ID A0A0E3GIF0_9FLAV Unreviewed; 495 AA. AC A0A0E3GIF0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 25-OCT-2017, entry version 15. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00006300}; DE Flags: Fragment; OS Dengue virus 2. OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Flaviviridae; Flavivirus; Dengue virus group. OX NCBI_TaxID=11060 {ECO:0000313|EMBL:AJQ21163.1}; RN [1] {ECO:0000313|EMBL:AJQ21163.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SG {ECO:0000313|EMBL:AJQ21163.1}; RX PubMed=25846296; RA Ng L.C., Chem Y.K., Koo C., Mudin R.N., Amin F.M., Lee K.S., RA Kheong C.C.; RT "2013 dengue outbreaks in Singapore and Malaysia caused by different RT viral strains."; RL Am. J. Trop. Med. Hyg. 92:1150-1155(2015). CC -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and CC is required for the interferon antagonism activity of the latter. CC {ECO:0000256|SAAS:SAAS00891765}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|SAAS:SAAS00006192}. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC {ECO:0000256|SAAS:SAAS00006038}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|SAAS:SAAS00006246}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S- CC adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. CC {ECO:0000256|SAAS:SAAS00006356}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl CC 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S- CC adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'- CC triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA]. CC {ECO:0000256|SAAS:SAAS00418663}. CC -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds CC in which each of the Xaa can be either Arg or Lys and Yaa can be CC either Ser or Ala. {ECO:0000256|SAAS:SAAS00006223}. CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane CC {ECO:0000256|SAAS:SAAS00536713}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS00536713}. CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane CC {ECO:0000256|SAAS:SAAS00536715}; Peripheral membrane protein CC {ECO:0000256|SAAS:SAAS00536715}; Cytoplasmic side CC {ECO:0000256|SAAS:SAAS00536715}. CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane CC {ECO:0000256|SAAS:SAAS00536731}; Peripheral membrane protein CC {ECO:0000256|SAAS:SAAS00536731}; Lumenal side CC {ECO:0000256|SAAS:SAAS00536731}. CC -!- SUBCELLULAR LOCATION: Host nucleus CC {ECO:0000256|SAAS:SAAS00536712}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|SAAS:SAAS00536690}. CC -!- SUBCELLULAR LOCATION: Virion membrane CC {ECO:0000256|SAAS:SAAS00595647}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS00595647}. 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; KJ806785; AJQ21163.1; -; Genomic_RNA. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR CDD; cd12149; Flavi_E_C; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 3.30.387.10; -; 1. DR Gene3D; 3.30.67.10; -; 1. DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1. DR InterPro; IPR027287; Flavi_E_Ig-like. DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like. DR InterPro; IPR011998; Glycoprot_cen/dimer. DR InterPro; IPR036253; Glycoprot_cen/dimer_sf. DR InterPro; IPR013756; GlyE_cen_dom_subdom2. DR InterPro; IPR014756; Ig_E-set. DR Pfam; PF02832; Flavi_glycop_C; 1. DR Pfam; PF00869; Flavi_glycoprot; 1. DR SUPFAM; SSF56983; SSF56983; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR TIGRFAMs; TIGR04240; flavi_E_stem; 1. PE 4: Predicted; KW Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00006413}; KW ATP-binding {ECO:0000256|SAAS:SAAS00006216}; KW Capsid protein {ECO:0000256|SAAS:SAAS00489305}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00139753}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|SAAS:SAAS00489633}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|SAAS:SAAS00489579}; KW Helicase {ECO:0000256|SAAS:SAAS00006215}; KW Host endoplasmic reticulum {ECO:0000256|SAAS:SAAS00006452}; KW Host membrane {ECO:0000256|SAAS:SAAS00489598}; KW Host nucleus {ECO:0000256|SAAS:SAAS00007343}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00140013}; KW Hydrolase {ECO:0000256|SAAS:SAAS00489277}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|SAAS:SAAS00006449}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|SAAS:SAAS00006440}; KW Inhibition of host STAT2 by virus {ECO:0000256|SAAS:SAAS00891972}; KW Membrane {ECO:0000256|SAAS:SAAS00139757, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|SAAS:SAAS00006255}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00006310}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00006429}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00006088}; KW Protease {ECO:0000256|SAAS:SAAS00139752}; KW RNA-binding {ECO:0000256|SAAS:SAAS00006139}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00006030}; KW Secreted {ECO:0000256|SAAS:SAAS00007119}; KW Serine protease {ECO:0000256|SAAS:SAAS00489446}; KW Transferase {ECO:0000256|SAAS:SAAS00006428}; KW Transmembrane {ECO:0000256|SAAS:SAAS00139804, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00489272, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00139905}; KW Viral envelope protein {ECO:0000313|EMBL:AJQ21163.1}; KW Viral immunoevasion {ECO:0000256|SAAS:SAAS00006449}; KW Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489650}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS00007194}; KW Virion {ECO:0000256|SAAS:SAAS00139808}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00140014}. FT TRANSMEM 442 466 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 473 493 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 296 Flavi_glycoprot. {ECO:0000259|Pfam: FT PF00869}. FT DOMAIN 298 393 Flavi_glycop_C. {ECO:0000259|Pfam: FT PF02832}. FT NON_TER 1 1 {ECO:0000313|EMBL:AJQ21163.1}. FT NON_TER 495 495 {ECO:0000313|EMBL:AJQ21163.1}. SQ SEQUENCE 495 AA; 54210 MW; 0054E60A9EDE325C CRC64; MRCIGISNRD FVEGVSGGSW VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KHPATLRKYC IEAKLTNTTT ASRCPTQGEP SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMEGKIV QPENLEYTIV ITPHSGEENA VGNDTGKHGK EIKVTPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ MENKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYVII GVEPGQLKLS WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VVITWIGMNS RSTSLSVSLV LVGVVTLYLG VMVQA //