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Genome polyprotein

 A1BPG4_9FLAV            Unreviewed;      3414 AA.
A1BPG4;
23-JAN-2007, integrated into UniProtKB/TrEMBL.
15-JUN-2010, sequence version 2.
12-SEP-2018, entry version 75.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Tick-borne encephalitis virus.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=11084 {ECO:0000313|EMBL:ABD62793.2, ECO:0000313|Proteomes:UP000123251};
[1] {ECO:0000313|EMBL:ABD62793.2, ECO:0000313|Proteomes:UP000123251}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Toro-2003 {ECO:0000313|EMBL:ABD62793.2};
PubMed=17277902; DOI=10.1007/s00705-006-0922-9;
Melik W., Nilsson A.S., Johansson M.;
"Detection strategies of tick-borne encephalitis virus in Swedish
Ixodes ricinus reveal evolutionary characteristics of emerging tick-
borne flaviviruses.";
Arch. Virol. 152:1027-1034(2007).
[2] {ECO:0000313|EMBL:ABD62793.2, ECO:0000313|Proteomes:UP000123251}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Toro-2003 {ECO:0000313|EMBL:ABD62793.2};
PubMed=20363326; DOI=10.1016/j.mcn.2010.03.012;
Wigerius M., Melik W., Elvang A., Johansson M.;
"Rac1 and Scribble are targets for the arrest of neurite outgrowth by
TBE virus NS5.";
Mol. Cell. Neurosci. 44:260-271(2010).
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000256|SAAS:SAAS00368577}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000256|SAAS:SAAS00368620}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}.
-!- SUBCELLULAR LOCATION: Host cytoplasm
{ECO:0000256|SAAS:SAAS00937464}. Host endoplasmic reticulum
{ECO:0000256|SAAS:SAAS00941764}. Virion membrane
{ECO:0000256|SAAS:SAAS00980400}; Multi-pass membrane protein
{ECO:0000256|SAAS:SAAS00980400}.
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EMBL; DQ401140; ABD62793.2; -; Genomic_RNA.
ProteinModelPortal; A1BPG4; -.
Proteomes; UP000123251; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
Gene3D; 3.30.387.10; -; 2.
Gene3D; 3.30.67.10; -; 4.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
4: Predicted;
Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00445756};
ATP-binding {ECO:0000256|SAAS:SAAS00058020};
Capsid protein {ECO:0000256|SAAS:SAAS00969288};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000123251};
Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3,
ECO:0000256|SAAS:SAAS00139753};
Fusion of virus membrane with host endosomal membrane
{ECO:0000256|SAAS:SAAS00489633};
Fusion of virus membrane with host membrane
{ECO:0000256|SAAS:SAAS00489633};
Helicase {ECO:0000256|SAAS:SAAS00058020};
Host cytoplasm {ECO:0000256|SAAS:SAAS00936979};
Host membrane {ECO:0000256|SAAS:SAAS00445977};
Host-virus interaction {ECO:0000256|SAAS:SAAS00445756,
ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00941647};
Hydrolase {ECO:0000256|SAAS:SAAS00058020};
Inhibition of host innate immune response by virus
{ECO:0000256|SAAS:SAAS00941647};
Membrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAAS:SAAS00445977, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4,
ECO:0000256|SAAS:SAAS00940329};
Methyltransferase {ECO:0000256|SAAS:SAAS00817755};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00058020};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
RNA-binding {ECO:0000256|SAAS:SAAS00076745};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Transferase {ECO:0000256|SAAS:SAAS00510600,
ECO:0000256|SAAS:SAAS00817755};
Transmembrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995};
Viral immunoevasion {ECO:0000256|SAAS:SAAS00941647};
Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489633};
Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00969288};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00445995,
ECO:0000256|SAAS:SAAS00489633};
Zinc {ECO:0000256|PIRSR:PIRSR003817-4}.
TRANSMEM 101 119 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 728 749 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 756 776 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1133 1152 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1164 1183 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1203 1223 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1235 1253 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1296 1317 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1455 1480 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2160 2183 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2195 2223 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2243 2259 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2344 2363 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2369 2387 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2433 2451 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1357 1488 FLAVIVIRUS_NS2B.
{ECO:0000259|PROSITE:PS51527}.
DOMAIN 1490 1669 Peptidase S7.
{ECO:0000259|PROSITE:PS51528}.
DOMAIN 1675 1831 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1841 2000 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2512 2776 MRNA cap 0-1 NS5-type MT.
{ECO:0000259|PROSITE:PS51591}.
DOMAIN 3040 3189 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
COILED 2779 2799 {ECO:0000256|SAM:Coils}.
ACT_SITE 1543 1543 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1567 1567 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1627 1627 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
METAL 2950 2950 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2954 2954 Zinc 1; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 2959 2959 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2962 2962 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3224 3224 Zinc 2; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 3240 3240 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3359 3359 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
DISULFID 283 310 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 340 396 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 354 385 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 372 401 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 466 570 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 587 618 {ECO:0000256|PIRSR:PIRSR003817-3}.
SEQUENCE 3414 AA; 378511 MW; D77EC6333055D85F CRC64;
MVKKAILKGK GGGPPRRVSK ETATKTRQPR VQMPNGLVLM RMMGILWHAV AGTARNPVLK
AFWNSVPLKQ ATAALRKIKR TVSALMVGLQ KRGKRRSATD WMSWLLVIAL LGMTLAATVR
KERDGSTVIR AEGKDAATQV RVENGTCVIL ATDMGSWCDD SLSYECVTID QGEEPVDVDC
FCRNVDGVYL EYGRCGKQEG SRTRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW
VWKNKLLALA MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAKTREYC LHAKLSDTKV AARCPTMGPA
TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA CEAKKKATGH VYDANKIVYT
VKVEPHTGDY VAANETHSGR KTASFTVSSE KTILTMGEYG DVSLLCRVAS GVDLAQTVIL
ELDKTVEHLP TAWQVHRDWF NDLALPWKHE GAQNWNNAER LVEFGAPHAV KMDVYNLGDQ
TGVLLKALAG VPVAHIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRAPTD
SGHDTVVMEV TFSGTKPCRI PVRAVAHGSP DVNVAMLITP NPTIENNGGG FIEMQLPPGD
NIIYVGELSH QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA WDFGSAGGFL SSIGKAVHTV
LGGAFNSIFG GVGFLPKLLL GVALAWLGLN MRNPTMSMSF LLAGGLVLAM TLGVGADVGC
AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE
MAMWRSSVTE LNLALAEGEA NLTVVVDKFD PTDYRGGVPG LLKKGKDIRV SWKSWGHSMI
WSIPEAPRRF MVGTEGQSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE PTHECDTGVM
GAAVKNGMAI HTDQSLWMRS MKNDTGTYIV ELLVTDLRNC SWPASHTIDN ADVVDSELFL
PASLAGPRSW YNRIPGYSEQ VKGPWKHTPI RVIREECPGT TVVINAKCDK RGASVRSTTE
SGKVIPEWCC RACTMPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP
GIVALFVVLE YIIRRRPSTG TTVVWGGIVV LALLVTGMVR IESLVRYVVA VGITFHLELG
PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPS VSLEDFWKWG
DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG LVCFLSVASA CSVWRLLRGH
REQKGLTWIV PLARLLGGEG SGIRLLAFWE LSAHRGRRSF SEPLTVVGVM LTLASGMMRH
TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWHP ELVNEGGEVS LRVRQDAMGN
FHLTELEKEE RMMAFWLLAG LAASAIHWSG ILGVMGLWTL TEMLRSSRRS DLVFSGQGGR
ERGDRPFEVK DGVYRIFSPG LFWGQSQVGV GYGSKGVLHT MWHVTRGAAL SIDDAVAGPY
WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGKAHEVH QCQPGELILD TGRKLGAIPI
DLVKGTSGSP ILNAQGVVVG LYGNGLKTNE TYVSSIAQGE AEKSRPNLPQ AVVGTGWTSK
GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP
AVSDQQAGGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
ENKCALVLMT ATPPGKSEPF PESNGAITSE ERQIPDGEWR DGFDWITEYE GRTAWFVPSI
AKGGAIARTL RQKGKSVICL NSKTFEKDYS RVRDEKPDFV VTTDISEMGA NLDVSRVIDG
RTNIKPEEVD GKVELTGTRR VTTASAAQRR GRVGRQDGRT DEYIYSGQCD DDDSGLVQWK
EAQILLDNIT TLRGPVATFY GPEQDKMPEV AGHYRLTEEK RKHFRHLLTH CDFTPWLAWH
VAANVSSVTD RSWTWEGPEA NAVDEASGDL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK
EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEEPGSRAM RMAERDAPEA
FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS LLLLWAGGVG YGNMAGVALI
FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKA DLSTVLWAEQ
EEPRPWSEWT NVDIQPARSW GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ASGAQAMRDL
GGGAPFFGVA GHVMTLGVVS LIGATPTSLM VGVGLAAFHL AIVVSGLEAE LTQRAHKVFF
SAMVRNPMVD GDVINPFGEG EAKPALYERK MSLVLAIVLC LMSVVMNRTM ASITEASAVG
LAAAGQLLKP EADTLWTMPV ACGMSGVVRG SLWGFLPLGH RLWLRASGGR RGGSEGDTLG
DLWKRRLNNC TREEFFVYRR TGIMETERDK ARELLRRGET NMGLAVSRGT AKLAWLEERG
YATLKGEVVD LGCGRGGWSY YAASRPAVMS VRAYTIGGRG HEAPKMVTSL GWNLIKFRSG
MDVFSMQPHR ADTIMCDIGE SSPDAAVEGE RTRKVILLME QWKNRNPTAA CVFKVLAPYR
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAVTGN IVNSVNVQSR KLLARFGDQR
GPTRVPELDL GVGTRCVVLA EDKVKEQDVR ERIRALREQY SETWHMDAEH PYRTWQYWGS
YRTAPTGSAA SLINGVVKLL SWPWNAREDV VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP
GTRVIMRAVN DWILERLAQK SRPRMCSKEE FIAKVRSNAA LGAWSDEQNR WAGAREAVED
PAFWQLVDEE RERHLMGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
LGFLNEDHWA SRESSGAGVE GISLNYLGWH LKKLSTLNGG LFYADDTAGW DTKVTNADLE
DEEQILRYME GEHKQLATTI MQKAYHAKVV KVARPSRDGG CIMDVITRRD QRGSGQVVTY
ALNTLTNIKV QLIRMMEGEG VIEAADAHNP RLLRVERWLK EHGEERLGRM LVSGDDCVVR
PLDDRFGKAL YFLNDMAKTR KDIGEWEHSA GFSSWEEVPF CSHHFHELVM KDGRTLVVPC
RDQDELVGRA RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPVDWV
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKE KVMEWRDVPY LPKAQDMLCS
SLVGRKERAE WAKNIWGAVE KVRKMMGPEK FRDYLSCMDR HDLHWELRLE SSII


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