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Q89277 (POLG_YEFVF) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 14 chains:

  1. Capsid protein C
    Alternative name(s):
    Core protein
  2. prM
  3. Peptide pr
  4. Small envelope protein M
    Alternative name(s):
    Matrix protein
  5. Envelope protein E
  6. Non-structural protein 1
    Short name=NS1
  7. Non-structural protein 2A
    Short name=NS2A
  8. Non-structural protein 2A-alpha
    Short name=NS2A-alpha
  9. Serine protease subunit NS2B
    Alternative name(s):
    Flavivirin protease NS2B regulatory subunit
    Non-structural protein 2B
  10. Serine protease NS3
    EC=3.4.21.91
    EC=3.6.1.15
    EC=3.6.4.13
    Alternative name(s):
    Flavivirin protease NS3 catalytic subunit
    Non-structural protein 3
  11. Non-structural protein 4A
    Short name=NS4A
  12. Peptide 2k
  13. Non-structural protein 4B
    Short name=NS4B
  14. RNA-directed RNA polymerase NS5
    EC=2.1.1.56
    EC=2.1.1.57
    EC=2.7.7.48
    Alternative name(s):
    Non-structural protein 5
OrganismYellow fever virus (strain French neurotropic vaccine FNV) (YFV) [Complete proteome]
Taxonomic identifier407135 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusYellow fever virus group
Virus hostAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes simpsoni [TaxID: 7161]
Homo sapiens (Human) [TaxID: 9606]
Aedes luteocephalus (Mosquito) [TaxID: 299629]
Simiiformes [TaxID: 314293]

Protein attributes

Sequence length3411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA By similarity.

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 homodimers are dissociated By similarity.

Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. 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.

Non-structural protein 1 is involved in virus replication and regulation of the innate immune response By similarity.

Non-structural protein 2A may be involved viral RNA replication and capsid assembly Potential.

Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity.

Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction By similarity.

Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functionning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase 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 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 By similarity.

RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) 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 genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway 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.

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

NTP + H2O = NDP + phosphate.

ATP + H2O = ADP + phosphate.

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

S-adenosyl-L-methionine + m7G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA.

Subunit structure

Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity By similarity.

Subcellular location

Capsid protein C: Virion Potential.

Peptide pr: Secreted By similarity.

Small envelope protein M: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Envelope protein E: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity.

Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Remains non-covalently associated to NS3 protease By similarity.

Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Located in RE-associated vesicles hosting the replication complex.

Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Host nucleus By similarity. Note: Located in RE-associated vesicles hosting the replication complex.

Domain

Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals By similarity.

Post-translational modification

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. Specific enzymatic cleavages in vivo yield mature proteins Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site By similarity.

RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.

Envelope protein E and non-structural protein 1 are N-glycosylated By similarity.

Sequence similarities

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 peptidase S7 domain.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processClathrin-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
Initiation of viral infection
RNA replication
Transcription
Transcription regulation
Viral attachment to host cell
Viral immunoevasion
Viral penetration into host cytoplasm
Virus endocytosis by host
   Cellular componentHost endoplasmic reticulum
Host membrane
Host nucleus
Membrane
Secreted
Viral envelope protein
Virion
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionCapsid protein
Helicase
Hydrolase
Methyltransferase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Serine protease
Transferase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processevasion by virus of host immune response

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular componenthost cell endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: InterPro

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

double-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

mRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: EC

mRNA (nucleoside-2'-O-)-methyltransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 34113411Genome polyprotein
PRO_0000405159
Chain1 – 101101Capsid protein C By similarity
PRO_0000261515
Propeptide102 – 12120ER anchor for the protein C, removed in mature form by serine protease NS3
PRO_0000261516
Chain122 – 285164prM By similarity
PRO_0000261517
Chain122 – 21089Peptide pr By similarity
PRO_0000261518
Chain211 – 28575Small envelope protein M By similarity
PRO_0000261519
Chain286 – 778493Envelope protein E By similarity
PRO_0000261520
Chain779 – 1130352Non-structural protein 1 By similarity
PRO_0000261521
Chain1131 – 1354224Non-structural protein 2A By similarity
PRO_0000261522
Chain1131 – 1320190Non-structural protein 2A-alpha By similarity
PRO_0000261523
Chain1355 – 1484130Serine protease subunit NS2B By similarity
PRO_0000261524
Chain1485 – 2107623Serine protease NS3 By similarity
PRO_0000261525
Chain2108 – 2233126Non-structural protein 4A By similarity
PRO_0000261526
Peptide2234 – 225623Peptide 2k
PRO_0000261527
Chain2257 – 2506250Non-structural protein 4B By similarity
PRO_0000261528
Chain2507 – 3411905RNA-directed RNA polymerase NS5 By similarity
PRO_0000261529

Regions

Topological domain1 – 104104Cytoplasmic Potential
Transmembrane105 – 12521Helical; Potential
Topological domain126 – 244119Extracellular Potential
Transmembrane245 – 26521Helical; Potential
Topological domain266 – 2705Cytoplasmic Potential
Transmembrane271 – 28515Helical; Potential
Topological domain286 – 730445Extracellular Potential
Intramembrane731 – 75121Helical; Potential
Topological domain752 – 7576Extracellular Potential
Intramembrane758 – 77821Helical; Potential
Topological domain779 – 1130352Extracellular Potential
Transmembrane1131 – 115121Helical; Potential
Topological domain1152 – 11609Cytoplasmic Potential
Transmembrane1161 – 118121Helical; Potential
Topological domain1182 – 120120Lumenal Potential
Transmembrane1202 – 122221Helical; Potential
Topological domain1223 – 12319Cytoplasmic Potential
Transmembrane1232 – 125221Helical; Potential
Topological domain1253 – 126210Lumenal Potential
Transmembrane1263 – 128523Helical; Potential
Topological domain1286 – 135570Cytoplasmic Potential
Transmembrane1356 – 137621Helical; Potential
Topological domain1377 – 13782Lumenal Potential
Transmembrane1379 – 139921Helical; Potential
Topological domain1400 – 145657Cytoplasmic Potential
Intramembrane1457 – 147721Helical; Potential
Topological domain1478 – 2157680Cytoplasmic Potential
Transmembrane2158 – 217821Helical; Potential
Topological domain2179 – 21868Lumenal Potential
Intramembrane2187 – 220721Helical; Potential
Topological domain2208 – 22092Lumenal Potential
Transmembrane2210 – 223021Helical; Potential
Topological domain2231 – 224111Cytoplasmic Potential
Transmembrane2242 – 226221Helical; Note=Signal for NS4B; Potential
Topological domain2263 – 229331Lumenal Potential
Intramembrane2294 – 231421Helical; Potential
Topological domain2315 – 233824Lumenal Potential
Intramembrane2339 – 235921Helical; Potential
Topological domain23601Lumenal Potential
Transmembrane2361 – 238020Helical; Potential
Topological domain2381 – 242141Cytoplasmic Potential
Transmembrane2422 – 244221Helical; Potential
Topological domain2443 – 24453Lumenal Potential
Transmembrane2446 – 246621Helical; Potential
Topological domain2467 – 3411945Cytoplasmic Potential
Domain1485 – 1665181Peptidase S7
Domain1669 – 1825157Helicase ATP-binding
Domain1820 – 1997178Helicase C-terminal
Domain3035 – 3187153RdRp catalytic
Nucleotide binding1682 – 16898ATP Potential
Region30 – 7445Hydrophobic; homodimerization of capsid protein C By similarity
Region383 – 39614Involved in fusion By similarity
Region1407 – 144640Interacts with and activates NS3 protease By similarity
Motif1773 – 17764DEAH box
Motif2878 – 291134Nuclear localization signal By similarity
Compositional bias2656 – 26605Poly-Ser

Sites

Active site15371Charge relay system; for serine protease NS3 activity By similarity
Active site15611Charge relay system; for serine protease NS3 activity By similarity
Active site16221Charge relay system; for serine protease NS3 activity By similarity
Active site25671For 2'-O-methyltransferase activity By similarity
Active site26521For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Active site26881For 2'-O-methyltransferase activity By similarity
Active site27241For 2'-O-methyltransferase activity By similarity
Site101 – 1022Cleavage; by viral protease NS3 Potential
Site121 – 1222Cleavage; by host signal peptidase By similarity
Site210 – 2112Cleavage; by host furin Potential
Site285 – 2862Cleavage; by host signal peptidase Potential
Site778 – 7792Cleavage; by host signal peptidase Potential
Site1130 – 11312Cleavage; by host Potential
Site1354 – 13552Cleavage; by viral protease NS3 Potential
Site1484 – 14852Cleavage; by autolysis Potential
Site2107 – 21082Cleavage; by autolysis Potential
Site2233 – 22342Cleavage; by viral protease NS3 Potential
Site2256 – 22572Cleavage; by host signal peptidase Potential
Site2506 – 25072Cleavage; by viral protease NS3 Potential

Amino acid modifications

Glycosylation1341N-linked (GlcNAc...); by host Potential
Glycosylation1501N-linked (GlcNAc...); by host Potential
Glycosylation9081N-linked (GlcNAc...); by host Potential
Glycosylation9861N-linked (GlcNAc...); by host Potential
Disulfide bond288 ↔ 315 By similarity
Disulfide bond345 ↔ 401 By similarity
Disulfide bond359 ↔ 390 By similarity
Disulfide bond377 ↔ 406 By similarity
Disulfide bond467 ↔ 568 By similarity
Disulfide bond585 ↔ 615 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89277 [UniParc].

Last modified December 1, 2001. Version 2.
Checksum: E7A5E79C999C9D8D

FASTA3,411379,189
        10         20         30         40         50         60 
MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK 

        70         80         90        100        110        120 
ITAHLKRLWK MLDPRQGLAA LRKVKRVVAG LMRGLSSRKR RSHDVLTVQF LILGMLLMTG 

       130        140        150        160        170        180 
GVTLVRKNRW LLLNVTSEDL GKTFSMGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD 

       190        200        210        220        230        240 
DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ 

       250        260        270        280        290        300 
KIERWFVRNP FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV 

       310        320        330        340        350        360 
HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPVE ARKVCYNAVL THVKINDKCP 

       370        380        390        400        410        420 
STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI 

       430        440        450        460        470        480 
QYVIRARLHV GAKQENWKTD IKTLKFDALS GSQEAEFTGY GKATLECQVQ TAVDFGNSYI 

       490        500        510        520        530        540 
AEMEKESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGDQEGSLK 

       550        560        570        580        590        600 
TALTGAMRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH 

       610        620        630        640        650        660 
GTVVMQVKVP KGAPCRIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY 

       670        680        690        700        710        720 
IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FFTSVGKGIH 

       730        740        750        760        770        780 
TVFGSAFQGL FGGLNWITKV IIGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ 

       790        800        810        820        830        840 
GCAINFAKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS 

       850        860        870        880        890        900 
LEHEMWRSRA DEINAILEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL 

       910        920        930        940        950        960 
VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV FEYTIDCDGS 

       970        980        990       1000       1010       1020 
ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK ECEWPLTHTI GTSVEESEMF 

      1030       1040       1050       1060       1070       1080 
MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVKREACPG TSVIIDGNCD GRGKSARSTT 

      1090       1100       1110       1120       1130       1140 
DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL 

      1150       1160       1170       1180       1190       1200 
VSMMIALEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD 

      1210       1220       1230       1240       1250       1260 
AMYMALIAAF SVRPGLLIGF GLRTLWSPRE RLVLALGAAM VEIALGGMMG GLWKYLNAVS 

      1270       1280       1290       1300       1310       1320 
LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLATMLF CTVVIIGVLY QNSKDTSMQK 

      1330       1340       1350       1360       1370       1380 
TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAAAGLVGV LAGLAFQEME 

      1390       1400       1410       1420       1430       1440 
NFLGPIAVGG ILMMLVSVAG RVDGLELKKL GEVAWEEEAE ISGSSARYDV ALSEQGEFKL 

      1450       1460       1470       1480       1490       1500 
LSEEKVPWDQ VVMTSLALVG AAIHPFALLL VLAGWLFHVR GARRSGDVLW DIPTPKVIEE 

      1510       1520       1530       1540       1550       1560 
CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK LIPSWASVKE 

      1570       1580       1590       1600       1610       1620 
DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS LFKVRNGGEI GAVALDYPSG 

      1630       1640       1650       1660       1670       1680 
TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS AISQTEVKEE GKEELQEIPT MLKKGKTTIL 

      1690       1700       1710       1720       1730       1740 
DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG 

      1750       1760       1770       1780       1790       1800 
SGREVIDAMC HATLTYRMLE PTRIVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT 

      1810       1820       1830       1840       1850       1860 
ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF LPSIRAANVM 

      1870       1880       1890       1900       1910       1920 
AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP 

      1930       1940       1950       1960       1970       1980 
VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS 

      1990       2000       2010       2020       2030       2040 
MLLDNMEVRG GMVAPLYGVE GTKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK 

      2050       2060       2070       2080       2090       2100 
AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RTPGGAKKPL RPRWCDERVS SDQSALSEFI 

      2110       2120       2130       2140       2150       2160 
KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVLLHS EEGSRAYRNA LSMMPEAMTI 

      2170       2180       2190       2200       2210       2220 
VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYIMLIFFV 

      2230       2240       2250       2260       2270       2280 
LMVVVIPEPG QQRSIQDNQV AFLIIGILTL VSVVAANELG MLEKTKEDLF GKKNSIPSSA 

      2290       2300       2310       2320       2330       2340 
SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI 

      2350       2360       2370       2380       2390       2400 
PFMKMNISVI MLLISGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA 

      2410       2420       2430       2440       2450       2460 
KNPVVDGNPT VDIEEAPEMP VLYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL 

      2470       2480       2490       2500       2510       2520 
GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVMYNLWK MKTGRRGTAN GKTLGEVWKR 

      2530       2540       2550       2560       2570       2580 
ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE 

      2590       2600       2610       2620       2630       2640 
GRVIDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR 

      2650       2660       2670       2680       2690       2700 
LEPVKCDTLL CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK 

      2710       2720       2730       2740       2750       2760 
LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE 

      2770       2780       2790       2800       2810       2820 
ADVTLPIGTR SVETDKGPLD KEAIEERVER IKSEYMTSWF YDNDNPYRTW HYCGSYVTKT 

      2830       2840       2850       2860       2870       2880 
SGSAASMVNG VIKILTYPWD KIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI 

      2890       2900       2910       2920       2930       2940 
MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE 

      2950       2960       2970       2980       2990       3000 
LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN 

      3010       3020       3030       3040       3050       3060 
EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT EADLDDEQEI 

      3070       3080       3090       3100       3110       3120 
LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI 

      3130       3140       3150       3160       3170       3180 
TNLKVQLIRM AEAEMVIHHQ HVQDCDESVL TRLEAWLTEH GCNRLRRMAV SGDDCVVRPI 

      3190       3200       3210       3220       3230       3240 
DDRFGLALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE 

      3250       3260       3270       3280       3290       3300 
QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ 

      3310       3320       3330       3340       3350       3360 
GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTMV KEWRDVPYLT KRQDKLCGSL 

      3370       3380       3390       3400       3410 
IGMTNRATWA SHIHLVIHRI RTLVGQEKYT DYLTVMDRYS VDADLQPGEL I 

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References

[1]"Comparison of the genomes of the wild-type French viscerotropic strain of yellow fever virus with its vaccine derivative French neurotropic vaccine."
Wang E., Ryman K.D., Jennings A.D., Wood D.J., Taffs F., Minor P.D., Sanders P.G., Barrett A.D.
J. Gen. Virol. 76:2749-2755(1995) [PubMed: 7595382] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U21055 Genomic RNA. Translation: AAA99712.1.

3D structure databases

HSSPHSSP built from PDB template 1YKS based on UniProtKB P19901.
ProteinModelPortalQ89277.
SMRQ89277. Positions 572-683, 1490-1667, 1671-2107, 2512-2772, 2780-3399.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR014001. DEAD-like_helicase.
IPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013756. Flav_glyE_cen_dom_subdom2.
IPR013754. Flav_glyE_dim.
IPR001122. Flavi_capsidC.
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.
IPR011999. GlycoprotE_cen/dimer_Flavivir.
IPR011998. GlycoprotE_cen/dimer_vir.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR001850. Peptidase_S7.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_RrmJ/FtsJ.
[Graphical view]
Gene3DG3DSA:3.30.67.10. Flav_glyE_cen_2. 1 hit.
G3DSA:2.60.98.10. Flav_glyE_dim. 3 hits.
G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.
PfamPF01003. 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.
PF00271. Helicase_C. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF56983. Flavi_glycoprotE. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. False negative.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_YEFVF
AccessionPrimary (citable) accession number: Q89277
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 1, 2001
Last modified: November 16, 2011
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families