ID A0A7R7E0K9_9FLAV Unreviewed; 3401 AA. AC A0A7R7E0K9; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 22-FEB-2023, entry version 8. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; OS Mpulungu flavivirus. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Flavivirus. OX NCBI_TaxID=2775126 {ECO:0000313|EMBL:BCL56285.1}; RN [1] {ECO:0000313|EMBL:BCL56285.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZT17-1078 {ECO:0000313|EMBL:BCL56285.1}; RA Harima H., Orba Y., Torii S., Qiu Y., Kajihara M., Eto Y., Matsuta N., RA Hangombe B.M., Eshita Y., Uemura K., Matsuno K., Sasaki M., Yoshii K., RA Nakao R., Takada A., Abe T., Wolfinger M.T., Simmunza M., Sawa H.; RT "African tick flaviviruses forming a novel evolutional clade show unique RT exoribonuclease-resistant RNA structures in the 3'-untranslated region of RT their genomes."; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. 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 -!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the CC serine protease function of NS3. {ECO:0000256|PROSITE- CC ProRule:PRU00859}. 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 -!- SUBUNIT: Interacts (via N-terminus) with serine protease NS3. CC {ECO:0000256|ARBA:ARBA00025871}. 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; LC582740; BCL56285.1; -; 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:0042025; C:host cell nucleus; 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:0003725; F:double-stranded RNA binding; IEA:InterPro. 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:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. 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; 1.20.1280.260; -; 1. DR Gene3D; 2.40.10.120; -; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 1.10.8.970; Flavivirus envelope glycoprotein M-like; 1. DR Gene3D; 2.60.260.50; Flavivirus polyprotein propeptide domain; 1. DR Gene3D; 3.30.70.2840; Flavivirus RNA-directed RNA polymerase, thumb domain; 3. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR Gene3D; 3.30.67.10; Viral Envelope Glycoprotein, domain 2; 1. DR Gene3D; 3.30.387.10; Viral Envelope Glycoprotein, domain 3; 1. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir. DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1. DR InterPro; IPR027287; Flavi_E_Ig-like. DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom. DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf. 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; IPR046811; Flavi_NS5_thumb. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR038688; Flavi_propep_sf. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR011998; Glycoprot_cen/dimer. DR InterPro; IPR036253; Glycoprot_cen/dimer_sf. DR InterPro; IPR038055; Glycoprot_E_dimer_dom. DR InterPro; IPR013756; GlyE_cen_dom_subdom2. 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; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR000208; RNA-dir_pol_flavivirus. 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; 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; PF20483; Flavi_NS5_thumb; 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 SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF81296; E set domains; 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 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 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 ECO:0000256|PROSITE-ProRule:PRU00859}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|PROSITE- KW ProRule:PRU00859}; 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|PROSITE- KW ProRule:PRU00859}; 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|PROSITE- KW ProRule:PRU00859}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE- KW ProRule:PRU00859}; 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 709..734 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 741..761 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1120..1138 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1150..1178 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1190..1209 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1221..1238 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1244..1270 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1277..1294 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1306..1331 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1343..1363 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1369..1387 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1441..1467 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2148..2168 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2175..2192 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2198..2216 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2228..2250 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2283..2301 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2308..2330 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2350..2373 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2417..2435 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1342..1473 FT /note="Flavivirus NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1474..1659 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1665..1820 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1830..2001 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2500..2764 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 3028..3177 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1395..1434 FT /note="Interacts with and activates NS3 protease" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00859" SQ SEQUENCE 3401 AA; 373946 MW; 46AA003913D66C09 CRC64; MAGKPPKRST ARLGQVKSRQ GTGLRAVLMV VVAKVMCILN GWKLPKATKA KWVTTPKEAL LRALKVVRKV VAQLTREVAG RRRANTGQGV LLLMWLSLAL GAHVFMRGDE IVINATRADL AQTFSLSTGG TCTVLATDIG SWCARSIEYD CPEIGNEVEP VDLDCYCRNV TNVRLMYGTC HAGGPRIAER SLSVTPPSQT VLTGRRDVWM EGARWKAHLT RAENWAFRHP LYVACLAALS WSVVRGTFAR AFIFAVLILL APAYGTQCLG VETRDFVQGV SGGTWIDVVL EKGACVTISA PDKPTMDIWL KDIYEEEPAK ERIYCMEAKQ GEIKVNARCP GTSTASLAEE QQASWYCKRT TSPRGWNNGC GLFGQGPIVG CIKVTCKDSS VLTGYDIDPT KAVYVVGIEA HASVANKTTA DPGKQERQFS ASAVSQVFVL GEYGTTTLEC KTAEAVDTSS MVIATLGTDS WIVHKDWFRD LPYPWKYDGG HWEGMENIIH WDPPTAAKMT AALLGDQSGA LRATMAGQVK ATVDTEGGRK RYHPSGGHVT CKVKLNNLKI KGITYRACDP QFKWAKPPTA TPHGTVVMTV TYAGKQKPCR VYATAVANEG DVKNIATQIT ANPIVPSEAS AEHEVLLEMQ VPPGDCIFVI GEAKYRWFQP GSTLGRMAEV TMKGAKRLVL LGDTAWDFGS VGGVLNSIGK GLHQVFGSVF HMVFGGTGFL SRILIGALLI WLGLQAHSTT LSLSFIGIGG MIVSLALGVG ADVACGVDFQ RMEFRCGQAL VVWKETPGWV EGYSLHPEDP GKLAAFVKDA WNEGICGIAP VGRLEHGMWK AVETELNAVL DENMVSVSVV VDPDDYGHYE RGKRKLPHVE ESLDHSWTSW GKSFITAPPR KSKAFLVGRS GQEECPFEKR AWNNFRVTEF GVGLTKTHAY LEVGRLDGMC DTGLMGAAVK NDIAVHADSG MWMQSVRNGT NTTIVQLELL DVKYCTWPAS YTIDNARVEE SLLFMPPKFG GPRSKYNTIP GYKIQVDGPW NKAPLKVERG ECPGTTVKVN ATCDGRGKSM RSTTESGTVI PSWCCRNCSL PPVRFVTKTD CWYPMEIRPV RPGEGFVYAW ALEVNGETII LGWPFGLVAA MMFLQIAIRH GRLGGHKFVW LGLVALFGIV SGIFTFEDLV RVILAIGILW REGVGTEASA ALVLEAVLAV RPGLLLAFVW RKHWNSSQTT ATLLALSFVQ QFLGGYGIPE VFDAMGLVGL MLAAMVQATS FHTGLCIMAL MTTGYPVVTQ AVQLLAVSLA IGQVRKVTKD GAARRAGLTA YVAGVGRFVP GFSTGMAFLV YGVVRRLRAQ RRAALGDGMA CLGVLIMGLK VAMGGSDSLP LVPVVGGVFV VMVAASLGTE GYMHIEKVGE TRWDAQAVIR GSTLNRAVRR DRNGFMHVCD EERHDDVWQM VLLGLTAMAG GIHWGLAACG VVAWLGWNML PRPGNRRADL VGPGPRRTLG EQRTSPLEDG VYRILAPGRL WGHRQAGAGV VIEGVLHTMF HVTHGAVLST DDGYLIPGYA DPERDLVTYA GPWKIAAKWK SGERVQLIAA SPGRPVQNID TLPGEFTLVT GEILGAVNID CPPGTSGSPI LNEDGVVVGL YGNGVIVDDG QYVSAISTTD PTDSSILDWL NENGATWMKA GSVKIVQAAP GSGKTRVLLP RMIAELKAKR KRTLVLAPTR VVLDEMCQAL KGVSKRVTTR GELKESGDGL ITLMCHATFS HLMLTPMARK NFEVVIMDEA HFLDPGSIAA RAYWEGMAKM GMSAFVMMSA TPPGEHLQAF PPAVGTINDR TEHIPTDWNA GHEWITEYEG RTAWFVPSAT AAARLAQVLI RHGKRVLCLS RSNFEKVNPQ VRRGEFDFVL TTDIAEMGAN LGVTRVIDPR LTRKPLARDD GIVMSGSIHV PTASAVQRRG RVGRAPHAVG EYVYQNQPDD DIREWACWTE AQMLLDNFQT PRSVAVGFCA AEAKYQPEAV GYFRLRNDKR EEFVRFLDVK GMTTWAAWKF ADAGMKARDR RWALDGPPTN TIWGSDGQPV MIRTDGVMKE VRMLVSDERF KEPEKVQELL QALRRSAGDI LDALGRVPGH LAQRIPKAAD TLGLLLNAEP GTRAFKEASR EGPEAIELLT LVSITLLLTG GLALVAAFRF TGNRMGVAAL SVAVTAVLMY WGGFSWGAMA GMVMTSTVFF LVVVPEPGGQ RGVLDNQLAY VIIGIAGVVG LVYCNEMGLL EKTKRDLFGP RIVASHPSMS RSWKFPDFRL DPAVTWGIYA GVVSVVTPWL LHMAEQAGAV AAAGVASAGA TSLAVLSSGI PFLGVSYETW AVFASTGWHM SFSTALAASV CCLVHWSIVI PGAQANICRR AFRMVYAMLA KNFSNDGIPT LEVPDTPRLE PAFEKRFAGW IMVALCVVSV VLDASTSNVL LTSMLGTVGM QQALGIETWG LWGIGQACGM AVVLWRADPV GLVPLLCRLV LFQRDGRRGA GHMGPTLGEV WKKRLNAMSK HRFYEYKTAG IVEVNRTEAR EALKRGLTDH GHPVSRGAAK LHWLVERGFL EPKGWVTDLG CGRGGWSQYT ATLPQVTRVV GYTLGTGGHE KPIPTESYGH NIITYHDKVD VMRLPTHLCD TVLCDIGESS SNVDVEAGRT IAVIEMFANW LEANPGAQFC CKVLCPYHPD VLAALEILVR EHGGGLVRVP LSRNSTHEMY WVSGVKNKPT RAVNELSSFL LGRMAKNHEK EIIEEVWLGT GVRHTVSEAE PDDPESIKGR LDRIRRTHEK TWRVDTHHPY RYWNYHGSYE GAQRGSAGSL VNGVVKMLSW PWSTIESVTC MNMTDTTPFG QQRVFREKVD TKVPEPSPGT RKAMAVVAEW MWERFFHRKV ARLCTREEFV AKVHSNAAIG AWDPQMGDWS SAAEAVQDET FWKMVDEERC RHRRGECEMC VYNMMGKREK KPAKFGKARG SRAIWYMWLG SRFLEFEALG FLNEDHWMDR ENSRAGVEGL GVQYLGYVLR DMDRLPGVGY VADDTAGWDT RVSNADLEDE EQLLRWLSPT HRALAEPIMK MAYHNKVALV SRRANDGTLV TDVISRRDQR GSGQVVTYAL NTWTNIKVQL LRMAEAEGIL GDNLLHQARV LPLRNWLARH GEERMSRMAI SGDDCVVRPP SEEFAFALKA LNDMGKVRKD KPEWEPSDIY AGWEDVPFCS HHFHELVLQD GRQIVVPCRD QDELVGRARI APGAGWSVAE TACLAKAYAQ MWLLLYPHRR DLRLLAFAVC SAVPVNWMPT GRTTWSVHAT REWMTNEDML DVWNQVWIED NPWMEEKTRV RHWNQVPYLP KSSDIACGSL IGRVNRAAWA RSIRDSVSKV RAKLGAERYV DYLGAMGRYV VQQSCYHTEV L //