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P14336 (POLG_TBEVW) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 13 chains:

  1. Peptide 2k
  2. Capsid protein C
    Alternative name(s):
    Core protein
  3. prM
  4. Peptide pr
  5. Small envelope protein M
    Alternative name(s):
    Matrix protein
  6. Envelope protein E
  7. Non-structural protein 1
    Short name=NS1
  8. Non-structural protein 2A
    Short name=NS2A
  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. Non-structural protein 4B
    Short name=NS4B
  13. 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
OrganismTick-borne encephalitis virus European subtype (strain Neudoerfl) (NEUV) (Neudoerfl virus) [Complete proteome]
Taxonomic identifier11088 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › tick-borne encephalitis virus group
Virus hostIxodes ricinus (Common tick) [TaxID: 34613]
Ixodes persulcatus (Taiga tick) [TaxID: 34615]

Protein attributes

Sequence length3414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

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. Inhibits host SCRIB and prevents activation of downstream JAK-STAT 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. NS5 interacts with human SCRIB (via PDZ domain); this interaction inhibits STAT1 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway By similarity. Ref.4

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: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

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.

Post-translational modification

Specific enzymatic cleavages in vivo by the viral protease NS3 and host cell enzymes 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 soluble protein C is released after cleavage by NS3 protease at a site upstream of this hydrophobic domain. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. 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 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 term3D-structure
Complete 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 – 34143414Genome polyprotein
PRO_0000405175
Chain1 – 9696Capsid protein C By similarity
PRO_0000037815
Propeptide97 – 11721ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000405176
Chain118 – 280163prM By similarity
PRO_0000405177
Chain118 – 20588Peptide pr By similarity
PRO_0000037816
Chain206 – 28075Small envelope protein M By similarity
PRO_0000037817
Chain281 – 776496Envelope protein E By similarity
PRO_0000037818
Chain777 – 1128352Non-structural protein 1 By similarity
PRO_0000037819
Chain1129 – 1358230Non-structural protein 2A By similarity
PRO_0000037820
Chain1359 – 1489131Serine protease subunit NS2B By similarity
PRO_0000037821
Chain1490 – 2110621Serine protease NS3 By similarity
PRO_0000037822
Chain2111 – 2236126Non-structural protein 4A By similarity
PRO_0000037823
Peptide2237 – 225923Peptide 2k By similarity
PRO_0000405178
Chain2260 – 2511252Non-structural protein 4B By similarity
PRO_0000037824
Chain2512 – 3414903RNA-directed RNA polymerase NS5 By similarity
PRO_0000037825

Regions

Topological domain1 – 9898Cytoplasmic Potential
Transmembrane99 – 11921Helical; Potential
Topological domain120 – 242123Extracellular Potential
Transmembrane243 – 26018Helical; Potential
Topological domain2611Cytoplasmic Potential
Transmembrane262 – 28019Helical; Potential
Topological domain281 – 727447Extracellular Potential
Intramembrane728 – 74821Helical; Potential
Topological domain749 – 75911Extracellular Potential
Intramembrane760 – 78021Helical; Potential
Topological domain781 – 1132352Extracellular Potential
Transmembrane1133 – 115321Helical; Potential
Topological domain1154 – 11585Cytoplasmic Potential
Transmembrane1159 – 117921Helical; Potential
Topological domain1180 – 11878Lumenal Potential
Transmembrane1188 – 120821Helical; Potential
Topological domain1209 – 129385Cytoplasmic Potential
Transmembrane1294 – 131421Helical; Potential
Topological domain1315 – 132713Lumenal Potential
Transmembrane1328 – 134821Helical; Potential
Topological domain1349 – 135911Cytoplasmic Potential
Transmembrane1360 – 137819Helical; Potential
Topological domain1379 – 13824Lumenal Potential
Transmembrane1383 – 140321Helical; Potential
Topological domain1404 – 145451Cytoplasmic Potential
Intramembrane1455 – 147521Helical; Potential
Topological domain1476 – 2160685Cytoplasmic Potential
Transmembrane2161 – 218121Helical; Potential
Topological domain2182 – 21898Lumenal Potential
Intramembrane2190 – 221021Helical; Potential
Topological domain22111Lumenal Potential
Transmembrane2212 – 223221Helical; Potential
Topological domain2233 – 224412Cytoplasmic Potential
Transmembrane2245 – 226521Helical; Note=Signal for NS4B; Potential
Topological domain2266 – 229934Lumenal Potential
Intramembrane2300 – 232021Helical; Potential
Topological domain2321 – 234323Lumenal Potential
Intramembrane2344 – 236421Helical; Potential
Topological domain2365 – 23684Lumenal Potential
Transmembrane2369 – 238921Helical; Potential
Topological domain2390 – 243243Cytoplasmic Potential
Transmembrane2433 – 245321Helical; Potential
Topological domain2454 – 247724Lumenal Potential
Transmembrane2478 – 249821Helical; Potential
Topological domain2499 – 3414916Cytoplasmic Potential
Domain1490 – 1669180Peptidase S7
Domain1675 – 1831157Helicase ATP-binding
Domain1841 – 2000160Helicase C-terminal
Domain3040 – 3189150RdRp catalytic
Nucleotide binding1688 – 16958ATP Potential
Region24 – 6845Hydrophobic; homodimerization of capsid protein C By similarity
Region378 – 39114Involved in fusion
Region1410 – 144940Interacts with and activates NS3 protease By similarity
Motif1779 – 17824DEAH box
Compositional bias1970 – 19734Poly-Asp
Compositional bias2201 – 22044Poly-Leu

Sites

Active site15431Charge relay system; for serine protease NS3 activity By similarity
Active site15671Charge relay system; for serine protease NS3 activity By similarity
Active site16271Charge relay system; for serine protease NS3 activity By similarity
Active site25721For 2'-O-methyltransferase activity By similarity
Active site26571For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Active site26941For 2'-O-methyltransferase activity By similarity
Active site27301For 2'-O-methyltransferase activity By similarity
Site96 – 972Cleavage; by viral protease NS3 Potential
Site117 – 1182Cleavage; by host signal peptidase By similarity
Site205 – 2062Cleavage; by host furin By similarity
Site280 – 2812Cleavage; by host signal peptidase Potential
Site776 – 7772Cleavage; by host signal peptidase Potential
Site1128 – 11292Cleavage; by host Potential
Site1358 – 13592Cleavage; by viral protease NS3 Potential
Site1489 – 14902Cleavage; by autolysis Potential
Site2110 – 21112Cleavage; by autolysis Potential
Site2236 – 22372Cleavage; by viral protease NS3 Potential
Site2259 – 22602Cleavage; by host signal peptidase Potential
Site2511 – 25122Cleavage; by viral protease NS3 Potential

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...); by host Potential
Glycosylation4341N-linked (GlcNAc...); by host Potential
Glycosylation8611N-linked (GlcNAc...); by host Potential
Glycosylation9831N-linked (GlcNAc...); by host Potential
Glycosylation9991N-linked (GlcNAc...); by host Potential
Disulfide bond283 ↔ 310
Disulfide bond340 ↔ 396
Disulfide bond354 ↔ 385
Disulfide bond372 ↔ 401
Disulfide bond466 ↔ 570
Disulfide bond587 ↔ 618

Secondary structure

1 ......................................................................... 3414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14336 [UniParc].

Last modified May 30, 2000. Version 4.
Checksum: 35DBCE014B310B79

FASTA3,414378,322
        10         20         30         40         50         60 
MVKKAILKGK GGGPPRRVSK ETATKTRQPR VQMPNGLVLM RMMGILWHAV AGTARNPVLK 

        70         80         90        100        110        120 
AFWNSVPLKQ ATAALRKIKR TVSALMVGLQ KRGKRRSATD WMSWLLVITL LGMTLAATVR 

       130        140        150        160        170        180 
KERDGSTVIR AEGKDAATQV RVENGTCVIL ATDMGSWCDD SLSYECVTID QGEEPVDVDC 

       190        200        210        220        230        240 
FCRNVDGVYL EYGRCGKQEG SRTRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW 

       250        260        270        280        290        300 
VWKNKLLALA MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR 

       310        320        330        340        350        360 
VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAKTREYC LHAKLSDTKV AARCPTMGPA 

       370        380        390        400        410        420 
TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA CEAKKKATGH VYDANKIVYT 

       430        440        450        460        470        480 
VKVEPHTGDY VAANETHSGR KTASFTISSE KTILTMGEYG DVSLLCRVAS GVDLAQTVIL 

       490        500        510        520        530        540 
ELDKTVEHLP TAWQVHRDWF NDLALPWKHE GAQNWNNAER LVEFGAPHAV KMDVYNLGDQ 

       550        560        570        580        590        600 
TGVLLKALAG VPVAHIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRAPTD 

       610        620        630        640        650        660 
SGHDTVVMEV TFSGTKPCRI PVRAVAHGSP DVNVAMLITP NPTIENNGGG FIEMQLPPGD 

       670        680        690        700        710        720 
NIIYVGELSH QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA WDFGSAGGFL SSIGKAVHTV 

       730        740        750        760        770        780 
LGGAFNSIFG GVGFLPKLLL GVALAWLGLN MRNPTMSMSF LLAGGLVLAM TLGVGADVGC 

       790        800        810        820        830        840 
AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE 

       850        860        870        880        890        900 
MAMWRSSVTE LNLALAEGEA NLTVVVDKFD PTDYRGGVPG LLKKGKDIKV SWKSWGHSMI 

       910        920        930        940        950        960 
WSIPEAPRRF MVGTEGQSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE PTHECDTGVM 

       970        980        990       1000       1010       1020 
GAAVKNGMAI HTDQSLWMRS MKNDTGTYIV ELLVTDLRNC SWPASHTIDN ADVVDSELFL 

      1030       1040       1050       1060       1070       1080 
PASLAGPRSW YNRIPGYSEQ VKGPWKYTPI RVIREECPGT TVTINAKCDK RGASVRSTTE 

      1090       1100       1110       1120       1130       1140 
SGKVIPEWCC RACTMPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP 

      1150       1160       1170       1180       1190       1200 
GIVALFVVLE YIIRRRPSTG TTVVWGGIVV LALLVTGMVR IESLVRYVVA VGITFHLELG 

      1210       1220       1230       1240       1250       1260 
PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPG ASLEEFWKWG 

      1270       1280       1290       1300       1310       1320 
DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG LVCFLSVASA CSVWRLLKGH 

      1330       1340       1350       1360       1370       1380 
REQKGLTWVV PLAGLLGGEG SGIRLLAFWE LSAHRGRRSF SEPLTVVGVM LTLASGMMRH 

      1390       1400       1410       1420       1430       1440 
TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWYP ELVNEGGEVS LRVRQDAMGN 

      1450       1460       1470       1480       1490       1500 
FHLTELEKEE RMMAFWLIAG LAASAIHWSG ILGVMGLWTL TEMLRSSRRS DLVFSGQGGR 

      1510       1520       1530       1540       1550       1560 
ERGDRPFEVK DGVYRIFSPG LFWGQNQVGV GYGSKGVLHT MWHVTRGAAL SIDDAVAGPY 

      1570       1580       1590       1600       1610       1620 
WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH QCQPGELILD TGRKLGAIPI 

      1630       1640       1650       1660       1670       1680 
DLVKGTSGSP ILNAQGVVVG LYGNGLKTNE TYVSSIAQGE AEKSRPNLPQ AVVGTGWTSK 

      1690       1700       1710       1720       1730       1740 
GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP 

      1750       1760       1770       1780       1790       1800 
AVSDQQAGGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK 

      1810       1820       1830       1840       1850       1860 
ENKCALVLMT ATPPGKSEPF PESNGAITSE ERQIPDGEWR DGFDWITEYE GRTAWFVPSI 

      1870       1880       1890       1900       1910       1920 
AKGGAIARTL RQKGKSVICL NSKTFEKDYS RVRDEKPDFV VTTDISEMGA NLDVSRVIDG 

      1930       1940       1950       1960       1970       1980 
RTNIKPEEVD GKVELTGTRR VTTASAAQRR GRVGRQDGRT DEYIYSGQCD DDDSGLVQWK 

      1990       2000       2010       2020       2030       2040 
EAQILLDNIT TLRGPVATFY GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH 

      2050       2060       2070       2080       2090       2100 
VAANVSSVTD RSWTWEGPEA NAVDEASGDL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK 

      2110       2120       2130       2140       2150       2160 
EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEEPGSRAM RMAERDAPEA 

      2170       2180       2190       2200       2210       2220 
FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS LLLLWAGGVG YGNMAGVALI 

      2230       2240       2250       2260       2270       2280 
FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKA DLSTALWSER 

      2290       2300       2310       2320       2330       2340 
EEPRPWSEWT NVDIQPARSW GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ASGAQAMRDL 

      2350       2360       2370       2380       2390       2400 
GGGAPFFGVA GHVMTLGVVS LIGATPTSLM VGVGLAALHL AIVVSGLEAE LTQRAHKVFF 

      2410       2420       2430       2440       2450       2460 
SAMVRNPMVD GDVINPFGEG EAKPALYERK MSLVLATVLC LMSVVMNRTV ASITEASAVG 

      2470       2480       2490       2500       2510       2520 
LAAAGQLLRP EADTLWTMPV ACGMSGVVRG SLWGFLPLGH RLWLRASGGR RGGSEGDTLG 

      2530       2540       2550       2560       2570       2580 
DLWKRRLNNC TREEFFVYRR TGILETERDK ARELLRRGET NVGLAVSRGT AKLAWLEERG 

      2590       2600       2610       2620       2630       2640 
YATLKGEVVD LGCGRGGWSY YAASRPAVMS VRAYTIGGKG HEAPKMVTSL GWNLIKFRSG 

      2650       2660       2670       2680       2690       2700 
MDVFSMQPHR ADTVMCDIGE SSPDAAVEGE RTRKVILLME QWKNRNPTAA CVFKVLAPYR 

      2710       2720       2730       2740       2750       2760 
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAVTGN IVNSVNVQSR KLLARFGDQR 

      2770       2780       2790       2800       2810       2820 
GPTKVPELDL GVGTRCVVLA EDKVKEQDVQ ERIRALREQY SETWHMDEEH PYRTWQYWGS 

      2830       2840       2850       2860       2870       2880 
YRTAPTGSAA SLINGVVKLL SWPWNAREDV VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP 

      2890       2900       2910       2920       2930       2940 
GTRVIMRAVN DWILERLAQK SKPRMCSREE FIAKVKSNAA LGAWSDEQNR WASAREAVED 

      2950       2960       2970       2980       2990       3000 
PAFWRLVDEE RERHLMGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA 

      3010       3020       3030       3040       3050       3060 
LGFLNEDHWA SRESSGAGVE GISLNYLGWH LKKLSTLNGG LFYADDTAGW DTKVTNADLE 

      3070       3080       3090       3100       3110       3120 
DEEQILRYME GEHKQLATTI MQKAYHAKVV KVARPSRDGG CIMDVITRRD QRGSGQVVTY 

      3130       3140       3150       3160       3170       3180 
ALNTLTNIKV QLIRMMEGEG VIEAADAHNP RLLRVERWLK EHGEERLGRM LVSGDDCVVR 

      3190       3200       3210       3220       3230       3240 
PLDDRFGKAL YFLNDMAKTR KDIGEWEHSA GFSSWEEVPF CSHHFHELVM KDGRTLVVPC 

      3250       3260       3270       3280       3290       3300 
RDQDELVGRA RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPADWV 

      3310       3320       3330       3340       3350       3360 
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKE RVMEWRDVPY LPKAQDMLCS 

      3370       3380       3390       3400       3410 
SLVGRRERAE WAKNIWGAVE KVRKMIGPEK FKDYLSCMDR HDLHWELRLE SSII

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References

[1]"The flavivirus 3'-noncoding region: extensive size heterogeneity independent of evolutionary relationships among strains of tick-borne encephalitis virus."
Wallner G., Mandl C.W., Kunz C., Heinz F.X.
Virology 213:169-178(1995) [PubMed: 7483260] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION.
Strain: Neudoerfl.
[2]"Sequence of the structural proteins of tick-borne encephalitis virus (western subtype) and comparative analysis with other flaviviruses."
Mandl C.W., Heinz F.X., Kunz C.
Virology 166:197-205(1988) [PubMed: 3413985] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-779.
Strain: Neudoerfl.
[3]"Genome sequence of tick-borne encephalitis virus (Western subtype) and comparative analysis of nonstructural proteins with other flaviviruses."
Mandl C.W., Heinz F.X., Stoeckl E., Kunz C.
Virology 173:291-301(1989) [PubMed: 2554575] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 767-3414.
Strain: Neudoerfl.
[4]"Isolation of capsid protein dimers from the tick-borne encephalitis flavivirus and in vitro assembly of capsid-like particles."
Kiermayr S., Kofler R.M., Mandl C.W., Messner P., Heinz F.X.
J. Virol. 78:8078-8084(2004) [PubMed: 15254179] [Abstract]
Cited for: SUBUNIT.
[5]"Characterization of a structural intermediate of flavivirus membrane fusion."
Stiasny K., Kossl C., Lepault J., Rey F.A., Heinz F.X.
PLoS Pathog. 3:E20-E20(2007) [PubMed: 17305426] [Abstract]
Cited for: TOPOLOGY OF ENVELOPE PROTEIN E.
[6]"The envelope glycoprotein from tick-borne encephalitis virus at 2-A resolution."
Rey F.A., Heinz F.X., Mandl C.W., Kunz C., Harrison S.C.
Nature 375:291-298(1995) [PubMed: 7753193] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 281-680.
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U27495 Genomic RNA. Translation: AAA86870.1.
PIRGNWVNE. A31052.
RefSeqNP_043135.1. NC_001672.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N6Gelectron microscopy16.00A/B/C281-675[»]
1NA4electron microscopy-A/B/C281-675[»]
1SVBX-ray1.90A281-675[»]
1URZX-ray2.70A/B/C/D/E/F281-681[»]
ProteinModelPortalP14336.
SMRP14336. Positions 281-675, 2512-2775, 2789-3402.
ModBaseSearch...

Protein family/group databases

MEROPSS07.001.
TCDB1.G.3.1.1. viral pore-forming membrane fusion protein-3 (VMFP3) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1489719.

Family and domain databases

InterProIPR014001. DEAD-like_helicase.
IPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
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:2.60.98.10. Flav_glyE_dim. 2 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.
PROSITEPS00690. DEAH_ATP_HELICASE. False negative.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_TBEVW
AccessionPrimary (citable) accession number: P14336
Secondary accession number(s): Q88493
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 30, 2000
Last modified: November 16, 2011
This is version 126 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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