ID A0A1B1LN31_9FLAV Unreviewed; 464 AA. AC A0A1B1LN31; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 02-JUN-2021, entry version 20. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; DE EC=3.4.21.91 {ECO:0000256|ARBA:ARBA00013228}; DE EC=3.6.1.15 {ECO:0000256|ARBA:ARBA00012445}; DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552}; DE AltName: Full=Non-structural protein 1 {ECO:0000256|ARBA:ARBA00016002}; DE AltName: Full=Non-structural protein 2A {ECO:0000256|ARBA:ARBA00019777, ECO:0000256|ARBA:ARBA00019791}; DE AltName: Full=Non-structural protein 3 {ECO:0000256|ARBA:ARBA00016254}; DE AltName: Full=Serine protease NS3 {ECO:0000256|ARBA:ARBA00016200}; DE Flags: Fragment; OS Dengue virus 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 -!- 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}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. 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:0016021; C:integral component of 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:nucleoside-triphosphatase 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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 2.40.10.10; -; 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; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 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-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; 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 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 //