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UniProtKB/Swiss-Prot entry Q89277


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name POLG_YEFVF
Primary accession number Q89277
Secondary accession numbers None
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on December 1, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Genome polyprotein
Synonyms None
Contains Protein C
     (Core protein)
     (Capsid protein)
prM
Peptide pr
Small envelope protein M
     (Matrix protein)
Envelope protein E
Non-structural protein 1
     (NS1)
Non-structural protein 2A
     (NS2A)
Non-structural protein 2A-alpha
     (NS2A-alpha)
Serine protease subunit NS2B
     (Non-structural protein 2B)
Serine protease subunit NS3
     (EC 3.4.21.91)
     (Non-structural protein 3)
Non-structural protein 4A
     (NS4A)
Peptide 2k
Non-structural protein 4B
     (NS4B)
RNA-directed RNA polymerase NS5
     (EC 2.7.7.48)
     (EC 2.1.1.56)
     (Non-structural protein 5)
Gene name None
From
Yellow fever virus (strain French neurotropic vaccine FNV) (YFV) [TaxID: 407135] 
Taxonomy Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; Flavivirus; Yellow fever virus group.
Virus hosts Aedes aegypti (Yellowfever mosquito) [TaxID: 7159]
Aedes luteocephalus [TaxID: 299629]
Aedes simpsoni [TaxID: 7161]
Homo sapiens (Human) [TaxID: 9606]
Simiiformes [TaxID: 314293]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7595382 [NCBI, ExPASy, EBI, Israel, Japan]
Wang E., Ryman K.D., Jennings A.D., Wood D.J., Taffs F., Minor P.D., Sanders P.G., Barrett A.D.;
"Comparison of the genomes of the wild-type French viscerotropic strain of yellow fever virus with its vaccine derivative French neurotropic vaccine.";
J. Gen. Virol. 76:2749-2755(1995).
Comments
  • FUNCTION: Protein C packages viral RNA to form a viral nucleocapsid, and promotes virion budding (By similarity).
  • FUNCTION: prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E heterodimers are dissociated (By similarity).
  • FUNCTION: Envelope protein E binds cell surface receptor and is involved in membrane fusion between virion and target cell. Synthesized as an homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).
  • FUNCTION: Non-structural protein 1 is slowly secreted from mammalian cells, but not from mosquito cells. The secreted form elicits protective immune response and plays an essential role in RNA replication (By similarity).
  • FUNCTION: Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity).
  • FUNCTION: Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).
  • FUNCTION: Non-structural protein 4A plays a role in RNA replication (By similarity).
  • FUNCTION: Non-structural protein 4B plays a role in RNA replication (By similarity).
  • FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and assure the capping of genomes in the cytoplasm. May be involved in methylation of 5'RNA cap structure (By similarity).
  • CATALYTIC ACTIVITY: 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.
  • CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
  • SUBUNIT: prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. Envelope protein E forms homodimers. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form an heterodimer. NS3 interacts with unphosphorylated NS5 (By similarity).
  • SUBCELLULAR LOCATION: Protein C: Virion (By similarity).
  • SUBCELLULAR LOCATION: Peptide pr: Secreted (By similarity).
  • SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane; Single-pass type I membrane protein (By similarity).
  • SUBCELLULAR LOCATION: Envelope protein E: Virion membrane; Single-pass type I membrane protein (By similarity).
  • SUBCELLULAR LOCATION: Non-structural protein 1: Secreted. Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side (By similarity).
  • SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Endoplasmic reticulum membrane (By similarity).
  • SUBCELLULAR LOCATION: Non-structural protein 2A: Endoplasmic reticulum membrane (By similarity).
  • SUBCELLULAR LOCATION: Serine protease subunit NS2B: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).
  • SUBCELLULAR LOCATION: Serine protease subunit NS3: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).
  • SUBCELLULAR LOCATION: Non-structural protein 4A: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).
  • SUBCELLULAR LOCATION: Non-structural protein 4B: Endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Note=The C-terminal transmembrane domain of non-structural protein 4B is presumably reoriented after cleavage on the lumenal side (By similarity).
  • SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus (By similarity).
  • DOMAIN: Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals (By similarity).
  • PTM: Specific enzymatic cleavages in vivo yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3 (By similarity).
  • PTM: RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization (By similarity).
  • PTM: Envelope protein E and non-structural protein 1 are N-glycosylated (By similarity).
  • MISCELLANEOUS: The virion is assembled in the endoplasmic reticulum lumen, transported by vesicles to the Golgi, then transported again to the cell membrane where it is released outside the cell.
  • SIMILARITY: Contains 1 helicase ATP-binding domain.
  • SIMILARITY: Contains 1 helicase C-terminal domain.
  • SIMILARITY: Contains 1 peptidase S7 domain [view classification].
  • SIMILARITY: Contains 1 RdRp catalytic domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U21055; AAA99712.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP Q9Q4T1; 1BEF. [HSSP ENTRY / PDB]
SMR Q89277; 1671-2107.
ModBase Q89277.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0030529; Cellular component: ribonucleoprotein complex (inferred from electronic annotation from UniProtKB-KW).
GO:0019028; Cellular component: viral capsid (inferred from electronic annotation from InterPro).
GO:0019031; Cellular component: viral envelope (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008026; Molecular function: ATP-dependent helicase activity (inferred from electronic annotation from InterPro).
GO:0003725; Molecular function: double-stranded RNA binding (inferred from electronic annotation from InterPro).
GO:0046872; Molecular function: metal ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004482; Molecular function: mRNA (guanine-N7-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0003724; Molecular function: RNA helicase activity (inferred from electronic annotation from InterPro).
GO:0003968; Molecular function: RNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
GO:0016070; Biological process: RNA metabolic process (inferred from electronic annotation from InterPro).
GO:0006410; Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0019079; Biological process: viral genome replication (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR014001; DEAD-like_N.
IPR011492; DEAD_Flavivir.
IPR001650; DNA/RNA_helicase_C.
IPR013755; Flav_glyE_cen_1.
IPR013756; Flav_glyE_cen_2.
IPR011999; Flav_glyE_cen_dm.
IPR001122; Flavi_capsidC.
IPR000069; Flavi_M.
IPR001157; Flavi_NS1.
IPR000752; Flavi_NS2A.
IPR000487; Flavi_NS2B.
IPR000404; Flavi_NS4A.
IPR001528; Flavi_NS4B.
IPR002535; Flavi_propep.
IPR000336; Flv_glyE_Ig-like.
IPR014412; Gen_Poly_FLV.
IPR014021; Helicase_SF1/SF2_ATP-bd.
IPR001850; Peptidase_S7.
IPR000208; RNA_pol_flaviviral.
IPR007094; RNA_pol_PSvir.
IPR002877; RrmJFtsJ_MeTrfase.
Graphical view of domain structure.
Gene3D G3DSA:3.30.387.10; Flav_glyE_cen_1; 1.
G3DSA:3.30.67.10; Flav_glyE_cen_2; 1.
G3DSA:2.60.40.350; Flv_glyE_Ig-like; 1.
Pfam PF01003; Flavi_capsid; 1.
PF07652; Flavi_DEAD; 1.
PF02832; Flavi_glycop_C; 1.
PF00869; Flavi_glycoprot; 1.
PF01004; Flavi_M; 1.
PF00948; Flavi_NS1; 1.
PF01005; Flavi_NS2A; 1.
PF01002; Flavi_NS2B; 1.
PF01350; Flavi_NS4A; 1.
PF01349; Flavi_NS4B; 1.
PF00972; Flavi_NS5; 1.
PF01570; Flavi_propep; 1.
PF01728; FtsJ; 1.
PF00271; Helicase_C; 1.
PF00949; Peptidase_S7; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF003817; Gen_Poly_FLV; 1.
ProDom PD001496; Flavi_NS1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00487; DEXDc; 1.
SM00490; HELICc; 1.
SMART graphical view of domain structure.
PROSITE PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; FALSE_NEG.
PS50507; RDRP_SSRNA_POS; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q89277.
ProtoNet Q89277.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Capsid protein; Cleavage on pair of basic residues; Complete proteome; Endoplasmic reticulum; Envelope protein; Glycoprotein; Helicase; Hydrolase; Membrane; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Protease; Ribonucleoprotein; RNA replication; RNA-binding; RNA-directed RNA polymerase; Secreted; Serine protease; Transferase; Transmembrane; Viral nucleoprotein; Virion.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed; by host. 
CHAIN   2    101  100     Protein C. PRO_0000261515
PROPEP   102    121  20     ER anchor for the protein C, removed in mature form by serine protease NS3. PRO_0000261516
CHAIN   122    285  164     prM. PRO_0000261517
CHAIN   122    210  89     Peptide pr. PRO_0000261518
CHAIN   211    285  75     Small envelope protein M. PRO_0000261519
CHAIN   286    778  493     Envelope protein E. PRO_0000261520
CHAIN   779   1130  352     Non-structural protein 1. PRO_0000261521
CHAIN   1131   1354  224     Non-structural protein 2A. PRO_0000261522
CHAIN   1131   1320  190     Non-structural protein 2A-alpha. PRO_0000261523
CHAIN   1355   1484  130     Serine protease subunit NS2B. PRO_0000261524
CHAIN   1485   2107  623     Serine protease subunit NS3. PRO_0000261525
CHAIN   2108   2233  126     Non-structural protein 4A. PRO_0000261526
PEPTIDE   2234   2256  23     Peptide 2k. PRO_0000261527
CHAIN   2257   2506  250     Non-structural protein 4B. PRO_0000261528
CHAIN   2507   3411  905     RNA-directed RNA polymerase NS5. PRO_0000261529
TOPO_DOM   2    101  100     Cytoplasmic (Potential). 
TRANSMEM   102    121  20     Potential. 
TOPO_DOM   122    244  123     Extracellular (Potential). 
TRANSMEM   245    265  21     Potential. 
TOPO_DOM   266    269  4     Cytoplasmic (Potential). 
TRANSMEM   270    287  18     Potential. 
TOPO_DOM   288    730  443     Extracellular (Potential). 
TRANSMEM   731    751  21     Potential. 
TOPO_DOM   752    757  6     Cytoplasmic (Potential). 
TRANSMEM   758    778  21     Potential. 
TOPO_DOM   779   1130  352     Extracellular (Potential). 
TRANSMEM   1131   1151  21     Potential. 
TOPO_DOM   1152   1160  9     Cytoplasmic (Potential). 
TRANSMEM   1161   1181  21     Potential. 
TOPO_DOM   1182   1201  20     Lumenal (Potential). 
TRANSMEM   1202   1222  21     Potential. 
TOPO_DOM   1223   1231  9     Cytoplasmic (Potential). 
TRANSMEM   1232   1252  21     Potential. 
TOPO_DOM   1253   1262  10     Lumenal (Potential). 
TRANSMEM   1263   1285  23     Potential. 
TOPO_DOM   1286   1287  2     Cytoplasmic (Potential). 
TRANSMEM   1288   1308  21     Potential. 
TOPO_DOM   1309   1321  13     Lumenal (Potential). 
TRANSMEM   1322   1342  21     Potential. 
TOPO_DOM   1343   2186  844     Cytoplasmic (Potential). 
TRANSMEM   2187   2207  21     Potential. 
TOPO_DOM   2208   2209  2     Lumenal (Potential). 
TRANSMEM   2210   2230  21     Potential. 
TOPO_DOM   2231   2233  3     Cytoplasmic (Potential). 
TRANSMEM   2234   2256  23     Potential. 
TOPO_DOM   2257   2359  103     Lumenal (Potential). 
TRANSMEM   2360   2380  21     Potential. 
TOPO_DOM   2381   2421  41     Cytoplasmic (Potential). 
TRANSMEM   2422   2442  21     Potential. 
TOPO_DOM   2443   2445  3     Lumenal (Potential). 
TRANSMEM   2446   2466  21     Potential. 
TOPO_DOM   2467   3411  945     Cytoplasmic (Potential). 
DOMAIN   1492   1666  175     Peptidase S7. 
DOMAIN   1669   1825  157     Helicase ATP-binding. 
DOMAIN   1820   1997  178     Helicase C-terminal. 
DOMAIN   3035   3187  153     RdRp catalytic. 
NP_BIND   1682   1689  8     ATP (Potential). 
REGION   383    396  14     Involved in fusion (By similarity). 
MOTIF   1773   1776  4     DEAH box (By similarity). 
MOTIF   2878   2911  34     Nuclear localization signal (By similarity). 
ACT_SITE   1537   1537        Charge relay system; for serine protease NS3 activity (By similarity). 
ACT_SITE   1561   1561        Charge relay system; for serine protease NS3 activity (By similarity). 
ACT_SITE   1622   1622        Charge relay system; for serine protease NS3 activity (By similarity). 
SITE   101    102  2     Cleavage; by serine protease NS3 (By similarity). 
SITE   121    122  2     Cleavage; by host signal peptidase (By similarity). 
SITE   210    211  2     Cleavage; by host furin (By similarity). 
SITE   285    286  2     Cleavage; by host signal peptidase (By similarity). 
SITE   778    779  2     Cleavage; by host signal peptidase (By similarity). 
SITE   1130   1131  2     Cleavage; by host (By similarity). 
SITE   1320   1321  2     Cleavage; by serine protease NS3 (By similarity). 
SITE   1354   1355  2     Cleavage; by serine protease NS3 (By similarity). 
SITE   1484   1485  2     Cleavage; by serine protease NS3 (By similarity). 
SITE   2107   2108  2     Cleavage; by serine protease NS3 (By similarity). 
SITE   2233   2234  2     Cleavage; by host signal peptidase (By similarity). 
SITE   2256   2257  2     Cleavage; by serine protease NS3 (By similarity). 
SITE   2506   2507  2     Cleavage; by serine protease NS3 (By similarity). 
CARBOHYD   134    134        N-linked (GlcNAc...) (Potential). 
CARBOHYD   150    150        N-linked (GlcNAc...) (Potential). 
CARBOHYD   908    908