ID V9IS50_9FLAV Unreviewed; 3390 AA. AC V9IS50; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 02-DEC-2020, entry version 49. DE RecName: Full=Core protein {ECO:0000256|ARBA:ARBA00019458}; DE EC=3.4.21.91 {ECO:0000256|ARBA:ARBA00013228}; DE EC=3.6.1.15 {ECO:0000256|ARBA:ARBA00012445}; DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552}; DE AltName: Full=Envelope protein E {ECO:0000256|ARBA:ARBA00017531}; DE AltName: Full=Flavivirin protease NS2B regulatory subunit {ECO:0000256|ARBA:ARBA00013313}; DE AltName: Full=Flavivirin protease NS3 catalytic subunit {ECO:0000256|ARBA:ARBA00018941}; DE AltName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; DE AltName: Full=Matrix protein {ECO:0000256|ARBA:ARBA00017678}; DE AltName: Full=Non-structural protein 1 {ECO:0000256|ARBA:ARBA00016002}; DE AltName: Full=Non-structural protein 2A {ECO:0000256|ARBA:ARBA00019777, ECO:0000256|ARBA:ARBA00019791}; DE AltName: Full=Non-structural protein 2B {ECO:0000256|ARBA:ARBA00019779}; DE AltName: Full=Non-structural protein 3 {ECO:0000256|ARBA:ARBA00016254}; DE AltName: Full=Non-structural protein 4A {ECO:0000256|ARBA:ARBA00019785}; DE AltName: Full=Non-structural protein 4B {ECO:0000256|ARBA:ARBA00019812}; DE AltName: Full=Peptide 2k {ECO:0000256|ARBA:ARBA00018340}; DE AltName: Full=Peptide pr {ECO:0000256|ARBA:ARBA00017165}; DE AltName: Full=Protein prM {ECO:0000256|ARBA:ARBA00013848}; DE AltName: Full=RNA-directed RNA polymerase NS5 {ECO:0000256|ARBA:ARBA00016595}; DE AltName: Full=Serine protease NS3 {ECO:0000256|ARBA:ARBA00016200}; DE AltName: Full=Serine protease subunit NS2B {ECO:0000256|ARBA:ARBA00015417}; DE AltName: Full=Small envelope protein M {ECO:0000256|ARBA:ARBA00018173}; OS Dengue virus 3. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Flavivirus. OX NCBI_TaxID=11069 {ECO:0000313|EMBL:AFK83764.1, ECO:0000313|Proteomes:UP000128110}; RN [1] {ECO:0000313|EMBL:AFK83764.1, ECO:0000313|Proteomes:UP000128110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D3PY/AS10/03 {ECO:0000313|EMBL:AFK83764.1}; RA Alfonso H.L., Amarilla A.A., Goncaves P.F., Barros M.T., Silva E.V.D.A., RA Nunes M., Vasconcelos P.F.C., Vieira D.S., Batista W.C., Bobadilla M.L., RA Vazquez C., Moran M., Figueiredo L.T.M., Aquino V.H.; RT "Molecular characterization of dengue virus type 3 isolated in Brazil and RT Paraguay."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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=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; JF808129; AFK83764.1; -; Genomic_RNA. DR Proteomes; UP000128110; 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:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. 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:UniProtKB-EC. DR GO; GO:0003968; F:RNA-directed 5'-3' 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:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. DR GO; GO:0039564; P:suppression by virus of host 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:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR CDD; cd12149; Flavi_E_C; 1. DR Gene3D; 1.10.10.930; -; 1. DR Gene3D; 1.10.8.970; -; 1. DR Gene3D; 1.20.1280.260; -; 1. DR Gene3D; 2.40.10.10; -; 2. DR Gene3D; 2.60.260.50; -; 1. 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 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; IPR001122; Flavi_capsidC. DR InterPro; IPR037172; Flavi_capsidC_sf. 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; 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; IPR014412; Gen_Poly_FLV. 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; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases. 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; PF00949; Peptidase_S7; 1. DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF101257; SSF101257; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF56672; SSF56672; 1. 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 4: Predicted; KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050}; 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, ECO:0000256|SAM:Phobius}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE- KW ProRule:PRU00859, 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}; KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 46..69 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 722..746 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 752..771 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1157..1175 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1195..1218 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2147..2166 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2173..2190 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2196..2213 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2225..2242 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1344..1473 FT /note="FLAVIVIRUS_NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1474..1651 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1654..1810 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1820..1986 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2492..2753 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 3017..3167 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1396..1435 FT /note="Interacts with and activates NS3 protease" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00859" FT ACT_SITE 1524 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1548 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1608 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT METAL 2927 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2931 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2936 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2939 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3202 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3218 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3337 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2546 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2576 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2577 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2594 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2595 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2621 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2622 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2708 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" 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 463..563 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 580..611 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" SQ SEQUENCE 3390 AA; 377814 MW; 594D3241159AD3DB CRC64; MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSKGLLNG QGPMKLVMAF IAFLRFLAIP PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK TSLCLMMILP AALAFHLTSR DGEPRMIVGK NERGKSLLFK TASGINMCTL IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC WCNLTSTWVT YGTCNQAGEH RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW ALRHPGFTIL ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT DSRCPTQGEA VLPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ CLEPIEGKVV QYENLKYTVI ITVHTGDQHQ VGNETQGVTA EITPQASTTE AILPEYGTLG LECSPRTGLD FNEMILLTMK NKAWMVHRQW FFDLPLPWTS GATTETPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT ALTGATEIQN SGGTSIFAGH LKCRLKMDKL ELKGMSYAMC TNTFVLKKEV SETQHGTILI KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP FGESNIVIGI GDNALKINWY KKGSSIGKMF EATARGARRM AILGDTAWDF GSVGGVLNSL GKMVHQIFGS AYTALFSGVS WVMKIGIGVL LTWIGLNSKN TSMSFSCIAI GIITLYLGAV VQADMGCVIN WKGKELKCGS GIFVTNEVHT WTEQYKFQAD SPKRLATAIA GAWENGVCGI RSTTRMENLL WKQIANELNY ILWENNIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE TQNSSFIIDG PNTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ LCDHRLMSAA VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWSNGVL ESDMIIPKSL AGPISQHNHR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI TENCGTRGPS LRTTTVSGKL IHEWCCRSCT LPPLRYMGED GCWYGMEIRP ISEKEENMVK SLVSAGSGKV DNCTMGVLCL AILFEDVMRG KFGKKHMIAG VFFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN GIALGLMALK LITQFETYQL WTALISLTCS NTMFTLTVAW RTATLILAGV SLLPVCQSSS MRKTDWLPMA VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL LIACYVITGT SADLTVEKAA DITWEEEAEQ TGVSHNLMTT VDDDGTMRIK DDETENILTV LLKTALTIVS GVFPYSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE QEEGVYRIKQ QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTYNGKRLEP NWASVKKDLI SYGGGWRLSA QWQKGEEVQV IAVEPGKNPK NFQTMPGTFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA IVREAIKRRL RTLILAPTRV VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT MRLLSPVRVP TYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP QSNAPIQDEE RDIPERSWNS GNEWITDFAG KTVWFVPSIK AGNDIANCLR KNGKKVIQLS RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FKADRVIDPR RCLKPVILTD GPERVILAGP MPVTAASAAQ RRGRVGRNPQ KENDQYIFTG QPLNNDEDHA HWTEAKMLLD NINTPEGIIP ALFEPEREKS AAIDGEYRLK GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG QRNNQILEEN MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL GLMILLTGGA MLFLISGKGI GKTSIGLICV IASSGMLWMA EIPLQWIASA IVLEFFMMVL LIPEPEKQRT PQDNQLAYVV IGILTLAAII AANEMGLLET TKRDLGMSKE PGVVSPTSYL DVDLHPASAW TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC YSQVNPLTLT AAVLLLITHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEALTLAT GPITTLWEGS PGKFWNTTIA VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK SGITEVDRTE AKEGLKRGEI THHAVSRGSA KLQWFVERNM VIPEGRVIDL GCGRGGWSYY CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES SPSPTVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS RNSTHEMYWI SNGTGNIVAS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET PNMDVIGERI KRTKEEHNST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRSMPGTR RVMGITAEWL WRTLGRNKKP RLCTREEFTK KVRTNAAMGA VFTEENQWDS AKAAVEDEDF WKLVDREREL HKLGKCGSCV YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH RQLANAIFKL TYQNKVVKVQ RPTPTGTVMD IISRKDQRGS GQVGTYGLNT FTNMEAQLIR QMEGEGVLSK ADLENPHLPE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD IPQWQPSKGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE TACLGKAYAQ MWSLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML TVWNRVWIED NPWMEDKTPV TTWENVPYLG KREDQWCGSL IGLTSRATWA QNIPTAIQQV RSLIGNEEFL DYMPSMKRFR KEEESEGAIW //