ID Q32ZD3_9FLAV Unreviewed; 3405 AA. AC Q32ZD3; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 28-JUN-2023, entry version 133. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; OS Sepik virus. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Flavivirus. OX NCBI_TaxID=44026 {ECO:0000313|EMBL:AAV34159.1, ECO:0000313|Proteomes:UP000124629}; RN [1] {ECO:0000313|EMBL:AAV34159.1, ECO:0000313|Proteomes:UP000124629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 insights RT into components, mechanisms, and unique traits as well as their RT evolutionary trends."; RL Clin. Microbiol. Rev. 18:608-637(2005). 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; AY632543; AAV34159.1; -; Genomic_RNA. DR MEROPS; S07.001; -. DR Proteomes; UP000124629; Genome. 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: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:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC. 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule 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 CDD; cd17931; DEXHc_viral_Ns3; 1. DR CDD; cd12149; Flavi_E_C; 1. DR CDD; cd17038; Flavi_M; 1. DR CDD; cd23204; Flavivirus_RdRp; 1. DR Gene3D; 1.10.260.90; -; 1. DR Gene3D; 1.20.1280.260; -; 1. DR Gene3D; 2.40.10.120; -; 2. 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; 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; IPR001122; Flavi_capsidC. DR InterPro; IPR011492; Flavi_DEAD. 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; IPR011998; Flavi_Glycoprot_E_cen/dimer. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR000752; Flavi_NS2A. DR InterPro; IPR000487; Flavi_NS2B. DR InterPro; IPR001850; Flavi_NS3_S7. 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; IPR047530; Flavi_RdRp. DR InterPro; IPR000208; Flavi_RdRp_fingers/palm. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf. DR InterPro; IPR014412; Gen_Poly_FLV. 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; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases_sf. 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; PF20483; Flavi_NS5_thumb; 1. DR Pfam; PF01570; Flavi_propep; 1. DR Pfam; PF01728; FtsJ; 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; 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 ECO:0000256|PIRSR:PIRSR003817-3}; 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}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR003817-4}; 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}; KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 39..56 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 719..743 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 750..770 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1154..1176 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1227..1245 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1319..1343 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1350..1371 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1377..1395 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1446..1473 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2152..2175 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2182..2198 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2204..2222 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2234..2251 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2286..2307 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1350..1479 FT /note="Flavivirus NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1480..1659 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1664..1820 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1815..1992 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..3180 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1402..1441 FT /note="Interacts with and activates NS3 protease" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00859" FT REGION 1937..1958 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1531 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1555 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1616 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT BINDING 2938 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2942 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2947 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2950 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3215 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3350 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT DISULFID 283..310 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 340..396 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 354..385 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 372..401 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 462..560 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 577..607 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" 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 //