ID A0A1B1LN31_9FLAV Unreviewed; 464 AA. AC A0A1B1LN31; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 11-DEC-2019, entry version 15. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS01197934}; DE Flags: Fragment; OS Dengue virus 2. OC Viruses; Riboviria; 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=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.48; Evidence={ECO:0000256|SAAS:SAAS01197940}; CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS01197955}. 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: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 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 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|SAAS:SAAS01197942}; KW Helicase {ECO:0000256|SAAS:SAAS01197975}; KW Hydrolase {ECO:0000256|SAAS:SAAS01197968}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS01197967}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01197972}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS01197959}; KW Transferase {ECO:0000256|SAAS:SAAS01197951}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS01197961}; KW Virion {ECO:0000256|SAAS:SAAS01197947}. 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 //