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Genome polyprotein

 A0A217EIG2_9FLAV        Unreviewed;      3390 AA.
A0A217EIG2;
27-SEP-2017, integrated into UniProtKB/TrEMBL.
27-SEP-2017, sequence version 1.
22-NOV-2017, entry version 3.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Name=Capsid {ECO:0000313|EMBL:SNQ41863.1};
Synonyms=Envelope {ECO:0000313|EMBL:SNQ41863.1},
Non-structural 1 {ECO:0000313|EMBL:SNQ41863.1},
Non-structural 2a {ECO:0000313|EMBL:SNQ41863.1},
Non-structural 2b {ECO:0000313|EMBL:SNQ41863.1},
Non-structural 3 {ECO:0000313|EMBL:SNQ41863.1},
Non-structural 4a {ECO:0000313|EMBL:SNQ41863.1},
Non-structural 4b {ECO:0000313|EMBL:SNQ41863.1},
Non-structural 5 {ECO:0000313|EMBL:SNQ41863.1},
Premembrane {ECO:0000313|EMBL:SNQ41863.1};
Dengue virus 3.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
NCBI_TaxID=11069 {ECO:0000313|EMBL:SNQ41863.1};
[1] {ECO:0000313|EMBL:SNQ41863.1}
NUCLEOTIDE SEQUENCE.
STRAIN=2424900 {ECO:0000313|EMBL:SNQ41863.1};
Kim H.J., Triplett B.A.;
Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000256|SAAS:SAAS00892720}.
-!- 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}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000256|SAAS:SAAS00232292}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{ECO:0000256|SAAS:SAAS00445805}.
-!- 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. {ECO:0000256|SAAS:SAAS00232385}.
-!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
{ECO:0000256|SAAS:SAAS00944756}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS00944756}; Lumenal side
{ECO:0000256|SAAS:SAAS00944756}.
-!- SUBCELLULAR LOCATION: Host nucleus
{ECO:0000256|SAAS:SAAS00892522}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|SAAS:SAAS00944768}.
-!- SUBCELLULAR LOCATION: Virion membrane
{ECO:0000256|SAAS:SAAS00944678}; Multi-pass membrane protein
{ECO:0000256|SAAS:SAAS00944678}.
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EMBL; LT898451; SNQ41863.1; -; Genomic_RNA.
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:0019031; C:viral envelope; IEA:InterPro.
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:0070008; F:serine-type exopeptidase 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; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
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; 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; 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; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 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; SSF101257; SSF101257; 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:SAAS00057850};
Disulfide bond {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 endoplasmic reticulum {ECO:0000256|SAAS:SAAS00944771};
Host membrane {ECO:0000256|SAAS:SAAS00445977};
Host nucleus {ECO:0000256|SAAS:SAAS00892445};
Host-virus interaction {ECO:0000256|SAAS:SAAS00445756,
ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00892696};
Hydrolase {ECO:0000256|SAAS:SAAS00058020,
ECO:0000256|SAAS:SAAS00462397};
Inhibition of host innate immune response by virus
{ECO:0000256|SAAS:SAAS00892696};
Inhibition of host interferon signaling pathway by virus
{ECO:0000256|SAAS:SAAS00892696};
Inhibition of host STAT2 by virus {ECO:0000256|SAAS:SAAS00892696};
Membrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAAS:SAAS00445977, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|SAAS:SAAS00940329};
Methyltransferase {ECO:0000256|SAAS:SAAS00817755};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00058020};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
Protease {ECO:0000256|SAAS:SAAS00462397};
RNA-binding {ECO:0000256|SAAS:SAAS00076745};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Secreted {ECO:0000256|SAAS:SAAS00944674};
Serine protease {ECO:0000256|SAAS:SAAS00462397};
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:SAAS00892696};
Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489633};
Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|SAAS:SAAS00057850, ECO:0000256|SAAS:SAAS00445995};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00445995,
ECO:0000256|SAAS:SAAS00489633}.
TRANSMEM 46 69 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 247 272 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 722 746 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 752 771 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1157 1175 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1195 1218 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1283 1304 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1316 1334 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1437 1464 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2147 2166 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2173 2190 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2196 2213 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2225 2242 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1344 1473 FLAVIVIRUS_NS2B.
{ECO:0000259|PROSITE:PS51527}.
DOMAIN 1474 1651 Peptidase S7.
{ECO:0000259|PROSITE:PS51528}.
DOMAIN 1654 1810 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1820 1986 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2492 2753 MRNA cap 0-1 NS5-type MT.
{ECO:0000259|PROSITE:PS51591}.
DOMAIN 3017 3167 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
ACT_SITE 1524 1524 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1548 1548 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1608 1608 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
SEQUENCE 3390 AA; 378028 MW; B122485A2B42FAF2 CRC64;
MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSRGLLNG QGPMKLVMAF IAFLRFLAIP
PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK TSLCLMMILP AALAFHLTSR
DGEPRMIVGK NERGKSLLFK TASGINMCTL IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC
WCNLTSTWVT YGTCNQAGEH RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW
ALRHPGFTIL ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW
VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT DSRCPTQGEA
VLPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ CLEPIEGKVV QYENLKYTVI
ITVHTGDQHQ VGNETQGVTA EITPQASTTE AILPEYGTLG LECSPRTGLD FNEMILLTMK
NKAWMVHRQW FFDLPLPWAS GATTETPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT
ALTGATEIQN SGGTSIFAGH LKCRLKMDKL ELKGMSYAMC TNTFVLKKEV SETQHGTILI
KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP FGESNIVIGI
GDNALKINWY KKGSSIGKMF EATARGARRM AILGDTAWDF GSVGGVLNSL GKMVHQIFGS
AYTALFSGVS WVMKIGIGVL LTWIGLNSKN TSMSFSCIAI GIITLYLGAV VQADMGCVIN
WKGKELKCGS GIFVTNEVHT WTEQYKFQAD SPKRLATAIA GAWENGVCGI RSTTRMENLL
WKQIANELNY ILWENNIKLT VVVGDTIGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE
TQNSSFIIDG PNTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ LCDHRLMSAA
VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWSNGVL ESDMIIPKSL
AGPISQHNYR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI TESCGTRGPS LRTTTVSGKL
IHEWCCRSCT LPPLRYMGED GCWYGMEIRP ISEKEENMVK SLVSAGSGKV DNFTMGVLCL
AILYEEVMRG KFGKKHMIAG VFFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL
ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN GIALGLMALK
LITQFETYQL WTALVSLTCS NTMFTLTVAW RTATLILAGV SLLPVCQSSS MRKTDWLPMA
VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL
LIACYVITGT SADLTVEKAA DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV
LLKTALLIVS GIFPYSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ
QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI SYGGGWRLSA
QWQKGEEVQV IAVEPGKNPK NFQTMPGTFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV
GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA
IVREAIKRRL RTLILAPTRV VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT
MRLLSPVRVP NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP
QSNAPIQDEE RDIPERSWNS GNEWITDFAG KTVWFVPSIK AGNDIANCLR KNGKKVIQLS
RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FKADRVIDPR RCLKPVILTD GPERVILAGP
MPVTAASAAQ RRGRVGRNPQ KENDQYIFTG QPLNNDEDHA HWTEAKMLLD NINTPEGILP
ALFEPEREKS AAIDGEYRLK GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG
QRNNQILEEN MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT
EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL GLMILLTGGA
MLFLISGKGI GKTSIGLICV IASSGMLWMA EVPLQWIASA IVLEFFMMVL LIPEPEKQRT
PQDNQLAYVV IGILTLAAII AANEMGLLET TKRDLGMSKE PGVVPPTSYL DVDLHPASAW
TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC
YSQVNPLTLT AAVLLLITHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV
IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEALTLAT GPITTLWEGS PGKFWNTTIA
VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK
SGITEVDRTE AKEGLKRGET THHAVSRGSA KLQWFVERNM VVPEGRVIDL GCGRGGWSYY
CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES
SPSPIVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS
RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET
PNMDVIGERI KRIKEEHNST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP
WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRPMPGTR KVMEITAEWL WRTLGRNKRP
RLCTREEFTK KVRTNAAMGA VFTEENQWDS AKAAVEDEEF WKLVDREREL HKLGKCGSCV
YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG
LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KIIQQMDPEH RQLANAIFKL
TYQNKVVKVQ RPTPTGTVMD IISRKDQRGS GQVGTYGLNT FTNMEAQLVR QMEGEGVLTK
ADLENPHLPE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD
IPQWQPSRGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE
TACLGKAYAQ MWSLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML
TVWNRVWIEE NPWMEDKTPV TTWENVPYLG KREDQWCGSL IGLTSRATWA QNIPTAIQQV
RSLIGNEEFL DYMPSMKRFR KEEESEGAIW


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