisAdd BLAST57
Intramembranei1477 – 1497HelicalSequence analysisAdd BLAST21
Topological domaini1498 – 2173CytoplasmicSequence analysisAdd BLAST676
Transmembranei2174 – 2194HelicalSequence analysisAdd BLAST21
Topological domaini2195 – 2199LumenalSequence analysis5
Intramembranei2200 – 2220HelicalSequence analysisAdd BLAST21
Topological domaini2221LumenalSequence analysis1
Transmembranei2222 – 2242HelicalSequence analysisAdd BLAST21
Topological domaini2243 – 2257CytoplasmicSequence analysisAdd BLAST15
Transmembranei2258 – 2278Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2279 – 2311LumenalSequence analysisAdd BLAST33
Intramembranei2312 – 2332HelicalSequence analysisAdd BLAST21
Topological domaini2333 – 2368LumenalSequence analysisAdd BLAST36
Transmembranei2369 – 2389HelicalSequence analysisAdd BLAST21
Topological domaini2390 – 2444CytoplasmicSequence analysisAdd BLAST55
Transmembranei2445 – 2465HelicalSequence analysisAdd BLAST21
Topological domaini2466 – 2469LumenalSequence analysis4
Transmembranei2470 – 2490HelicalSequence analysisAdd BLAST21
Topological domaini2491 – 3432CytoplasmicSequence analysisAdd BLAST942

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
Mutagenesisi1703G → A: Complete loss of both the ATPase and helicase activities. 1 Publication1
Mutagenesisi1704K → D, E, H, N, Q or R: Complete loss of both the ATPase and helicase activities. 1 Publication1
Mutagenesisi1705T → A: Complete loss of both the ATPase and helicase activities. 1 Publication1
Mutagenesisi1961Q → A: 80% loss of ATPase activity. 1 Publication1
Mutagenesisi1962R → A: 90% loss of ATPase activity. 1 Publication1
Mutagenesisi1965R → A: Complete loss of ATPase activity. 1 Publication1
Mutagenesisi1968R → A: Complete loss of ATPase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004051881 – 3432Genome polyproteinAdd BLAST3432
ChainiPRO_00000378361 – 105Capsid protein CBy similarityAdd BLAST105
PropeptideiPRO_0000405189106 – 127ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST22
ChainiPRO_0000405190128 – 294Protein prMBy similarityAdd BLAST167
ChainiPRO_0000037837128 – 219Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037838220 – 294Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037839295 – 794Envelope protein EBy similarityAdd BLAST500
ChainiPRO_0000037840795 – 1146Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000378411147 – 1373Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00000378421374 – 1504Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000378431505 – 2123Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00000378442124 – 2249Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051912250 – 2272Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000378452273 – 2527Non-structural protein 4BBy similarityAdd BLAST255
ChainiPRO_00000378462528 – 3432RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi142N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi297 ↔ 324By similarity
Disulfide bondi354 ↔ 415By similarity
Disulfide bondi354 ↔ 410By similarity
Disulfide bondi368 ↔ 399By similarity
Disulfide bondi386 ↔ 415By similarity
Disulfide bondi386 ↔ 410By similarity
Glycosylationi448N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi484 ↔ 581By similarity
Disulfide bondi598 ↔ 629By similarity
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 residuei2583PhosphoserineBy 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
Sitei105 – 106Cleavage; by viral protease NS3Sequence analysis2
Sitei127 – 128Cleavage; by host signal peptidaseBy similarity2
Sitei219 – 220Cleavage; by host furinBy similarity2
Sitei294 – 295Cleavage; by host signal peptidaseSequence analysis2
Sitei794 – 795Cleavage; by host signal peptidaseSequence analysis2
Sitei1146 – 1147Cleavage; by hostBy similarity2
Sitei1373 – 1374Cleavage; by viral protease NS3Sequence analysis2
Sitei1504 – 1505Cleavage; by autolysisSequence analysis2
Sitei2123 – 2124Cleavage; by autolysisSequence analysis2
Sitei2249 – 2250Cleavage; by viral protease NS3Sequence analysis2
Sitei2272 – 2273Cleavage; by host signal peptidaseSequence analysis2
Sitei2527 – 2528Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

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

Proteomic databases

PRIDEiP27395

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

13432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi301 – 307Combined sources7
Beta strandi313 – 322Combined sources10
Beta strandi324 – 328Combined sources5
Beta strandi335 – 344Combined sources10
Beta strandi348 – 366Combined sources19
Helixi377 – 380Combined sources4
Beta strandi384 – 394Combined sources11
Helixi395 – 397Combined sources3
Beta strandi403 – 423Combined sources21
Beta strandi428 – 437Combined sources10
Turni443 – 447Combined sources5
Helixi449 – 454Combined sources6
Beta strandi458 – 463Combined sources6
Beta strandi465 – 467Combined sources3
Beta strandi469 – 473Combined sources5
Helixi475 – 477Combined sources3
Beta strandi478 – 485Combined sources8
Helixi486 – 488Combined sources3
Beta strandi494 – 500Combined sources7
Beta strandi503 – 508Combined sources6
Turni509 – 514Combined sources6
Beta strandi519 – 521Combined sources3
Beta strandi524 – 528Combined sources5
Helixi530 – 533Combined sources4
Beta strandi534 – 540Combined sources7
Beta strandi543 – 548Combined sources6
Helixi553 – 559Combined sources7
Beta strandi561 – 575Combined sources15
Beta strandi578 – 584Combined sources7
Turni591 – 594Combined sources4
Beta strandi602 – 610Combined sources9
Beta strandi612 – 614Combined sources3
Beta strandi616 – 622Combined sources7
Beta strandi628 – 630Combined sources3
Beta strandi633 – 638Combined sources6
Beta strandi641 – 644Combined sources4
Beta strandi646 – 650Combined sources5
Beta strandi662 – 669Combined sources8
Beta strandi672 – 681Combined sources10
Helixi682 – 684Combined sources3
Beta strandi686 – 692Combined sources7
Helixi975 – 977Combined sources3
Beta strandi978 – 983Combined sources6
Beta strandi986 – 1013Combined sources28
Helixi1021 – 1023Combined sources3
Helixi1032 – 1034Combined sources3
Helixi1039 – 1041Combined sources3
Beta strandi1064 – 1066Combined sources3
Beta strandi1068 – 1072Combined sources5
Beta strandi1078 – 1081Combined sources4
Beta strandi1092 – 1095Combined sources4
Beta strandi1104 – 1109Combined sources6
Beta strandi1115 – 1119Combined sources5
Beta strandi1122 – 1125Combined sources4
Helixi1686 – 1688Combined sources3
Beta strandi1693 – 1696Combined sources4
Turni1704 – 1707Combined sources4
Helixi1708 – 1718Combined sources11
Beta strandi1723 – 1727Combined sources5
Helixi1730 – 1739Combined sources10
Turni1740 – 1742Combined sources3
Beta strandi1745 – 1747Combined sources3
Beta strandi1761 – 1766Combined sources6
Helixi1767 – 1775Combined sources9
Beta strandi1784 – 1790Combined sources7
Helixi1796 – 1810Combined sources15
Beta strandi1815 – 1819Combined sources5
Beta strandi1837 – 1841Combined sources5
Helixi1854 – 1858Combined sources5
Beta strandi1863 – 1866Combined sources4
Helixi1870 – 1882Combined sources13
Beta strandi1887 – 1891Combined sources5
Helixi1894 – 1898Combined sources5
Helixi1899 – 1901Combined sources3
Beta strandi1902 – 1904Combined sources3
Beta strandi1908 – 1914Combined sources7
Beta strandi1925 – 1929Combined sources5
Beta strandi1936 – 1939Combined sources4
Beta strandi1941 – 1943Combined sources3
Beta strandi1945 – 1948Combined sources4
Helixi1956 – 1963Combined sources8
Beta strandi1975 – 1979Combined sources5
Helixi1991 – 2001Combined sources11
Helixi2015 – 2020Combined sources6
Turni2025 – 2028Combined sources4
Helixi2032 – 2043Combined sources12
Helixi2049 – 2057Combined sources9
Helixi2066 – 2068Combined sources3
Helixi2073 – 2075Combined sources3
Beta strandi2085 – 2087Combined sources3
Beta strandi2093 – 2095Combined sources3
Beta strandi2099 – 2102Combined sources4
Helixi2103 – 2106Combined sources4
Helixi2109 – 2120Combined sources12
Helixi2535 – 2544Combined sources10
Helixi2548 – 2554Combined sources7
Turni2555 – 2558Combined sources4
Beta strandi2560 – 2562Combined sources3
Helixi2565 – 2572Combined sources8
Helixi2585 – 2593Combined sources9
Turni2594 – 2596Combined sources3
Beta strandi2602 – 2607Combined sources6
Helixi2613 – 2619Combined sources7
Beta strandi2624 – 2630Combined sources7
Helixi2648 – 2650Combined sources3
Beta strandi2651 – 2654Combined sources4
Helixi2659 – 2661Combined sources3
Beta strandi2668 – 2672Combined sources5
Helixi2681 – 2699Combined sources19
Beta strandi2704 – 2711Combined sources8
Helixi2716 – 2729Combined sources14
Beta strandi2732 – 2734Combined sources3
Beta strandi2746 – 2749Combined sources4
Helixi2756 – 2770Combined sources15
Beta strandi2780 – 2782Combined sources3
Helixi2802 – 2816Combined sources15
Turni2817 – 2820Combined sources4
Beta strandi2830 – 2839Combined sources10
Helixi2852 – 2856Combined sources5
Helixi2859 – 2863Combined sources5
Helixi2865 – 2868Combined sources4
Beta strandi2870 – 2872Combined sources3
Helixi2877 – 2887Combined sources11
Helixi2897 – 2914Combined sources18
Turni2915 – 2917Combined sources3
Helixi2925 – 2932Combined sources8
Turni2933 – 2935Combined sources3
Helixi2943 – 2945Combined sources3
Turni2946 – 2948Combined sources3
Helixi2951 – 2956Combined sources6
Helixi2958 – 2972Combined sources15
Beta strandi2981 – 2987Combined sources7
Beta strandi2989 – 2991Combined sources3
Turni2994 – 2996Combined sources3
Beta strandi3001 – 3005Combined sources5
Helixi3008 – 3018Combined sources11
Helixi3020 – 3023Combined sources4
Turni3024 – 3027Combined sources4
Helixi3029 – 3032Combined sources4
Beta strandi3033 – 3035Combined sources3
Helixi3041 – 3053Combined sources13
Beta strandi3054 – 3057Combined sources4
Helixi3067 – 3069Combined sources3
Helixi3073 – 3079Combined sources7
Helixi3080 – 3085Combined sources6
Helixi3088 – 3100Combined sources13
Turni3101 – 3103Combined sources3
Beta strandi3104 – 3113Combined sources10
Turni3114 – 3116Combined sources3
Beta strandi3117 – 3126Combined sources10
Helixi3136 – 3155Combined sources20
Helixi3161 – 3163Combined sources3
Helixi3169 – 3187Combined sources19
Beta strandi3190 – 3193Combined sources4
Beta strandi3196 – 3199Combined sources4
Helixi3204 – 3208Combined sources5
Helixi3211 – 3215Combined sources5
Beta strandi3220 – 3223Combined sources4
Beta strandi3232 – 3234Combined sources3
Helixi3235 – 3237Combined sources3
Beta strandi3243 – 3249Combined sources7
Beta strandi3255 – 3260Combined sources6
Helixi3263 – 3270Combined sources8
Beta strandi3272 – 3275Combined sources4
Helixi3280 – 3297Combined sources18
Helixi3302 – 3314Combined sources13
Beta strandi3336 – 3339Combined sources4
Helixi3341 – 3349Combined sources9
Turni3350 – 3352Combined sources3
Helixi3365 – 3367Combined sources3
Helixi3373 – 3378Combined sources6
Helixi3386 – 3406Combined sources21
Helixi3415 – 3417Combined sources3
Helixi3419 – 3421Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z83X-ray1.80A1685-2123[»]
3P54X-ray2.10A295-700[»]
4HDGX-ray2.38A/B2799-3432[»]
4HDHX-ray2.28A/B2799-3432[»]
4K6MX-ray2.60A/B2528-3432[»]
4MTPX-ray3.65A/B/C/D2799-3432[»]
5O19X-ray2.10A965-1146[»]
5O36X-ray2.60A965-1158[»]
5WSNelectron microscopy4.30B/D/F220-293[»]
ProteinModelPortaliP27395
SMRiP27395
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27395

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1505 – 1682Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1685 – 1841Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1852 – 2017Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2528 – 2793mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3057 – 3209RdRp 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
Regioni392 – 405Fusion peptideBy similarityAdd BLAST14
Regioni1427 – 1466Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1689 – 1692Important for RNA-bindingBy similarity4
Regioni2168 – 2172Regulates the ATPase activity of NS3 helicaseBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1789 – 1792DEAH 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

OrthoDBiVOG0900007N

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, 3 hits
3.30.387.10, 2 hits
3.30.67.10, 4 hits
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
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
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

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Isoform Genome polyprotein (identifier: P27395-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL
60 70 80 90 100
ITFFKFTALA PTKALLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR
110 120 130 140 150
KQNKRGGNEG SIMWLASLAV VIACAGAMKL SNFQGKLLMT INNTDIADVI
160 170 180 190 200
VIPTSKGENR CWVRAIDVGY MCEDTITYEC PKLTMGNDPE DVDCWCDNQE
210 220 230 240 250
VYVQYGRCTR TRHSKRSRRS VSVQTHGESS LVNKKEAWLD STKATRYLMK
260 270 280 290 300
TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM
310 320 330 340 350
GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV
360 370 380 390 400
RSYCYHASVT DISTVARCPT TGEAHNEKRA DSSYVCKQGF TDRGWGNGCG
410 420 430 440 450
LFGKGSIDTC AKFSCTSKAI GRTIQPENIK YEVGIFVHGT TTSENHGNYS
460 470 480 490 500
AQVGASQAAK FTVTPNAPSI TLKLGDYGEV TLDCEPRSGL NTEAFYVMTV
510 520 530 540 550
GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEGAH ATKQSVVALG
560 570 580 590 600
SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE
610 620 630 640 650
KFSFAKNPVD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT
660 670 680 690 700
VNPFVATSSA NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA
710 720 730 740 750
FSTTLKGAQR LAALGDTAWD FGSIGGVFNS IGRAVHQVFG GAFRTLFGGM
760 770 780 790 800
SWITQGLMGA LLLWMGVNAR DRSIALAFLA TGGVLVFLAT NVHADTGCAI
810 820 830 840 850
DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV HKAHKEGVCG
860 870 880 890 900
VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM
910 920 930 940 950
TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE
960 970 980 990 1000
DFGFGITSTR VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY
1010 1020 1030 1040 1050
NDTWKLERAV FGEVKSCTWP ETHTLWGDDV EESELIIPHT IAGPKSKHNR
1060 1070 1080 1090 1100
REGYKTQNQG PWDENGIVLD FDYCPGTKVT ITEDCSKRGP SVRTTTDSGK
1110 1120 1130 1140 1150
LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVMHDETTLV RSQVDAFKGE
1160 1170 1180 1190 1200
MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGVLLVL MLGGITYTDL
1210 1220 1230 1240 1250
ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN
1260 1270 1280 1290 1300
VILVLGAAFF QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV
1310 1320 1330 1340 1350
LALLTPGMRA LYLDTYRIIL LVIGICSLLH ERKKTMAKKK GAVLLGLALT
1360 1370 1380 1390 1400
STGWFSPTTI AAGLMVCNPN KKRGWPATEF LSAVGLMFAI VGGLAELDIE
1410 1420 1430 1440 1450
SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA ITGSSRRLDV
1460 1470 1480 1490 1500
KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK
1510 1520 1530 1540 1550
TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF
1560 1570 1580 1590 1600
HTLWHTTRGA AIMSGEGKLT PYWGSVREDR IAYGGPWRFD RKWNGTDDVQ
1610 1620 1630 1640 1650
VIVVEPGKAA VNIQTKPGVF RTPFGEVGAV SLDYPRGTSG SPILDSNGDI
1660 1670 1680 1690 1700
IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP EAYTPNMLRK RQMTVLDLHP
1710 1720 1730 1740 1750
GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL RGLPVRYQTS
1760 1770 1780 1790 1800
AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA
1810 1820 1830 1840 1850
ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS
1860 1870 1880 1890 1900
SGYEWITEYA GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP
1910 1920 1930 1940 1950
KCKNGDWDFV ITTDISEMGA NFGASRVIDC RKSVKPTILE EGEGRVILGN
1960 1970 1980 1990 2000
PSPITSASAA QRRGRVGRNP NQVGDEYHYG GATSEDDSNL AHWTEAKIML
2010 2020 2030 2040 2050
DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE LLRTADLPVW
2060 2070 2080 2090 2100
LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW
2110 2120 2130 2140 2150
LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM
2160 2170 2180 2190 2200
YLVATAEKGG KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI
2210 2220 2230 2240 2250
GKMGLGALVL TLATFFLWAA EVPGTKIAGT LLIALLLMVV LIPEPEKQRS
2260 2270 2280 2290 2300
QTDNQLAVFL ICVLTVVGVV AANEYGMLEK TKADLKSMFG GKTQASGLTG
2310 2320 2330 2340 2350
LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS LASINSQAGS
2360 2370 2380 2390 2400
LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG
2410 2420 2430 2440 2450
WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL
2460 2470 2480 2490 2500
IGVSVAAFLV NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH
2510 2520 2530 2540 2550
VMRGSYLAGG SIAWTLIKNA DKPSLKRGRP GGRTLGEQWK EKLNAMSREE
2560 2570 2580 2590 2600
FFKYRREAII EVDRTEARRA RRENNIVGGH PVSRGSAKLR WLVEKGFVSP
2610 2620 2630 2640 2650
IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP MLMQSYGWNL
2660 2670 2680 2690 2700
VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH
2710 2720 2730 2740 2750
RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS
2760 2770 2780 2790 2800
GAAGNVVHAV NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH
2810 2820 2830 2840 2850
SNQEKIKKRI QKLKEEFATT WHKDPEHPYR TWTYHGSYEV KATGSASSLV
2860 2870 2880 2890 2900
NGVVELMSKP WDAIANVTTM AMTDTTPFGQ QRVFKEKVDT KAPEPPAGAK
2910 2920 2930 2940 2950
EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA VFAEQNQWST
2960 2970 2980 2990 3000
AREAVDDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS
3010 3020 3030 3040 3050
RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD
3060 3070 3080 3090 3100
IAGKQGGKMY ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL
3110 3120 3130 3140 3150
TYRHKVVKVM RPAAEGKTVM DVISREDQRG SGQVVTYALN TFTNIAVQLV
3160 3170 3180 3190 3200
RLMEAEGVIG PQHLEQLPRK TKIAVRTWLF ENGEERVTRM AISGDDCVVK
3210 3220 3230 3240 3250
PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF CSNHFQEIVM
3260 3270 3280 3290 3300
KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH
3310 3320 3330 3340 3350
RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLQVWNRVWI
3360 3370 3380 3390 3400
EENEWMMDKT PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN
3410 3420 3430
QVRAVIGKEN YVDYMTSLRR YEDVLIQEDR VI
Length:3,432
Mass (Da):380,211
Last modified:August 1, 1992 - v1
Checksum:i11B9423735B1B5FE
GO
Isoform Structural polyprotein (identifier: P0DOH7-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DOH7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Product of a -1 ribosomal frameshifting.By similarity
Length:1,198
Mass (Da):131,562
GO

Sequence cautioni

The sequence AAA46249 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55506 Genomic RNA Translation: AAA46248.1
M55506 Genomic RNA Translation: AAA46249.1 Different initiation.
PIRiA35519 GNWVJS

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Entry informationi

Entry nameiPOLG_JAEV1
AccessioniPrimary (citable) accession number: P27395
Secondary accession number(s): Q82920
, Q82921, Q82922, Q82923, Q82924, Q82925, Q82926, Q82927, Q82928
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 23, 2018
This is version 151 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

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