ID I3UJT6_9FLAV Unreviewed; 2073 AA.
AC I3UJT6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:AFK65750.1};
RN [1] {ECO:0000313|EMBL:AFK65750.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DENV-2/NI/BID-V3226/2008 {ECO:0000313|EMBL:AFK65750.1};
RX PubMed=22647702; DOI=10.1128/JVI.00736-12;
RA Parameswaran P., Charlebois P., Tellez Y., Nunez A., Ryan E.M.,
RA Malboeuf C.M., Levin J.Z., Lennon N.J., Balmaseda A., Harris E., Henn M.R.;
RT "Genome-wide patterns of intrahuman dengue virus diversity reveal
RT associations with viral phylogenetic clade and interhost diversity.";
RL J. Virol. 86:8546-8558(2012).
RN [2] {ECO:0000313|EMBL:AFK65750.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DENV-2/NI/BID-V3226/2008 {ECO:0000313|EMBL:AFK65750.1};
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RG Genome Resources in Dengue Consortium;
RA Henn M., Balmaseda A., Young S., Koehrsen M., Lennon N., Anderson S.,
RA Rizzolo K., Green L., Ryan E., Yu Q., Berlin A., Neiman D., Sykes S.,
RA Borenstein D., Engels R., Freedman E., Gellesch M., Heilman E., Howarth C.,
RA Jen D., Larson L., Neiman D., Park D., Pearson M., Roberts A., Sisk P.,
RA Stolte C., White J., Alvarado L., Godfrey P., Shenoy N., Yandava C.,
RA Zeng Q., Gomez T., Nunez A., Nusbaum C., Harris E., Birren B.;
RL Submitted (MAY-2012) 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; JX079689; AFK65750.1; -; 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; cd18806; SF2_C_viral; 1.
DR Gene3D; 2.40.10.120; -; 2.
DR Gene3D; 3.30.70.2840; Flavivirus RNA-directed RNA polymerase, thumb domain; 1.
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; 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; 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; 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; 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:ARBA00022883};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022883};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
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:ARBA00022883};
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 388..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 677..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1377..1396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1403..1420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1426..1443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1455..1472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 575..704
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 705..882
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 884..1040
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1050..1217
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1722..1984
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFK65750.1"
FT NON_TER 2073
FT /evidence="ECO:0000313|EMBL:AFK65750.1"
SQ SEQUENCE 2073 AA; 230112 MW; 7CDDC4694BCE8C0D CRC64;
MVQADSGCVV SWKNKELKCG SGIFITDNVH TWTEQYKFQP ESPSKLASAI QKAHEEGICG
IRSVTRLENL MWKQITPELN HILSENEVKL TIMTGDIKGI MQAGKRSLRP QPTELKYSWK
TWGKAKMLST ESHNQTFLID GPETAECPNT NRAWNSLEVE DYGFGVFTTN IWLKLREKQD
VFCDSKLMSA AIKDNRAVHA DMGYWIESAL NDTWKMEKAS FIEVKSCHWP KSHTLWSNGV
LESEMIIPKN FAGPVSQHNY RPGYHTQTAG PWHLGKLEMD FDFCEGTTVV VTEDCGNRGP
SLRTTTASGK LITEWCCRSC TLPPLRYRGE DGCWYGMEIR PLKEKEENLV NSLVTAGHGQ
IDNFSLGVLG MALFLEEMLR TRIGTKHAIL LVAVSFVTLI TGNMSFRDLG RVMVMVGATM
TDDIGMGVTY LALLAAFKVR PTFAAGLLLR KLTSKELMMA TIGIALLSQS TIPETILELT
DALALGMMVL KIVRNMEKYQ LAVTIMAISC VPNAVILQNA WKVSCTILAA VSVSPLLLTS
SQQKADWIPL ALTIKGLNPT AIFLTTLSRT SKKRSWPLNE AIMAVGMVSI LASSLLKNDI
PMTGPLVAGG LLTVCYVLTG RSADLELERA ADVKWEDQAE ISGSSPILSI TISEDGSMSI
KNEEEEQTLT ILIRTGLLVI SGVFPVSIPI TAAAWYLWEV KKQRAGVLWD VPSPPPVEKA
ELEDGAYRIK QRGILGYSQI GAGVYKEGTF HTMWHVTRGA VLMHRGKRIE PSWADVKKDL
ISYGGGWKLE GEWKEGEEVQ VLALEPGKNP RAVQTKPGIF KTNTGTIGAV SLDFSPGTSG
SPIVDRKGKV VGLYGNGVVT RSGAYVSAIA QTEKSIEDNP EIEDDIFRKK RLTIMDLHPG
AGKTKRYLPA IVREAIKRGL RTLILAPTRV VAAEMEEALR GLPIRYQTPA IKTEHTGREI
VDLMCHATFT MRLLSPVRVP NYNLIIMDEA HFTDPASIAA RGYISTRVEM GEAAGIFMTA
TPPGSRDPFP QSNAPIMDEE REIPERSWNS GHEWVTDFKG KTVWFVPSIK AGNDIAACLR
KNGKKVIQLS RKTFDSEYVK TRANDWDFVV TTDISEMGAN FKAERVIDPR RCMKPVILTD
GEERVILAGP MPVTHSSAAQ RRGRIGRNPK NENDQYIYMG EPLENDEDCA HWKEAKMLLD
NINTPEGIIP SMFEPEREKV DAIDGEYRLR GEARKTFVDL MRRGDLPVWL AYKVAAEGIN
YADRKWCFDG IKNNQILEEN MEVEIWTKEG ERKKLKPRWL DARIYSDPLA LKEFKEFAAG
RKSLTLNLIT EMGRLPTFMT QKARNALDNL AVLHTAEAGG RAYNHALSEL PETLETLLLL
TLLATVTGGI FLFLMSGKGI GKMTLGMCCI ITASILLWYA QIQPHWIAAS IILEFFLIVL
LIPEPEKQRT PQDNQLTYVV IAILTVVAAT MANEMGFLEK TKKDLGLGSI TTQESESNIL
DIDLRPASAW TLYAVATTFV TPMLRHSIEN SSVNVSLTAI ANQATVLMGL GKGWPLSKMD
IGVPLLAIGC YSQVNPITLT AALLLLVAHY AIIGPGLQAK ATREAQKRAA AGIMKNPTVD
GITVIDLEPI PYDPKFEKQL GQVMLLILCV TQVLMMRTTW ALCEALTLAT GPISTLWEGN
PGRFWNTTIA VSMANIFRGS YLAGAGLLFS IMKNTTSTRR GTGNIGETLG EKWKSRLNAL
GKSEFQIYKK SGIQEVDRTL AKEGIKRGET DHHAVSRGSA KLRWFVERNM VTPEGKVVDL
GCGRGGWSYY CGGLKNVREV KGLTKGGPGH EEPIPMSTYG WNLVRLQSGV DVFFTPPEKC
DTLLCDIGES SPNPTIEAGR TLRVLNLVEN WLNNNTQFCI KVLNPYMPSV IEKMEALQRQ
YGGALVRNPL SRNSTHEMYW VSNATGNIVS SVNMISRMLI NRFTMKHKKA TYEPDVDLGS
GTRNIGIESE IPNLDIIGKR IEKIKQEHEI SWHYDQDHPY KTWAYHGSYE TKQTGSASSM
VNGVVRLLTK PWDVVPMVTQ MAMTDTTPFG QQR
//
