ID Q91NH1_9FLAV Unreviewed; 3392 AA. AC Q91NH1; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 07-APR-2021, entry version 144. 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 1. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Flavivirus. OX NCBI_TaxID=11053 {ECO:0000313|EMBL:AAK60418.1, ECO:0000313|Proteomes:UP000102548}; RN [1] {ECO:0000313|EMBL:AAK60418.1, ECO:0000313|Proteomes:UP000102548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D1/H/IMTSSA/98/606 {ECO:0000313|EMBL:AAK60418.1}; RX PubMed=11369871; RA Tolou H.J., Couissinier-Paris P., Durand J.P., Mercier V., de Pina J.J., RA de Micco P., Billoir F., Charrel R.N., de Lamballerie X.; RT "Evidence for recombination in natural populations of dengue virus type 1 RT based on the analysis of complete genome sequences."; RL J. Gen. Virol. 82:1283-1290(2001). 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; AF298808; AAK60418.1; -; Genomic_RNA. DR IntAct; Q91NH1; 11. DR MINT; Q91NH1; -. DR MEROPS; S07.001; -. DR BRENDA; 3.4.21.91; 9643. DR Proteomes; UP000102548; 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; cd20761; capping_2-OMTase_Flaviviridae; 1. 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; -; 1. 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}; 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 46..69 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 101..118 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 724..748 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 755..773 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1124..1146 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1158..1177 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1197..1220 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1442..1469 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2149..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..2215 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2227..2244 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1346..1475 FT /note="FLAVIVIRUS_NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1476..1653 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1656..1812 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1822..1988 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2495..2756 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 3020..3169 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1398..1437 FT /note="Interacts with and activates NS3 protease" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00859" FT ACT_SITE 1526 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1550 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1610 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT METAL 2930 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2934 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2939 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2942 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3204 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3220 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3339 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2549 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2579 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2580 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2597 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2598 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2624 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2625 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2711 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 465..565 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 582..613 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" SQ SEQUENCE 3392 AA; 379033 MW; 5BD567C366E75623 CRC64; MNNQRKKTGR PSFNMLKRAR NRVSTVSQLA KRFSKGLLSG QGPMKLVMAF IAFLTFLAIP PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR SVTMLLMLLP TVLAFHLTTR GGEPHMIVTK QERGKSLLFK TSTGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQRVETW ALRHPGFTVT ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLITCAKFK CVTKLEGKIV QYENLKYSVI VTVHTGDQHQ VGNESTEHGT TATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT MKEKSWLVHK QWFLDLPLPW TSGATTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV LVQVKYEGTD APCKIPFSTQ DEKGVTQNGR VITANPIVTD KEKPVNIEAE PPFGESYIVV GAGEKALKLS WFKKGSTIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLVHQIF GTAYGVLFSG VSWTMKIGIG VLLTWLGLNS RSTSLSMTCI AVGLVTLYLG VMVQADSGCV INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRVEN IMWKQISNEL NHILFENDMK FTVVVGDVSG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG ADVQNSTFII DGPNTPECPD DQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQVCDHRLMS AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCVW PKSHTLWSNG VLESEMIIPK IYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG KIIHEWCCRS CTLPPLRFKG EDGCWYGMEI RPVKEKEENL VKSMVSAGLG EVDSFSLGLL CISIMIEEVM RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMIGAN ASDRMGMGTT YLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLVAS VELPNSLEEL GDGLAMGIMI LKLLTDFQSH QLWAELLSLT FIKTTCSLHY AWKTMAMVLS IVSLFPLCMS TTSQKTTWLP VLLGSLGCKP LTMFLIAENK IWGRKSWPLN EGIMAVGIVS ILLSSLLKND VPLAGPLIAG GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGASHNIL VEVQDDGTMK IKDEERDDTL TILLKATLLA VSGVYPLSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI MQRGLLGRSQ VGVGVFQENV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRL QGSWNTGEEV QVIAVEPGKN PKNVQTAPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFR KRNLTIMDLH PGSGKTRRYL PAIVREAIKR KLRTLILAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGK EIVDLMCHAT FTMRLLSPVR VPNYNMIIMD EAHFTDPSSI AARGYISTRV GMGEAAAIFM TATPPGSVEA FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVIQ LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA GPMPVTVASA AQRRGRIGRN QNKEGDQYIY MGQPLNNDED HAHWTEAKML LDNINTPEGI IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL ILEIGKLPQH LTQRAQNALD NLVMLHNSEQ GGRAYRHAME ELPDTIETLM LLALIAVLTG GVTLFFLSGR GLGKTSIGLL CVMASSVLLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ RTPQDNQLAY VVIGLLFMIL TVAANEMGLL ETTKKDLGIG HVAVENHHHA TMLDVDLHPA SAWTLYAVAT TIITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDIGVPLLA LGCYSQVNPL TLTAAVLMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT YKRSGIIEVD RSEAKEGLKR GETTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW SYYCAGLKKV TEVKGYTKGG AGHEEPIPMA TYGWNLVKLH SGKDVFFTPP EKCDTLLCDI GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVTVE PEVANLDIIG QRIENIKHEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPKAKR GTAQVMEVTA RWLWGFLSRN KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA RCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE GEGLHRLGYI LRGISKIPGG NMYADDTAGW DTRISEDDLQ NEAKITDIME PEHALLATSI FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEAQ LIRQMESEGI FSPSELETPN LAQRVLNWLE KYGVERLKRM AISGDDCVVK PIDDRFATAL TALNDMGKVR KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAEWSL RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTEN MLSVWNRVWI EENPWMEDKT HVSSWEDVPY LGKREDQWCG SLIGLTARAT WATNIQVAIN QVRRLIGNEN YLDYMTSMKR FKNDSDPEGA LW //