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Genome polyprotein

 A0EKV0_9FLAV            Unreviewed;      3414 AA.
A0EKV0;
28-NOV-2006, integrated into UniProtKB/TrEMBL.
28-NOV-2006, sequence version 1.
12-SEP-2018, entry version 98.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Greek goat encephalitis virus.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=41406 {ECO:0000313|EMBL:ABB90677.1, ECO:0000313|Proteomes:UP000163447};
[1] {ECO:0000313|EMBL:ABB90677.1, ECO:0000313|Proteomes:UP000163447}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=17169393; DOI=10.1016/j.virol.2006.09.015;
Grard G., Moureau G., Charrel R.N., Lemasson J.J., Gonzalez J.P.,
Gallian P., Gritsun T.S., Holmes E.C., Gould E.A., de Lamballerie X.;
"Genetic characterization of tick-borne flaviviruses: new insights
into evolution, pathogenetic determinants and taxonomy.";
Virology 361:80-92(2007).
-!- 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; DQ235153; ABB90677.1; -; Genomic_RNA.
ProteinModelPortal; A0EKV0; -.
Proteomes; UP000163447; 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:UP000163447};
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 34 54 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 101 119 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 246 279 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 727 749 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 756 776 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1133 1153 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1160 1179 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1204 1225 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1237 1257 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1296 1317 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1383 1401 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 2346 2363 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2369 2387 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2433 2451 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1357 1487 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; 378081 MW; B2BF496B1C2F2273 CRC64;
MAGKAILKGK GSGPPRRALK ETARKTRQLR VQMPNGLVLM RMMGILWHAI AGTARGPVLK
SFWNAVPLRQ AITALRKIKR AVSALMVGLQ RRGKRRSATD WISWLLVITL LGVVLAATVR
KEKDGTTVIR AEGRDAATQV RVDNGTCVLL ATDMGSWCDD SLSYECVTID QGEEPVDVDC
FCRNVEGVYL EYGRCGRQEG ARTRRSVLIP SHAQGELTGR GSKWLEGDSL RTHLTRVEGW
VWKNKLLALA MVVVVWLTLE SVVARVAVLV ALLCLAPVYA SRCTHLENRD FVTGTQGTTR
VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAKTREYC LHAKLSETKV AARCPMMGPA
VLAEERQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA CGAKKKATGY VYDANKIVYT
VKVEPHTGDY VAANETHSGR KTATFTVSSE KTILTMGEYG DVSLLCRVAS GVDLAQTVIL
ELDKTAEHLP TAWQVHRDWF NDLALPWKHE GALGWNNAER LVEFGAPHAV KMDVYNLGDQ
TGVLLKALAG VPVAHIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTTCDKT KFTWKRVPTD
SGHDTVVMEV TFSGSKPCRI PVRAVAHGSP DVNVAMLITP NPTIENSGGG FIEMQLPPGD
NIIYVGELSH QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA WDFGSAGGFL TSIGKAMHTV
LGGAFNAIFG GVGFLPKLLL GVALAWLGLN MRNPTMSVSF LLAGGLILAM TLGVGADVGC
AVDSERMELR CGEGLVVWRE VSEWYDNYAY YPETPGALAS AIKEAFEEGN CGIVPQNRLE
MAMWRSSVTE LNLALAEGDA NLTVVVDKLD PTDYRGGVPG VLKKGKDMRV SWKGWGQSMI
WSVPEAPRRF MVGTEGGNEC PLERRKTGVL TVAEFGVGLR TKVFLDFRQE PTHECDTGVM
GAAVKNGMAI HTDQSLWMRS VKNDTGTYIV ELLVTDLRNC SWPASHTIDN AGVMDSELFL
PASLAGPRSW YNRIPGYSEQ VKGPWRHTPI RVVREECPGT SVTINAKCDK RGASVRSTTE
SGKVIPEWCC RTCTMPPVTY RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP
GIVALFVILE YVIRRRPSTG TTIVWGGVVI FALLVTGMVK IESLVRYVVA VGITFHLELG
PETVALMLLQ AVFELRVGLL GAFALRRSLT VREMVTTYFL LLVLELGLPG ASFEGLWKWG
DALAMGAMIF RACTMEGKTG TGLLLMALMT QRDVAIVHHG LVCFLGVASA CSVWRLARGH
REQKGLPWIV SLARLIGREG SGIRLLAFWE LATRGGRRSF SEPLTVVGVM LTLAGGMMRH
TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWHP ELVNEGGEVS LRVRQDSMGN
FHLTELEKEE RMMAFWLLAG LAASALHWSG ILGVMGLWTL TEMLRSPRKS DLVFSGQGSR
ERGDRPFEVK DGVYRIFSPG LLWGQRQVGV GYGSRGVLHT MWHVTRGAAL SIDDAVAGPY
WADVREDVVC YGGAWSLEEK WKGEAVQIHA FPPGRAHEVH QCQPGELILD TGKRLGAVPI
DLAKGTSGSP ILNAHGVVVG LYGNGLKTNE TYVSSIAQGE VEKSRPNLPQ AVVGTGWMSK
GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP
AVSDQQVGGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
ENKCALVLMT ATPPGKSEPF PESNGAITSE ERQIPEGEWR DGFDWITEYD GRTAWFVPSI
AKGGVIARAL RQKGKSVICL NSKTFEKDYS RVKDEKPDFV VTTDISEMGA NLDVSRVIDG
RTNIKPEEVD GKVELTGVRR VTTASAAQRR GRVGRQGGRT DEYIYSGQCD DDDSGLVQWK
EAQILLDNIT TLRGPVATFY GPEQQKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH
VAANVSSVTD RSWTWEGPEA NAVDEANGEL VTFRSPNGAE RTLRPVWRDA RMFREGRDIK
EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEEPGSRAM KMAERDAPEA
FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLTS LLLLWAGGVG YGNMAGVALI
FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKT DLSTVLWSER
EEPRPWEEWT NIDIQPARSW GTYVLVVSLF TPYIVHQLQT RIQQLVNSAV AAGAQAMRDL
GGGTPFFGVA GHVITLGVVS LVGATPTSLV VGVGLAAFHL AIVVSGLEAE LTQRAHKIFF
SAMVRNPMVD GDVINPFGGG EAKPALYERK MSLVLAMALC LMSVVMNRTV IAVTEALAVG
LAAAGQLFRP EVDTLWTMPV ACGLSGVVRG SLWGFLPLGH RLWLQASGSR RGGSEGDTLG
DLWKRKLNSC TREEFFVYRR TGILETERDK ARELLRRGET NMGLAVSRGT AKLAWLEERG
YATLKGEVVD LGCGRGGWSY YAASRPAVMS VKAYTIGGKG HETPKMVTSL GWNLIKFRAG
MDVFGMQPHR ADTIMCDIGE SSPDAAVEGE RTRRVILLME QWKNRNPTAS CVFKVLAPYR
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAITGN IVNSVNIQSR KLLARFGDQR
GPTKVPELDL GVGTRCVVLA EDRVEEKDVQ ERIRALREQY NETWHVDKEH PYRTWQYWGS
YRTAPTGSAA SLINGVVKLL SWPWNGREDV VRMAMTDTTA FGQQRVFKEK VDTKAQEPQP
GTKVIMRAVN DWILERLAQK SKPRMCSKEE FIAKVKSNAA LGAWSDEQNR WASAKEAVED
PAFWQLVDEE RKRHLMGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
LGFLNEDHWA SRESSGAGVE GIGLNYLGWH LKKLSALNGG LFYADDTAGW DTKVTNADLE
DEEQILRYME GEHRQLAATV MQKAYHAKVV KVARPSRDGG CIMDVITRRD QRGSGQVVTY
ALNTLTNIKV QLIRMMEGEG VIEAADAHNP RLLRVERWLK EHGEERLGRM LVSGDDCVVR
PVDDRFGRAL YFLNDMAKTR KDIGEWEHST GFSSWEEVPF CSHHFHELVM KDGRTLVVPC
RDQDELVGRA RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA ISSAVPVDWV
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMENKE KVTEWRDVPY LPKAQDMLCS
SLVGRRERAE WAKNIWGAVE KVRKMIGPER FKDYLSCMDR HDLHWEPRLE SSII


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