ID W0LHK6_9FLAV Unreviewed; 2318 AA.
AC W0LHK6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:AHG23263.1};
RN [1] {ECO:0000313|EMBL:AHG23263.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DENV-3/BR/BID-V3608/2007 {ECO:0000313|EMBL:AHG23263.1};
RG Genome Resources in Dengue Consortium;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Zody M.C., Henn M., Newman R.M., Bosch I., Schmidt D., Comach G.,
RA Rothman 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KF955498; AHG23263.1; -; 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: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; 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; 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 Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF07652; Flavi_DEAD; 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 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1075..1094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1101..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1124..1141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1153..1170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 272..401
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 402..579
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 582..738
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 748..914
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1420..1681
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 1945..2095
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHG23263.1"
SQ SEQUENCE 2318 AA; 259360 MW; 31C3165931470C5E CRC64;
TTTVSGKLIH EWCCRSCTLP PLRYMGEDGC WYGMEIRPIS EKEENMVKSL VSAGSGKVDN
FTMGVLCLAI LFEEVMRGKF GKKHMIAGVF FTFVLLLSGQ ITWRDMTHTL IMIGSNASDR
MGMGVTYLAL IATFKIQPFL ALGFFLRKLT SRENLLLGVG LAMATTLQLP EDIEQMANGI
ALGLMALKLI TQFETYQLWT ALISLTCSNT MFTLTVAWRT ATLILAGVSL LPVCQSSSMR
KTDWLPMAVA AMGVPPLPLF IFSLKDTLKR RSWPLNEGVM AVGLVSILAS SLLRNDVPMA
GPLVAGGLLI ACYVITGTSA DLTVEKAADI TWEEEAEQTG VSHNLMITVD DDGTMRIKDD
ETENILTVLL KTALLIVSGV FPYSIPATLL VWHTWQKQTQ RSGVLWDVPS PPETQKAELE
EGVYRIKQQG IFGKTQVGVG VQKEGVFHTM WHVTRGAVLT YNGKRLEPNW ASVKKDLISY
GGGWRLSAQW QKGEEVQVIA VEPGKNPKNF QTTPGTFQTT TGEIGAIALD FKPGTSGSPI
INREGKVVGL YGNGVVTKNG GYVSGIAQTN AEPDGPTPEL EEEMFKKRNL TIMDLHPGSG
KTRKYLPAII REAIKRRLRT LILAPTRVVA AEMEEALKGL PIRYQTTATK SEHTGREIVD
LMCHATFTMR LLSPVRVPNY NLIIMDEAHF TDPASIAARG YISTRVGMGE AAAIFMTATP
PGTADAFPQS NAPIQDEERD IPERSWNSGN EWITDFAGKT VWFVPSIKAG NDIANCLRKN
GKKVIQLSRK TFDTEYQKTK LNDWDFVVTT DISEMGANFK ADRVIDPRRC LKPVILTDGP
ERVILAGPMP VTAASAAQRR GRVGRNPQKE NDQYIFTGQP LNNDEDHAHW TEAKMLLDNI
NTPEGIIPAL FEPEREKSAA IDGEYRLKGE SRKTFVELMR RGDLPVWLAH KVASEGIKYT
DRKWCFDGQR NNQILEENMD VEIWTKEGEK KKLRPRWLDA RTYSDPLALK EFKDFAAGRK
SIALDLVTEI GRVPSHLAHR TRNALDNLVM LHTSEHGGRA YRHAVEELPE TMETLLLLGL
MILLTGGAML FLISGKGIGK TSIGLICVIA SSGMLWMAEI PLQWIASAIV LEFFMMVLLI
PEPEKQRTPQ DNQLAYVVIG ILTLAAIIAA NEMGLLETTK RDLGMSKEPG VVSPTSYLDV
DLHPASAWTL YAVATTVITP MLRHTIENST ANVSLAAIAN QAVVLMGLDK GWPISKMDLG
VPLLALGCYS QVNPLTLTAA VLLLITHYAI IGPGLQAKAT REAQKRTAAG IMKNPTVDGI
MTIDLDPVIY DSKFEKQLGQ VMLLVLCAVQ LLLMRTSWAL CEALTLATGP ITTLWEGSPG
KFWNTTIAVS MANIFRGSYL AGAGLAFSIM KSVGTGKRGT GSQGETLGEK WKKKLNQLSR
KEFDLYKKSG ITEVDRTEAK EGLKRGEITH HAVSRGSAKL QWFVERNMVI PEGRVIDLGC
GRGGWSYYCA GLKKVTEVRG YTKGGPGHEE PVPMSTYGWN IVKLMSGKDV FYLPPEKCDT
LLCDIGESSP SPTVEESRTI RVLKMVEPWL KNNQFCIKVL NPYMPTVIEH LERLQRKHGG
MLVRNPLSRN STHEMYWISN GTGNIVASVN MVSRLLLNRF TMTHRRPTIE KDVDLGAGTR
HVNAEPETPN MDVIGERIKR IKEEHNSTWH YDDENPYKTW AYHGSYEVKA TGSASSMING
VVKLLTKPWD VVPMVTQMAM TDTTPFGQQR VFKEKVDTRT PRSMPGTRRV MEITAEWLWR
TLGRNKKPRL CTREEFTKKV RTNAAMGAVF TEENQWDSAK AAVEDEDFWK LVDRERELHK
LGKCGSCVYN MMGKREKKLG EFGKAKGSRA IWYMWLGARY LEFEALGFLN EDHWFSRENS
YSGVEGEGLH KLGYILRDIS KIPGGAMYAD DTAGWDTRIT EDDLHNEEKI TQQMDPEHRQ
LANAIFKLTY QNKVVKVQRP TPTGTVMDII SRKDQRGSGQ VGTYGLNTFT NMEAQLIRQM
EGEGVLSKAD LENPHLPEKK ITQWLETKGV ERLKRMAISG DDCVVKPIDD RFANALLALN
DMGKVRKDIP QWQPSKGWHD WQQVPFCSHH FHELIMKDGR KLVVPCRPQD ELIGRARISQ
GAGWSLRETA CLGKAYAQMW SLMYFHRRDL RLASNAICSA VPVHWVPTSR TTWSIHAHHQ
WMTTEDMLTV WNRVWIEDNP WMEDKTPVTT WENVPYLGKR EDQWCGSLIG LTSRATWAQN
IPTAIQQVRS LIGNEEFLDY MPSMKRFRKE EELEGAIW
//
