ID A0A1B1LN31_9FLAV Unreviewed; 464 AA. AC A0A1B1LN31; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 22-FEB-2023, entry version 27. 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; Flavivirus. OX NCBI_TaxID=11060 {ECO:0000313|EMBL:ANS54450.1}; RN [1] {ECO:0000313|EMBL:ANS54450.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UOH_3001 {ECO:0000313|EMBL:ANS54450.1}; RA Vaddadi K., Gandikota C., Venkataramana M.; RT "Molecular characterization of dengue virus serotypes in Southern India."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. 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}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004153}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. 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; KU551902; ANS54450.1; -; Genomic_RNA. DR SMR; A0A1B1LN31; -. 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-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. 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: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; cd17931; DEXHc_viral_Ns3; 1. DR CDD; cd18806; SF2_C_viral; 1. DR Gene3D; 2.40.10.120; -; 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 InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF00949; Peptidase_S7; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; 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 DOMAIN 1..177 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 179..335 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 345..464 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ANS54450.1" FT NON_TER 464 FT /evidence="ECO:0000313|EMBL:ANS54450.1" SQ SEQUENCE 464 AA; 51342 MW; 65E07C46CC041E87 CRC64; GVLWDVPSPP PVGKAELEDG AYRIKQKGIL GYSQIGAGVY KEGTFHTMWH VTRGAVLMHK GKRIEPSWAD VRKDLISYGG GWKLEGEWKE GEEVQVLALE PGKNPRAVQT KPGLFKTNTG TIGAVSLDFS PGTSGSPIVD KKGKVVGLYG NGVVTRSGTY VSAIAQTEKS IEDNPEIEDD IFRKRRLTIM DLHPGAGKTK RYLPAIVREA IKRGLRTLIL APTRVVAAEM EEALRGLPIR YQTPAIRAEH TGREIVDLMC HATFTMRLLS PVRVPNYNLI IMDEAHFTDP ASIAARGYIS TRVEMGEAAG IFMTATPPGS RDPFPQSNAP IMDEEREIPE RSWNSGHEWV TDFKGKTVWF VPSIKAGNDI AACLRKNGKK VIQLSRKTFD SEYIKTRTND WDFVVTTDIS EMGANFKAER VIDPRRCMKP VILTDGEERV ILAGPMPVTH SSAAQRRGRI GRNP //