ID W0FXJ7_9FLAV Unreviewed; 2695 AA.
AC W0FXJ7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS dengue virus type 3.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus denguei;
OC Dengue virus.
OX NCBI_TaxID=11069 {ECO:0000313|EMBL:AHF45690.1};
RN [1] {ECO:0000313|EMBL:AHF45690.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DENV-3/NI/BID-V4794/2009 {ECO:0000313|EMBL:AHF45690.1};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RG Genome Resources in Dengue Consortium;
RA Zody M.C., Henn M., Newman R.M., Harris E., Balmaseda A., Tangni G.,
RA Nunez A., Poon T.W., Charlebois P., Weiner B., Yang X., Larson L.,
RA Piper M.E., Fitzgerald M., Lui A., Young S., Gargeya S., Levin J.,
RA Malboeuf C., Qu J., Berlin A.M., Chapman S.B., Murphy C., Wortman J.,
RA Nusbaum C., Birren B.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the viral RNA replication complex that functions
CC in virion assembly and antagonizes the host immune response.
CC {ECO:0000256|ARBA:ARBA00024317}.
CC -!- FUNCTION: Functions as a signal peptide for NS4B and is required for
CC the interferon antagonism activity of the latter.
CC {ECO:0000256|ARBA:ARBA00003504}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC EC=3.4.21.91; Evidence={ECO:0000256|ARBA:ARBA00024468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001491};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004461}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004461}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004461}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; KF921917; AHF45690.1; -; Genomic_RNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0039564; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR CDD; cd17931; DEXHc_viral_Ns3; 1.
DR CDD; cd23204; Flavivirus_RdRp; 1.
DR CDD; cd18806; SF2_C_viral; 1.
DR Gene3D; 1.10.260.90; -; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.40.10.120; -; 2.
DR Gene3D; 3.30.70.2840; Flavivirus RNA-directed RNA polymerase, thumb domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR001850; Flavi_NS3_S7.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR046811; Flavi_NS5_thumb.
DR InterPro; IPR047530; Flavi_RdRp.
DR InterPro; IPR000208; Flavi_RdRp_fingers/palm.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR InterPro; IPR049486; NS3-hel_C_flaviviridae.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR04240; flavi_E_stem; 1.
DR Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF21659; Flavi_E_stem; 1.
DR Pfam; PF00948; Flavi_NS1; 1.
DR Pfam; PF01005; Flavi_NS2A; 1.
DR Pfam; PF01002; Flavi_NS2B; 1.
DR Pfam; PF01350; Flavi_NS4A; 1.
DR Pfam; PF01349; Flavi_NS4B; 1.
DR Pfam; PF00972; Flavi_NS5; 1.
DR Pfam; PF20483; Flavi_NS5_thumb; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022830};
KW Inhibition of host STAT2 by virus {ECO:0000256|ARBA:ARBA00022883};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00022883};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 27..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 742..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1452..1471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1478..1495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1501..1518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1530..1547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 649..778
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 779..956
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 959..1115
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1125..1291
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1797..2058
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 2322..2472
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHF45690.1"
SQ SEQUENCE 2695 AA; 301215 MW; BAC5E39E36FA10EB CRC64;
TAWDFGSVGG VLNSLGKMVH QIFGSAYTAL FSGVSWVMKI GIGVLLTWIG LNSKNTSMSF
SCIAIGIITL YLGAVVQADM GCVINWKGKE LKCGSGIFVT NEVHTWTEQY KFQADSPKRL
ATAIAGAWEN GVCGIRSTTR MENLLWKQIA NELNYILWEN NIKLTVVVGD IIGVLEQGKR
TLTPQPMELK YSWKTWGKAK IVTAETQNSS FIIDGPNTPE CPSVSRAWNV WEVEDYGFGV
FTTNIWLKLR EVYTQLCDHR LMSAAVKDER AVHADMGYWI ESQKNGSWKL EKASLIEVKT
CTWPKSHTLW SNGVLESDMI IPKSLAGPIS QHNHRPGYHT QTAGPWHLGK LELDFNYCEG
TTVVITENCG TRGPSLRTTT VSGKLIHEWC CRSCTLPPLR YMGEDGCWYG MEIRPISEKE
ENMVKSLVSA GSGKVDNFTM GVLCLAILFE EVMRGKFGKK HMIAGVFFTF VLLLSGQITW
RDMAHTLIMI GSNASDRMGM GVTYLALIAT FKIQPFLALG FFLRKLTSRE NLLLGVGLAM
ATTLQLPEDI EQMANGIALG LMALKLITQF EIYQLWTALI SLTCSNTIFT LTVAWRTATL
ILAGVSLLPM CQSSSMRKTD WLPMAVAAMG VPPLPLFIFS LKDTLKRRSW PLNEGVMAVG
LVSILASSLL RNDVPMAGPL VAGGLLIACY VITGTSADLT VEKAADITWE EEAEQTGVSH
NLMITVDDDG TMRIKDDETE NILTVLLKTA LLIVSGIFPY SIPATLLVWH TWQKQTQRSG
VLWDVPSPPE TQKAELEEGV YRIKQQGIFG KTQVGVGVQK EGVFHTMWHV TRGAVLTYNG
KRLEPNWASV KKDLISYGGG WRLSAQWQKG EEVQVIAVEP GKNPKNFQTM PGTFQTTTGE
IGAIALDFKP GTSGSPIINR EGKVVGLYGN GVVTKNGGYV SGIAQTNAEP DGPTPELEEE
MFKKRNLTIM DLHPGSGKTR KYLPAIVREA IKRRLRTLIL APTRVVAAEM EEALKGLPIR
YQTTATKSEH TGREIVDLMC HATFTMRLLS PVRVPNYNLI VMDEAHFTDP ASIAARGYIS
TRVGMGEAAA IFMTATPPGT ADAFPQSNAP IQDEERDIPE RSWNSGNEWI TDFAGKTVWF
VPSIKAGNDI ANCLRKNGKK VIQLSRKTFD TEYQKTKLND WDFVVTTDIS EMGANFKADR
VIDPRRCLKP VILTDGPERV ILAGPMPVTA ASAAQRRGRV GRNPQKENDQ YIFTGQPLNN
DEDHAHWTEA KMLLDNINTP EGIIPALFEP EREKSAAIDG EYRLKGESRK TFVELMRRGD
LPVWLAHKVA SEGIKYTDRK WCFDGQRNNQ ILEENMDVEI WTKEGEKKKL RPRWLDARTY
SDPLALKEFK EFAAGRKSIA LDLVTEIGRV PSHLAHRTRN ALDNLVMLHT SEHGGRAYRH
AVEELPETME TLLLLGLMIL LTGGAMLFLI SGKGIGKTSI GLICVIASSG MLWMAEIPLQ
WIASAIVLEF FMMVLLIPEP EKQRTPQDNQ LAYVVIGILT LAAIIAANEM GLLETTKRDL
GMSKEPGVVS PTSYLDVDLH PASAWTLYAV ATTVITPMLR HTIENSTANV SLAAIANQAV
VLMGLDKGWP ISKMDLGVPL LALGCYSQVN PLTLTAAVLL LITHYAIIGP GLQAKATREA
QKRTAAGIMK NPTVDGIMTI DLDPVIYDSK FEKQLGQVML LVLCAVQLLL MRTSWALCEA
LTLATGPITT LWEGSPGKFW NTTIAVSMAN IFRGSYLAGA GLAFSIMKSV GTGKRGTGSQ
GETLGEKWKK KLNQLSRKDF DLYKKSGITE VDRTEAKEGL KRGEITHHAV SRGSAKLQWF
VERNMVIPEG RVIDLGCGRG GWSYYCAGLK KVTEVRGYTK GGPGHEEPVP MSTYGWNIVK
LMSGKDVFYL PPEKCDTLLC DIGESSPSPT VEESRTIRVL KMVEPWLKNN QFCIKVLNPY
MPTVIEHLER LQRKHGGMLV RNPLSRNSTH EMYWISNGTG NIVASVNMVS RLLLNRFTMT
HRRPTIEKDV DLGAGTRHVN AEPETPNMDV IGERIKRIKE EHNSTWHYDD ENPYKTWAYH
GSYEVKATGS ASSMINGVVK LLTKPWDVVP MVTQMAMTDT TPFGQQRVFK EKVDTRTPRS
MPGTRRVMGI TAEWLWRTLG RNKKPRLCTR EEFTKKVRTN AAMGAVFTEE NQWDSAKAAV
EDEDFWKLVD RERELHKLGK CGSCVYNMMG KREKKLGEFG KAKGSRAIWY MWLGARYLEF
EALGFLNEDH WFSRENSYSG VEGEGLHKLG YILRDISKIP GGAMYADDTA GWDTRITEDD
LHNEEKITQQ MDPEHRQLAN AIFKLTYQNK VVKVQRPTPT GTVMDIISRK DQRGSGQVGT
YGLNTFTNME AQLIRQMEGE GVLSKADLEN PHLPEKKITQ WLETKGVERL KRMAISGDDC
VVKPIDDRFA NALLALNDMG KVRKDIPQWQ PSKGWHDWQQ VPFCSHHFHE LIMKDGRKLV
VPCRPQDELI GRARISQGAG WSLKETACLG KAYAQMWSLM YFHRRDLRLA SNAICSAVPV
HWVPTSRTTW SIHAHHQWMT TEDMLTVWNR VWIEDNPWME DKTPVTTWEN VPYLGKREDQ
WCGSLIGLTS RATWAQNIPT AIQQVRSLIG NEEFLDYMPS MKRFRKEEES EGAIW
//
