ID W0LL03_9FLAV Unreviewed; 2387 AA.
AC W0LL03;
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 2.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus denguei;
OC Dengue virus.
OX NCBI_TaxID=11060 {ECO:0000313|EMBL:AHG23109.1};
RN [1] {ECO:0000313|EMBL:AHG23109.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DENV-2/VE/BID-V1143/39083.5 {ECO:0000313|EMBL:AHG23109.1};
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}.
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DR EMBL; KF955340; AHG23109.1; -; 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; 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 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 444..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1144..1163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1170..1187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1193..1210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1222..1239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..471
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 472..649
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 651..807
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 817..984
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1489..1751
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 2015..2164
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHG23109.1"
SQ SEQUENCE 2387 AA; 266861 MW; FF116AB95E8EB010 CRC64;
HLWSNGVLES EMIIPKNFAG PVSQHNYRPG YHTQTAGPWH LGKLEMDFDF CEGTTVVVTE
DCGNRGPSLR TTTASGKLIT EWCCRSCTLP PLRYRGEDGC WYGMEIRPLK EKEENLVNSL
VTAGHGQIDN FSLGVLGMAL FLEEMLRTRV GTKHAILLVA VSFVTLITGN MSFRDLGRVM
VMVGATMTDD IGMGVTYLAL LAAFKVRPTF AAGLLLRKLT SKELMMATIG ITLLSQSTIP
ETILELTDAL ALGMMVLKIV RNMEKYQLAV TIMAISCVPN AVILRNAWKV SCTILAAVSV
SPLLLTSSQQ KADWIPLALT IKGLNPTAIF LTTLSRTSKK RSWPLNEAIM AVGMVSILAS
SLLKNDIPMT GPLVAGGLLT VCYVLTGRSA DLELERAADV KWEDQAEISG SSPILSITIS
EDGSMSIKNE EEEQTLTILI RTGLLVISGV FPVSIPITAA AWYLWEVKKQ RAGVLWDVPS
PPPVGKAELE DGAYRIKQRG ILGYSQIGAG VYKEGTFHTM WHVTRGAVLM HRGKRIEPSW
ADVKKDLISY GGGWKLEGEW KEGEEVQVLA LEPGKNPRAV QTKPGIFKTN TGTIGAVSLD
FSPGTSGSPI VDRKGKVVGL YGNGVVTRSG AYVSAIAQTE KSIEDNPEIE DDIFRKKRLT
IMDLHPGAGK TKRYLPAIVR EAIKRGLRTL ILAPTRVVAA EMEEALRGLP IRYQTPAIKA
EHTGREIVDL MCHATFTMRL LSPVRVPNYN LIIMDEAHFT DPASIAARGY ISTRVEMGEA
AGIFMTATPP GSRDPFPQSN APIMDEEREI PERSWNSGHE WVTDFKGKTV WFVPSIKAGN
DIAACLRKNG KKVIQLSRKT FDSEYVKTRA NDWDFVVTTD ISEMGANFKA ERVIDPRRCM
KPVILTDGEE RVILAGPMPV THSSAAQRRG RIGRNPKNEN DQYIYMGEPL ENDEDCAHWK
EAKMLLDNIN TPEGIIPSMF EPEREKVDAI DGEYRLRGEA RKTFVDLMRR GDLPVWLAYK
VAAEGINYAD RKWCFDGIKN NQILEENVEV EIWTKEGDRK KLKPRWLDAR IYSDPLALKE
FKEFAAGRKS LTLNLITEMG RLPTFMTQKA RNALDNLAVL HTAEAGGRAY NHALSELPET
LETLLLLTLL ATVTGGIFLF LMSGKGIGKM TLGMCCIITA SVLLWYAQIQ PHWIAASIIL
EFFLIVLLIP EPEKQRTPQD NQLTYVVIAI LTVVAATMAN EMGFLEKTKK DLGLGSITTQ
ESESNILDID LRPASAWTLY AVATTFVTPM LRHSIENSSV NVSLTAIANQ ATVLMGLGKG
WPLSKMDIGV PLLAIGCYSQ VNPITLTAAL LLLVAHYAII GPGLQAKATR EAQKRAAAGI
MKNPTVDGIT VIDLEPIPYD PKFEKQLGQV MLLILCVTQV LMMRTTWALC EALTLATGPI
STLWEGNPGR FWNTTIAVSM ANIFRGSYLA GAGLLFSIMK NTTNTRRGTG NIGETLGEKW
KSRLNALGKS EFQIYKKSGI QEVDRTLAKE GIKRGETDHH AVSRGSAKLR WFVERNMVTP
EGKVVDLGCG RGGWSYYCGG LKNVREVKGL TKGGPGHEEP IPMSTYGWNL VRLQSGVDVF
FTPPEKCDTL LCDIGESSPN PTIEAGRTLR VLNLVENWLN NNTQFCIKVL NPYMPSVIEK
METLQRKYGG ALVRNPLSRN STHEMYWVSN ATGNIVSSVN MISRMLINRF TMKHKKATYE
PDVDLGSGTR NIGIESEIPN LDIIGKRIEK IKQEHETSWH YDQDHPYKTW AYHGSYETKQ
TGSASSMVNG VVRLLTKPWD VVPMVTQMAM TDTTPFGQQR VFKEKVDTRT QEPKEGTKKL
MRITAEWLWK ELGKKKTPRM CTREEFTRKV RSNAALGAIF TDENKWKSAR EAVEDGRFWE
LVDKERNLHL EGKCETCVYN MMGKREKKLG EFGKAKGSRA IWYMWLGARF LEFEALGFLN
EDHWFSRGNS LSGVEGEGLH RLGYILRDVG KKEGGAMYAD DTAGWDTRIT LEDLKNEEMV
TNHMKGEHKK LAEAIFKLTY QNKVVRVQRP TPRGTVMDII SRRDQRGSGQ VGTYGLNTFT
NMEAQLIRQM EGEGIFKSIQ HLTATEEIAV QNWLARVGRE RLSRMAISGD DCVVKPIDDR
FASALTALND MGKVRKDIQQ WEPSRGWNDW TQVPFCSHHF HELVMKDGRV LVVPCRNQDE
LIGRARISQG AGWSLKETAC LGKSYAQMWT LMYFHRRDLR LAANAICSAV PSHWVPTSRT
TWSIHAKHEW MTTEDMLAVW NRVWIQENPW MEDKTPVESW EEVPYLGKRE DQWCGSLIGL
TSRATWAKNI QTAINQVRSL IGNEEYTDYM PSMKRFRREE EEAGVLW
//
