ID Q32ZD3_9FLAV Unreviewed; 3405 AA. AC Q32ZD3; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 16-APR-2014, entry version 75. DE SubName: Full=Polyprotein; OS Sepik virus. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; OC Flavivirus; mosquito-borne viruses. OX NCBI_TaxID=44026; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=16223950; DOI=10.1128/CMR.18.4.608-637.2005; RA Kuno G., Chang G.J.; RT "Biological transmission of arboviruses: reexamination of and new RT insights into components, mechanisms, and unique traits as well as RT their evolutionary trends."; RL Clin. Microbiol. Rev. 18:608-637(2005). CC -!- FUNCTION: Envelope protein E binding to host cell surface receptor CC is followed by virus internalization through clathrin-mediated CC endocytosis. Envelope protein E is subsequently involved in CC membrane fusion between virion and host late endosomes. CC Synthesized as a homodimer with prM which acts as a chaperone for CC envelope protein E. After cleavage of prM, envelope protein E CC dissociate from small envelope protein M and homodimerizes (By CC similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane CC protein. Host endoplasmic reticulum membrane; Multi-pass membrane CC protein (By similarity). CC -!- SIMILARITY: Contains RdRp catalytic domain. CC -!- SIMILARITY: Contains helicase ATP-binding domain. CC -!- SIMILARITY: Contains helicase C-terminal domain. 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; AY632543; AAV34159.1; -; Genomic_RNA. DR MEROPS; S07.001; -. 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:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0075512; P:clathrin-mediated endocytosis of virus by host cell; 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:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.98.10; -; 1. DR Gene3D; 3.30.387.10; -; 1. DR Gene3D; 3.30.67.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR000752; Flavi_NS2A. DR InterPro; IPR000487; Flavi_NS2B. DR InterPro; IPR000404; Flavi_NS4A. DR InterPro; IPR001528; Flavi_NS4B. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR027287; Flavovir_Ig-like. DR InterPro; IPR014412; Gen_Poly_FLV. DR InterPro; IPR011998; Glycoprot_cen/dimer. DR InterPro; IPR013756; GlyE_cen_dom_subdom2. DR InterPro; IPR013754; GlyE_dim. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000208; RNA-dir_pol_flavivirus. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR009003; Trypsin-like_Pept_dom. DR Pfam; PF01003; Flavi_capsid; 1. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF02832; Flavi_glycop_C; 1. DR Pfam; PF00869; Flavi_glycoprot; 1. DR Pfam; PF01004; Flavi_M; 1. DR Pfam; PF00948; Flavi_NS1; 1. DR Pfam; PF01005; Flavi_NS2A; 1. DR Pfam; PF01002; Flavi_NS2B; 1. DR Pfam; PF01350; Flavi_NS4A; 1. DR Pfam; PF01349; Flavi_NS4B; 1. DR Pfam; PF00972; Flavi_NS5; 1. DR Pfam; PF01570; Flavi_propep; 1. DR Pfam; PF01728; FtsJ; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00949; Peptidase_S7; 1. DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF56983; SSF56983; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR TIGRFAMs; TIGR04240; flavi_E_stem; 1. DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1. DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1. PE 3: Inferred from homology; KW ATP-binding; Capsid protein; KW Clathrin-mediated endocytosis of virus by host; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Helicase; KW Host endoplasmic reticulum; Host membrane; Host-virus interaction; KW Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase; KW Protease; RNA-directed RNA polymerase; Serine protease; Transferase; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral envelope protein; Viral penetration into host cytoplasm; KW Viral RNA replication; Virion; Virus endocytosis by host; KW Virus entry into host cell. SQ SEQUENCE 3405 AA; 379445 MW; B27D0C3D46A90304 CRC64; MATRGASKSR VTTRGVNMVT AKAKSLAVKI KNKTKQNTRG LRGFLLFLVA QIFWARKLTP QVKKLWRMVD KVQGLKILKK LRNIVTNLMK GLSGRRKRRS PPASIILLLL PLMAYSASVT RQHGAGLLLN VTFADVGKTF EVQGGNCSVN TLEAGKWCDD YVEYACVTLT EGEEPDDLDC WCYGVDNVRV TYGRCKGGGS RRSRRSALIT PHVDKGLTTR QEKWLPSKIG EQQLQKVEKW IIRNPLYALG AIALAYFIGT SVVQKVVIAI LLLGIGPAYS THCLGIPKRD FIRGLDGNTW VSVVLEQGGC VTLIADNKPS VDVWLSSIVV DTPTLVRKIC YESSVTGSKA EGACPTMGDA HLTEEGNEEW ECKRSFSDRG WGNGCGLFGK GSIVACAKFS CTKEMEVYQI DSTKIEYTIS AQVHSGAKKE DWVNHTKLIK FVPTTGTSTV TFTGYGNFGL ECHVQMMVDL GNSYLVKVGT DAWLVNKQWA HDITLPWQSG TGGHWRDKHF MVDFEQPHAV TMKALVLGSQ EGALRTALSG AMVVEVSSNR YTLKGGHVTC KAYMNDLTLK GSTYPMCKKG MSFVKQPVET DHGTAVMQVK VTNGAPCRIP VIASDSMAGT ENRGSVITTN PIAALNNDEV LVEISPPFGE SYIIVGSGDD KLTYHWQRSG STIGNLFTET MKGAQRMIIT GEHSWDFGST GGFFASVGKA IHTVFGTAFH AMFGGLSWMT KILIGGLMVW LGLNSRSSSL SMAFICLGAL LLVLATGVGA EVGCSLNWKQ REVKCGDGMF VFKDTDDWFT KYQYIPEDPK TMAGLIAQAH EEGLCGLNSV GDLEHRMWVS RVDEINAILE ENDIDLTVVV QDSASIYQRG SHAFPRPKGE LKYGWKTWGK NIIFSPSRKN GTFIIDGKSK SECPFNKRVW NSIKVEEFGT GIYQTRVFMR PDYDYSKLCD TGMLGAAAKG DASVHGDPLF WMESQNVNDT WTITSLEALN YRECEWPSSH TLDGSRVIES DMFMPRSLAG PVSRHNHIPG YKVQSSGPWH NTPLEVKREE CPGTHVTVEE TCDDRGKSVR STTDSGKIIP EWCCRSCTMP PVSFWGPDGC WYSMEVRPKH TNEGHLVKSW VVASKGDVDP FSLGLLMLFL CSDMFLMKRF SMRALIAGSI IMLGAMTLGS LTYLDLLRYV VTVGMYMAEA NSGGDVTHLA LIAVFRVRAG FVSVLALKQM WSPRERFVAA CGIVMVQIAL GDIMNTNLME WLNAAGMSIL VIKSIVDPRK CNVVLPLLCL LTPLTTTEIQ RAVMLFCSVV ISVTVLQTDS VSTRKSIPLI ALTICSFFKW TSPFLGLVCY LAFTRIPQRS WPLGETMAAV GLVGVLAGMG LKDMNGMLGP VAVGGVLLIV MSLSGKVDGL VIKKISDIGW DEDAEISGAS HRYDVEQTET GEFKIRNEEP APWTQVMILT IAIVSAAVHP ACLAVVTLGW FFWQKTATRS GVLWDIPTVV PPEEVGYLED GVYTINQKNV LGMAQKGVGV VKDGVFHTMW HVTRGAFLLF EGKRLTPAWA NVKEDLISYG GGWKLEAKWD GTEEVQLIAV APGKNPMNIQ TTPSIFQLTN GKEIGAVNLD FPSGTSGSPI VNKNGEVIGL YGNGILIGNN TYVSAITQSE SSLEQDNDQL QDIPNMLRKG MLTVLDFHPG AGKTRVYLPQ ILKECERLRL KTLVLAPTRV VLSEMKEAMP KMSIKFHTQA FSNTATGKEI IDAMCHATLT HRMLEPTRVT NWEVVIMDEA HFMDPASIAA RGWAAHRSRA RECATIFMSA TPPGTSNEFP ESNGTIEDIR KDIPSEPWTK GHEWILEDRR PTAWFLPSIR VANSIANCLR KAERTVVVLN RKTFEKEYPT IKSKRPDFIL ATDIAEMGAN LRVERVIDCR TAYKPFLVDD GTKVMVKGPL KISASSAAQR RGRVGRDPNR DTDTYVYGDS TTEDNGHYVC WTEGSMLLDN MEIKNGMIAP LYGIEGTKTT TVPGETRLRD EQRKVFRELV KRLDMPVWLS WHVAKAGLKV QDRSWCFDGE DDNTLLNDNG EPIFARSPGG GKKPLKPRWV DTRVCSDNSA LIDFIKFAEG RRSINGLLIG LQGFPKYLSG RMKEAVDTLT VLYNSEAGSR AYKHALAMMP EAVTIFLLIM LTIICTSGIV MFFLAPKGLS RMSMAMMTML VSAYLMSLGG MNPVQVSCVM LVFFIFMVVL IPEPGTQRST YDNQLIYLLV GVMSVILMVT ANEMGMLEKT KRDIFGTTVV EEGKKWTFPE LDLHPGAAWT VYVGLVTLVT PMLHHWIKVD YGNISLSGIT QNAQVLGLMD KGIPFIKMNM SVVILLLSAW NGITLLPLFA GMGAAALHWG FILPGLRAQA AKAAQKRVYH GVAKNPVVDG NPTADIDDAP GMPAMYEKKL ALIILFILAT VNLILTRTPF SIAELVVLGS AALGPLLEGN TNAYWNGPIA VAFTGLMRGN YYATIGLMYN GWLAKQTRRG RAAGVTLGEV WKRQLNMMGK QEFEKYKISD IMEVDRSVAQ RYLKEGRNDV GISVSRGTAK MRWLHERGYV KLSGRVIDLG CGRGGWSYYS AAQKEVMSVK GYTLGINGHE KPVHMQTLGW NIIKFKDKSD VFTMPAEPCE TLLCDIGESS SNFLIEKDRT LKVLENFERW KHVNTENFCV KVLCPYHPDV IEKLERMQLR FGGGLVRIPF SRNSTHEMYY ISGARNNITH MVNTTSRSLL RRMFRPTGKA LVESDVFLPT GTRSVASEAG PVDHDALQLR VDQIKHEYSK TWTIDLNHPY RTWHYLGSYL CKATGSSSSM LNGIVKMLSM PWDKFESVTL LAMTDTTPFG QQRVFKEKVD TRAPSPPPGT RAIMRVVNSW LFKHLAREMR PRICTKEEFI SKVRSHAAIG AYLEEHENWR SASEAVQDPR FWKLVDEERK LHLQGKCRTC VYNMMGKREK KPAEFGKAKG SRAIWYMWLG ARFLEFEALG FLNEDHWVSR GNSGGGVEGT GLQYLGYILK RLGEKPGGRM YADDTAGWDT RITEEDLEDE QEILKYMTKD HKKLAWAVTE LAYKNKVVKV MRPGPGGLTF MDIISRRDQR GSGQVVTYAL NTVTNLKVQL IRMAESEHVI TRHDVESVSP STLRGLEDWL ERFGTDRLSR MAVSGDDCVV KPIDDQFADA LYHLNAMSKI RKDIDDWKPS TGWDSWEAVP FCSHHFHEII LKDGRTIIAP CRDQDELIGR ARVSPGNGWM IRETACLSKA YAQMWLLMYF HRRDLRVMGN AICSAVPVDW VPTGRTTWSI HGKGEWMTTE NMLDVWNRVW IMENPYQADK TPVTEWRDVP YLPKSIDKTC NSLVGTTQRA TWARDVKHTV HRIRKLVGNE KFYDYMSTMD RYRELDEEGP GEILW //