ID V5TGF6_9FLAV Unreviewed; 618 AA. AC V5TGF6; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 12-AUG-2020, entry version 29. 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. OC Viruses; Riboviria; Flaviviridae; Flavivirus. OX NCBI_TaxID=12637 {ECO:0000313|EMBL:AHB63926.1}; RN [1] {ECO:0000313|EMBL:AHB63926.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DENV-2/PK {ECO:0000313|EMBL:AHB63926.1}; RA Akram M., Idrees M., Fatima Z.; RT "Complete genome sequence of Dengue serotype 2 isolated in Pakistan."; RL Submitted (JUL-2013) 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=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}. 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; KF381205; AHB63926.1; -; Genomic_RNA. DR GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; 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; 2. 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 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 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..178 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 180..336 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 346..513 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AHB63926.1" FT NON_TER 618 FT /evidence="ECO:0000313|EMBL:AHB63926.1" SQ SEQUENCE 618 AA; 69247 MW; 70974FE11683A012 CRC64; AGVLSAVPSP PPVGKAELED GAYRIKQKGI LGYSQIGAGV YKEGTFHTMW HVTRGAVLMH KGKRIEPSWA DVRKDLISYG GGRKLEGEWK EGEEVQVLAL EPGKNPRAVQ TKPGLFKTNT GTIGAVSLDF SPGASGSPIV DKKGKVVGLY GNGVVTRSGT YVSAIAQTEK SIEDNPEIED DIFRKKRLTI MDLHPGAGKT KRYLPAIVRE AIKRGLRTLI LAPTRVVAAE MEEALRGLPI RYQTPAIRAE HTGREIVDLM CHATFTMRLL SPVRVPNYNL IIMDEAHFTD PASIAARGYI STRVEMGEAA GIFMTATPPG SRDPFPQSNA PIMDEEREIP ERSWNSGHEW VTDFKGKTVW FVPSIKAGND IAACLRKNGK KVIQLSRKTF DSEYIKTRTN DWDFVVTTDI SEMGANFKAE RVIDPRRCMK PVILTDGEER VILAGPMPVT HSSAAQRRGR IGRNPKNEND QYIYMGEPLE NDEDCAHWKE AKMLLDNINT PEGIIPSMFE PEREKVDAID GEYRLRGEAR KTFVDLMRRG DLPVWLAYRV AAEGINYADR RWCFDGIKNN QILEENVEVE IWTKEGERKK LKPRWLDARI YSDPLALKEF KEFAAGRK //