ID A0A679E720_9FLAV Unreviewed; 3363 AA. AC A0A679E720; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 13-SEP-2023, entry version 15. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; OS Culex flavivirus. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Flavivirus. OX NCBI_TaxID=390844 {ECO:0000313|EMBL:BBO25549.1}; RN [1] {ECO:0000313|EMBL:BBO25549.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=16GH36 {ECO:0000313|EMBL:BBO25549.1}; RA Amoa-Bosompem M., Kobayashi D., Murota K., Faizah A.N., Itokawa K., RA Fujita R., Osei J.H.N., Agbosu E., Pratt D., Kimura S., Kwofie K.D., RA Ohashi M., Bonney J.H.K., Dadzie S., Sasaki T., Ohta N., Isawa H., RA Sawabe K., Iwanaga S.; RT "Entomological Assessment of the Status and Risk of Mosquito-borne RT Arboviral Transmission in Ghana."; RL Viruses 12:0-147(2020). CC -!- FUNCTION: Component of the viral RNA replication complex that functions CC in virion assembly and antagonizes the host immune response. CC {ECO:0000256|ARBA:ARBA00024317}. CC -!- FUNCTION: Functions as a signal peptide for NS4B and is required for CC the interferon antagonism activity of the latter. CC {ECO:0000256|ARBA:ARBA00003504}. 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}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004397}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004367}; Lumenal side CC {ECO:0000256|ARBA:ARBA00004367}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004461}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004461}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004461}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00023443}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00023443}; Lumenal side CC {ECO:0000256|ARBA:ARBA00023443}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Membrane CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004385}. 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; LC504568; BBO25549.1; -; Genomic_RNA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW. 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:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral entry into host cell; 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 CDD; cd20761; capping_2-OMTase_Flaviviridae; 1. DR Gene3D; 1.10.260.90; -; 1. DR Gene3D; 2.40.10.120; -; 1. DR Gene3D; 3.30.70.2840; Flavivirus RNA-directed RNA polymerase, thumb domain; 2. 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR Gene3D; 3.30.387.10; Viral Envelope Glycoprotein, domain 3; 1. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1. DR InterPro; IPR011492; Flavi_DEAD. DR InterPro; IPR011998; Flavi_Glycoprot_E_cen/dimer. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR001850; Flavi_NS3_S7. DR InterPro; IPR046811; Flavi_NS5_thumb. DR InterPro; IPR000208; Flavi_RdRp_fingers/palm. DR InterPro; IPR036253; Glycoprot_cen/dimer_sf. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF00869; Flavi_glycoprot; 1. DR Pfam; PF00948; Flavi_NS1; 1. DR Pfam; PF00972; Flavi_NS5; 1. DR Pfam; PF20483; Flavi_NS5_thumb; 1. DR Pfam; PF01728; FtsJ; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00949; Peptidase_S7; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 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 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 Helicase {ECO:0000256|ARBA:ARBA00022806}; 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 Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|ARBA:ARBA00022830}; KW Inhibition of host STAT2 by virus {ECO:0000256|ARBA:ARBA00022883}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW mRNA capping {ECO:0000256|ARBA:ARBA00023042}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}; 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 TRANSMEM 122..142 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1141..1160 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1180..1200 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1207..1224 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1230..1249 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1261..1289 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1336..1353 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1406..1432 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2097..2122 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2173..2193 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2200..2218 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2263..2284 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2296..2314 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2320..2346 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2409..2425 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2437..2465 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1455..1634 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1665..1769 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1780..1955 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2473..2727 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 2991..3138 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1..62 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 23..41 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 3363 AA; 373300 MW; BDDDFC6D20A979C8 CRC64; MGRDDGKKKK GPGSSRWLLP SERAGLGRKE EKKKKEKRSV RSTPQLVSGG AQHRRGGGMG PRARGLLGRL GIGWGSILQE DIVQALMHLV LVLHSVFIAI DRRLRSLTRR VTALEAKRSA KNAVRITLIL TGLMMVLGAV VIDMQVSTAK GTQIFEGKTN RTDHVHLFKL PTDGCWSGTL VMKKCPKVAD LAKDLEGVDC GSSWTEFTLR YHRCVPKKRE RRAANTNQKL DFLAEVELVT FKAIRENKTI AIIVLLCVAI AKRWPMWVVI LLAIGTWTTV KGEFVEPLYT LKAEKMTMLQ TIMRPDESYV ISTPNGLLEF RTGAAEIYGG QWMRELLADC HANASYSTDV CPGGSQLNMG EINGKERVCS TQPYNRGWGT GCFKWGIGFV ATCVELHCEE GYNVSSIARS SIVMNITAKF HSVDDVQQLI SDVPVTFRFA KLGNAAVTCR LESERLLLDY YHVTGKYHEG LFVRSQIDEW PGAHATASGR AGLERIVVWG DARANEVLVK NILEPQLIWD NAIATQDGFR DVGFSCQIML DKLVSGSFKD CPGIKSSVFV QSGFGYDGVV MTSLSKATNE SCSVGLTCHG CYLLATKMVF GPGTSTAKAF VGCGNHTGTL VIGGTTIHVE CVLNPISQGW RMAKHVVDKY RRFGTAGVGG VWYDFVGKFS LFSLLSSSTI LVGLAALVLL DKRIVFLLLL CGYFIYTKAD VGCGFDPERK VVSCGSGGFV WKSLSQWPTR EHSVELDDQH LITALVSEQL KKTNKVCIIC EDVLQCAAAR GAVGDITHVD NEIVYVNTSL SFDRTFPRIP KKVHGVKIGD LTMQLALASV GGAVDPSQYG ELSSGFLSRT KIAETGEHKV IRVITSASPY EKICEQAFAL QYGFVRFTRR VFGSNVVVKP VAKPTDYCPT YLAGSFVKND IGAYTDGMMW MKSKKVNGTW TLVDLELTQS HQCIWPQAYT FDLTAFNDSS LFMPAQYGAP MSKANHIPGY KTQTEFPWYK ADIVLREGVV PGTQVEESPS CDNRGSAVKV DPAIAKKWCC KTCLSADKRV FHFKVDNDYF YPMEIRPAAT QPEVTIDADG EDMDEMASMF GTMKAVVPPV EGSYPDFRLS PSVEGVSPLL VGALLHLLTI RTKHRWAQRT CGTWILFLLF GVPSNTYAGW SWIGLSYSLA AVPNGSALLV HFWLAVQLSS SHLFFLGWAL RQRVRSSVGY ALSVFFAEWL LLKLRQLWES TYLLDHVLFP MYVMLAFNLK SQFVPVDSMV LLNYVVTHPA VATATVTGGA LVICSIRVYK NWGCSPNLWR SGLRASKPSL IAGMCLAGLY VLSTCLEFYQ MPTTASVVFL GGLLIGIVTR MAPPTHLELV PVAGTGVPLD CEEEPTILPS GLEGTYGPDG VEFTNLTDNS RVSTGLLVYV GCMGVMAMNT YVGVILMCAC WWTNAPEWLP LYVAGSSIFR SNEVNDVLIT PPEYEQEAQL SNDFGHLPDG TYRVVARSLF MTSHVGAGYA KDGVFNTLWH VTSGGSLTWQ GRHVRLHSGD VYRDMASYGG PWNIADSPES SVVVRVVQND GSVLCARSST ASISVDGKRV QVIGHDYGKG SSGSPVHALD GRVVGLYGYG FFIGWKYHSL ITSGEVVAED TVEEDTVSRR FVDWHPGKGK TRRVLVEEAK SHIAKEKRLL ILTPTRVVKD EVVRAIAEAC PGVVVGSNLA MYRRNAITVA CHATLTQYLM EKGIDSIRFS TIIMDECHFL DPLSIACRGV MDYYNGKGVA VVYMSATPPG CAGNNGSNHP IADVATQFPR ELTASWVRGQ ANGKTIIFVP TQHQANTLAS ELGGVSLTRE SFDVAIGKAR RQETQFIVST DISEMGANLG VQTVIDTRVA VKPVISEGSV MLEKVGITQA SAIQRRGRTG RREAGKYVYP IGSELENEAT EWACWTEAQM ILDQMACGPM REEIENFQPQ GTYLLAPESR PRFINFIKKD VPVWLAWHWA NAFEHKHSVL FQGQNATSLK IRTEAGDHKY APRFHDDRFE KNNELDKRSK IMLYLKQRSN FNFDLGGVLY GLFVAFRDTN MERLGTSYRS AIEILHEISN VDDPMVSNVV MGKSLQAWAA VIIGMVTGIV LLVVFVVVCR CVKRLFGGKA AAQQSPPYSS FPTVQAAGFC QFGSMVMAIG PLCAVVAGIP PAFVFVAVLG LFVIMCCSAN NVHRAYTTDT VTLVVIGVCV CVMGVVAWEM DLLPNIRRDL GYLLERFASK QEPDIPQASF ARPEVPELHI TSLPGALVVS FAIAIVGGAI ANCLSDSGFL RKLFSNEEQS AAVIGGIQLA LISWETLVPV AFAGFFATTF VTKIYGCMVG GIYLVLAHYD RKYAFTVKAT KVLIARTSRK DLDDEITGRD GVTRGRPTFY ALQICCSLLW TITSPSLKHV VVSVAVIVFA FLTFRRPNNR LLVTFDYSSV LLILMIFAEP GQVFLVGASL LFWFVAHQSR MALRSLVKTD ACGLGYRWKE MLNALDKNAF DKYRSRGVNE TEKGDFVSRG GLKMDELIRK FQWEPRGAAL DLGCGRGGWT QRLVMDTRVN SVMGLTLGGA SRENPLPFKT KGHNLAVLKA GVDVYALEPR DCNTIVCDIG ESDPRPEVEK TRTLKVLTML EKWLIHNPGA AFCCKVLSPY HLEVLRKLEM LQHKHNGKLV RLSLSRNSTA EMYYVSGPRA NIVGSVFHVL GALIGRFKRN DPVQRDAPPK LEMGTRSDPR AKVKLQDPTI VAGRVKRLRE ENASTWFVDR EHPYQSFNYH GSFVTDDISP GGQTVNPMMR RIMWPWDFLS RVTTFMMTDV STYAQQKILR EKVDTLTLEP DQRTRAINRL IMRHFSAMFK RRGLTPRILT PVEYMSNVKS GAAIGGWSKE MPWNKVQEAL ADPVFWRMVA DERARHLRGD CELCVFNTMG KKEKKPSSFG EARGSRIIWY MWLGSRFLEY EALGFLNEDH WVARKNFPCG VGGVGVNYFG YYLKEIMQKG KWMIADDVAG WDTRITEADL EDELWFLLDQ VNDPYHAKLI RVVFKFCYMN MVALFPRNHP QFRSGTVFDV VSRTDQRGSG QVTTYALNTV TNGKNQVGRM LEAEGLLDAP LEVIDGWLSS HLEDVLSGMV VAGDDVVVAT NNENFHTSLR YITAASKTRK NLQPTEPSPR YTSWEHVEFC SHHYHPLVLQ DGREIIAPCR DQHEIIGRAR IQKGGIVDMS AAGCLAKAHA QMWALYYFHR RDLRLGFAAI TSAVPVNWIP TGRISWSVHQ HAEWMTTQDM LEVWNTVWIV NNPWMATKDL VKAWSEIPYL PKTKDINCGS LIGERDRAAW SKNIVSTVST TRRIIEQEAG SQKFTEGLRI LGRYRAPADD VFW //