Q01299 (POLG_TBEVH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 13 chains: Peptide 2k Capsid protein C Alternative name(s): Core protein prM Peptide pr Small envelope protein M Alternative name(s): Matrix protein Envelope protein E Non-structural protein 1 Short name=NS1 Non-structural protein 2A Short name=NS2A Serine protease subunit NS2B Alternative name(s): Flavivirin protease NS2B regulatory subunit Non-structural protein 2B 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 Non-structural protein 4A Short name=NS4A Non-structural protein 4B Short name=NS4B 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
Organism	Tick-borne encephalitis virus (strain Hypr) (TBEV) [Complete proteome]
Taxonomic identifier	70733 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › tick-borne encephalitis virus group
Virus host	Ixodes ricinus (Common tick) [TaxID: 34613] Ixodes persulcatus (Taiga tick) [TaxID: 34615]

Protein attributes

Sequence length	3414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.3 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. Ref.3 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. Ref.3 Non-structural protein 1 is involved in virus replication and regulation of the innate immune response By similarity. Ref.3 Non-structural protein 2A may be involved viral RNA replication and capsid assembly Potential. Ref.3 Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity. Ref.3 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. Ref.3 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. Ref.3 Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter By similarity. Ref.3 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. Ref.3
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. NS5 interacts with host SCRIB (via fourth PDZ domain); this interaction inhibits downstream STAT1 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway. Ref.3
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.
Miscellaneous	The non-structural protein NS1 presents 2. alternative cleavage sites for its C-terminus (either at position 1128 or at 1190), which may define a soluble or a membrane-bound form of NS1.
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 process	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 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 component	Host endoplasmic reticulum Host membrane Host nucleus Membrane Secreted Viral envelope protein Virion
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding
Molecular function	Capsid protein Helicase Hydrolase Methyltransferase Nucleotidyltransferase Protease RNA-directed RNA polymerase Serine protease Transferase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	evasion 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 component	host 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 function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3414	3414	Genome polyprotein		PRO_0000405167
	Chain	1 – 96	96	Capsid protein C By similarity		PRO_0000037793
	Propeptide	97 – 117	21	ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity		PRO_0000405168
	Chain	118 – 280	163	prM By similarity		PRO_0000405169
	Chain	118 – 205	88	Peptide pr By similarity		PRO_0000037794
	Chain	206 – 280	75	Small envelope protein M By similarity		PRO_0000037795
	Chain	281 – 776	496	Envelope protein E By similarity		PRO_0000037796
	Chain	777 – 1128	352	Non-structural protein 1 By similarity		PRO_0000037797
	Chain	1129 – 1358	230	Non-structural protein 2A By similarity		PRO_0000037798
	Chain	1359 – 1489	131	Serine protease subunit NS2B By similarity		PRO_0000037799
	Chain	1490 – 2110	621	Serine protease NS3 By similarity		PRO_0000037800
	Chain	2111 – 2236	126	Non-structural protein 4A By similarity		PRO_0000037801
	Peptide	2237 – 2259	23	Peptide 2k By similarity		PRO_0000405170
	Chain	2260 – 2511	252	Non-structural protein 4B By similarity		PRO_0000037802
	Chain	2512 – 3414	903	RNA-directed RNA polymerase NS5 By similarity		PRO_0000037803
Regions
	Topological domain	1 – 98	98	Cytoplasmic Potential
	Transmembrane	99 – 119	21	Helical; Potential
	Topological domain	120 – 242	123	Extracellular Potential
	Transmembrane	243 – 260	18	Helical; Potential
	Topological domain	261	1	Cytoplasmic Potential
	Transmembrane	262 – 280	19	Helical; Potential
	Topological domain	281 – 727	447	Extracellular Potential
	Intramembrane	728 – 748	21	Helical; Potential
	Topological domain	749 – 759	11	Extracellular Potential
	Intramembrane	760 – 780	21	Helical; Potential
	Topological domain	781 – 1132	352	Extracellular Potential
	Transmembrane	1133 – 1153	21	Helical; Potential
	Topological domain	1154 – 1158	5	Cytoplasmic Potential
	Transmembrane	1159 – 1179	21	Helical; Potential
	Topological domain	1180 – 1187	8	Lumenal Potential
	Transmembrane	1188 – 1208	21	Helical; Potential
	Topological domain	1209 – 1293	85	Cytoplasmic Potential
	Transmembrane	1294 – 1314	21	Helical; Potential
	Topological domain	1315 – 1327	13	Lumenal Potential
	Transmembrane	1328 – 1348	21	Helical; Potential
	Topological domain	1349 – 1359	11	Cytoplasmic Potential
	Transmembrane	1360 – 1377	18	Helical; Potential
	Topological domain	1378 – 1382	5	Lumenal Potential
	Transmembrane	1383 – 1403	21	Helical; Potential
	Topological domain	1404 – 1454	51	Cytoplasmic Potential
	Intramembrane	1455 – 1475	21	Helical; Potential
	Topological domain	1476 – 2160	685	Cytoplasmic Potential
	Transmembrane	2161 – 2181	21	Helical; Potential
	Topological domain	2182 – 2189	8	Lumenal Potential
	Intramembrane	2190 – 2210	21	Helical; Potential
	Topological domain	2211	1	Lumenal Potential
	Transmembrane	2212 – 2232	21	Helical; Potential
	Topological domain	2233 – 2244	12	Cytoplasmic Potential
	Transmembrane	2245 – 2265	21	Helical; Note=Signal for NS4B; Potential
	Topological domain	2266 – 2299	34	Lumenal Potential
	Intramembrane	2300 – 2320	21	Helical; Potential
	Topological domain	2321 – 2343	23	Lumenal Potential
	Intramembrane	2344 – 2364	21	Helical; Potential
	Topological domain	2365 – 2368	4	Lumenal Potential
	Transmembrane	2369 – 2389	21	Helical; Potential
	Topological domain	2390 – 2432	43	Cytoplasmic Potential
	Transmembrane	2433 – 2453	21	Helical; Potential
	Topological domain	2454 – 2477	24	Lumenal Potential
	Transmembrane	2478 – 2498	21	Helical; Potential
	Topological domain	2499 – 3414	916	Cytoplasmic Potential
	Domain	1490 – 1669	180	Peptidase S7
	Domain	1675 – 1831	157	Helicase ATP-binding
	Domain	1841 – 2000	160	Helicase C-terminal
	Domain	3040 – 3189	150	RdRp catalytic
	Nucleotide binding	1688 – 1695	8	ATP Potential
	Region	24 – 68	45	Hydrophobic; homodimerization of capsid protein C By similarity
	Region	1410 – 1449	40	Interacts with and activates NS3 protease By similarity
	Motif	1779 – 1782	4	DEAH box
	Compositional bias	1970 – 1973	4	Poly-Asp
	Compositional bias	2201 – 2204	4	Poly-Leu
Sites
	Active site	1543	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1567	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1627	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	2572	1	For 2'-O-methyltransferase activity By similarity
	Active site	2657	1	For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
	Active site	2694	1	For 2'-O-methyltransferase activity By similarity
	Active site	2730	1	For 2'-O-methyltransferase activity By similarity
	Site	96 – 97	2	Cleavage; by viral protease NS3 Potential
	Site	117 – 118	2	Cleavage; by host signal peptidase By similarity
	Site	205 – 206	2	Cleavage; by host furin By similarity
	Site	280 – 281	2	Cleavage; by host signal peptidase Potential
	Site	776 – 777	2	Cleavage; by host signal peptidase Potential
	Site	1128 – 1129	2	Cleavage; by host Potential
	Site	1358 – 1359	2	Cleavage; by viral protease NS3 Potential
	Site	1489 – 1490	2	Cleavage; by autolysis Potential
	Site	2110 – 2111	2	Cleavage; by autolysis Potential
	Site	2236 – 2237	2	Cleavage; by viral protease NS3 Potential
	Site	2259 – 2260	2	Cleavage; by host signal peptidase Potential
	Site	2511 – 2512	2	Cleavage; by viral protease NS3 Potential
Amino acid modifications
	Glycosylation	144	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	434	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	861	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	983	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	999	1	N-linked (GlcNAc...); by host Potential
	Disulfide bond	283 ↔ 310		By similarity
	Disulfide bond	340 ↔ 396		By similarity
	Disulfide bond	354 ↔ 385		By similarity
	Disulfide bond	372 ↔ 401		By similarity
	Disulfide bond	466 ↔ 570		By similarity
	Disulfide bond	587 ↔ 618		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01299 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EC0B1A5325A08C19	FASTA	3,414	378,545
	10 20 30 40 50 60 MVKKAILKGK GGGPPRRVSK ETATKTRQPR VQMPNGLVLM RMMGILWHAV AGTARNPVLK 70 80 90 100 110 120 AFWNSVPLKQ ATAALRKIKR TVSALMVGLQ KRGKRRSATD WMSWLLVITL LGMTIAATVR 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 VWKNRLLALA MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR 310 320 330 340 350 360 VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAQTREYC LHAKLSDTKV AARCPTMGPA 370 380 390 400 410 420 TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA CEAKKKATGH VYDANKIVYT 430 440 450 460 470 480 VKVEPHTGDY VAANETHSGR KTASFTVSSE KTILTMGEYG DVSLLCRVAS GVDLAQTVIL 490 500 510 520 530 540 ELDKTVEHLP TAWQVHRDWF NDLALPWKHE GARNWNNAER 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 NIIYVGELSY QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA WDFGSAGGFL SSIGKALHTV 730 740 750 760 770 780 LGGAFNSIFG GVGFLPKLLL GVALAWLGLN MRNPTMSMSF LLAGVLVLAM TLGVGADVGC 790 800 810 820 830 840 AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE 850 860 870 880 890 900 MAMWRSSVTE LNLALAEGEA NLTVMVDKFD 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 VKGPWKHTPI RVIREECPGT TVTINAKCDK RGASVRSTTE 1090 1100 1110 1120 1130 1140 SGKVIPEWCC RACTMPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP 1150 1160 1170 1180 1190 1200 GIVALFVVLE YIIRRRPSTG STVVWGGIVV LALLVTGMVR MESLVRYVVA VGITFHLELG 1210 1220 1230 1240 1250 1260 PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPS ANLEDFWKWG 1270 1280 1290 1300 1310 1320 DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG LVCFLSAASA CSIWRLLRGH 1330 1340 1350 1360 1370 1380 REQKGLTWIV PLARLLGGEG SGIRLLAFWE LSAHRGRRSF SEPLTVVGVM LTLASGMMRH 1390 1400 1410 1420 1430 1440 TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWHP ELVNEGGEVS LRVRQDAMGN 1450 1460 1470 1480 1490 1500 FHLTELEKEE RMMAFWLIAG LAASAIHWSG IIGVMGLWTL TKMLRSSRRS DLVFSGQGGR 1510 1520 1530 1540 1550 1560 ERGDRPFEVK DGVYRIFSPG LFWGQNQVGV GYGSKGVLHT MWHVTRGAAL SIDDAVAGPY 1570 1580 1590 1600 1610 1620 WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGKAHEVH 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 ERQIPNGEWR 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 NAVDEASGGL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK 2110 2120 2130 2140 2150 2160 EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEKPDSRAM RMAERDAPEA 2170 2180 2190 2200 2210 2220 FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS LLLLWAGGVG YGNMAGVALI 2230 2240 2250 2260 2270 2280 FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKA DLSTVLWSER 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 EAKPALYERR MSLVLAIVLC LMSVVMNRTV ASITEASAVG 2470 2480 2490 2500 2510 2520 LAAAGQLLRP EADTLWTMPV ACGMSGVVRG SLWGFLPLGH RLWLRASGGR RGGSEGDTLG 2530 2540 2550 2560 2570 2580 DLWKRRLNNC TREEFFVYRR TGILETERDK ARELLRRGET NMGLAVSRGT AKLAWLEERG 2590 2600 2610 2620 2630 2640 YATLKGEVVD LGCGRGGWSY YAASRPAVMS VRAYTIGGRG 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 GPTRVPELDL GVGTRCVVLA EDKVKEQDVQ ERIKALREQY 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 PAFWHLVDEE 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 GLSSWEEVPF CSHHFHELVM KDGRTLVVPC 3250 3260 3270 3280 3290 3300 RDQDELVGRA RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPVDWV 3310 3320 3330 3340 3350 3360 PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKG KVMEWRDVPY LPKAQDMLCS 3370 3380 3390 3400 3410 SLVGRKERAE WAKNIWGAVE KVRKMIGPEK FKDYLSCMDR HDLHWELRLE SSII

References

[1]	Wallner G., Mandl C.W., Ecker M., Holzmann H., Stiasny K., Kunz C., Heinz F.X. Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Presence of poly(A) in a flavivirus: significant differences between the 3' noncoding regions of the genomic RNAs of tick-borne encephalitis virus strains." Mandl C.W., Kunz C., Heinz F.X. J. Virol. 65:4070-4077(1991) [PubMed: 1712858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 3357-3414.
[3]	"Tick-borne encephalitis virus NS5 associates with membrane protein scribble and impairs interferon-stimulated JAK-STAT signalling." Werme K., Wigerius M., Johansson M. Cell. Microbiol. 10:696-712(2008) [PubMed: 18042258] [Abstract] Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5, INTERACTION OF NS5 WITH HUMAN SCRIB.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U39292 Genomic RNA. Translation: AAB53095.1. M76660 Genomic RNA. Translation: AAA47904.1.
3D structure databases
ProteinModelPortal	Q01299.
SMR	Q01299. Positions 281-675, 2512-2775, 2789-3402.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR014001. 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]
Gene3D	G3DSA:2.60.98.10. Flav_glyE_dim. 2 hits. G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.
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. PF00271. Helicase_C. 1 hit. PF00949. Peptidase_S7. 1 hit. [Graphical view]
PIRSF	PIRSF003817. Gen_Poly_FLV. 1 hit.
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
SUPFAM	SSF56983. Flavi_glycoprotE. 1 hit. SSF81296. Ig_E-set. 1 hit. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS00690. 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]
ProtoNet	Search...

Entry information

Entry name

POLG_TBEVH

Accession

Primary (citable) accession number: Q01299

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 16, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program