ID   Q91NH1_9FLAV            Unreviewed;      3392 AA.
AC   Q91NH1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   28-MAR-2018, entry version 124.
DE   RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
OS   Dengue virus 1.
OC   Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
OC   Flaviviridae; Flavivirus; Dengue virus group.
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.,
RA   de Pina J.J., de Micco P., Billoir F., Charrel R.N.,
RA   de Lamballerie X.;
RT   "Evidence for recombination in natural populations of dengue virus
RT   type 1 based on the analysis of complete genome sequences.";
RL   J. Gen. Virol. 82:1283-1290(2001).
CC   -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
CC       is required for the interferon antagonism activity of the latter.
CC       {ECO:0000256|SAAS:SAAS00892720}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {ECO:0000256|SAAS:SAAS00368577}.
CC   -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
CC       {ECO:0000256|SAAS:SAAS00368620}.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
CC       {ECO:0000256|SAAS:SAAS00251038}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
CC       5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
CC       adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
CC       triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
CC       {ECO:0000256|SAAS:SAAS00461695}.
CC   -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
CC       in which each of the Xaa can be either Arg or Lys and Yaa can be
CC       either Ser or Ala. {ECO:0000256|SAAS:SAAS00252694}.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000256|SAAS:SAAS00949449}; Peripheral membrane protein
CC       {ECO:0000256|SAAS:SAAS00949449}; Lumenal side
CC       {ECO:0000256|SAAS:SAAS00949449}. Host nucleus
CC       {ECO:0000256|SAAS:SAAS00892522}. Secreted
CC       {ECO:0000256|SAAS:SAAS00949493}. Virion membrane
CC       {ECO:0000256|SAAS:SAAS00980400}; Multi-pass membrane protein
CC       {ECO:0000256|SAAS:SAAS00980400}.
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DR   EMBL; AF298808; AAK60418.1; -; Genomic_RNA.
DR   ProteinModelPortal; Q91NH1; -.
DR   IntAct; Q91NH1; 11.
DR   MINT; Q91NH1; -.
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-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0070008; F:serine-type exopeptidase 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   CDD; cd00079; HELICc; 1.
DR   Gene3D; 1.10.10.930; -; 1.
DR   Gene3D; 1.10.8.970; -; 1.
DR   Gene3D; 1.20.1280.260; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.98.10; -; 3.
DR   Gene3D; 3.30.387.10; -; 2.
DR   Gene3D; 3.30.67.10; -; 4.
DR   InterPro; IPR011492; DEAD_Flavivir.
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; 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; 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; 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|SAAS:SAAS00445756};
KW   ATP-binding {ECO:0000256|SAAS:SAAS00969169};
KW   Capsid protein {ECO:0000256|SAAS:SAAS00969288};
KW   Complete proteome {ECO:0000313|Proteomes:UP000102548};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3,
KW   ECO:0000256|SAAS:SAAS00139753};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|SAAS:SAAS00489633};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|SAAS:SAAS00489579};
KW   Helicase {ECO:0000256|SAAS:SAAS00058020};
KW   Host endoplasmic reticulum {ECO:0000256|SAAS:SAAS00949494};
KW   Host membrane {ECO:0000256|SAAS:SAAS00445977};
KW   Host nucleus {ECO:0000256|SAAS:SAAS00892445};
KW   Host-virus interaction {ECO:0000256|SAAS:SAAS00445875};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00969059};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|SAAS:SAAS00941647};
KW   Inhibition of host interferon signaling pathway by virus
KW   {ECO:0000256|SAAS:SAAS00892563};
KW   Inhibition of host STAT2 by virus {ECO:0000256|SAAS:SAAS00892696};
KW   Membrane {ECO:0000256|SAAS:SAAS00445865, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4,
KW   ECO:0000256|SAAS:SAAS00940329};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS00817755};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00969385};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510590};
KW   Protease {ECO:0000256|SAAS:SAAS00255078};
KW   RNA-binding {ECO:0000256|SAAS:SAAS00076745};
KW   RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
KW   Secreted {ECO:0000256|SAAS:SAAS00949393};
KW   Serine protease {ECO:0000256|SAAS:SAAS00255094};
KW   Transferase {ECO:0000256|SAAS:SAAS00510371};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00445861,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00445939,
KW   ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995};
KW   Viral immunoevasion {ECO:0000256|SAAS:SAAS00941647};
KW   Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489650};
KW   Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
KW   Virion {ECO:0000256|SAAS:SAAS00445868};
KW   Virus entry into host cell {ECO:0000256|SAAS:SAAS00445755};
KW   Zinc {ECO:0000256|PIRSR:PIRSR003817-4}.
FT   TRANSMEM     46     69       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    101    118       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    724    748       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    755    773       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1124   1146       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1158   1177       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1197   1220       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1442   1469       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   2149   2168       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   2175   2192       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   2198   2215       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   2227   2244       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1346   1475       FLAVIVIRUS_NS2B. {ECO:0000259|PROSITE:
FT                                PS51527}.
FT   DOMAIN     1476   1653       Peptidase S7. {ECO:0000259|PROSITE:
FT                                PS51528}.
FT   DOMAIN     1656   1812       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN     1822   1988       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   DOMAIN     2495   2756       MRNA cap 0-1 NS5-type MT.
FT                                {ECO:0000259|PROSITE:PS51591}.
FT   DOMAIN     3020   3169       RdRp catalytic. {ECO:0000259|PROSITE:
FT                                PS50507}.
FT   ACT_SITE   1526   1526       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000256|PIRSR:
FT                                PIRSR003817-1}.
FT   ACT_SITE   1550   1550       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000256|PIRSR:
FT                                PIRSR003817-1}.
FT   ACT_SITE   1610   1610       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000256|PIRSR:
FT                                PIRSR003817-1}.
FT   METAL      2930   2930       Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
FT                                4}.
FT   METAL      2934   2934       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR003817-4}.
FT   METAL      2939   2939       Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
FT                                4}.
FT   METAL      2942   2942       Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
FT                                4}.
FT   METAL      3204   3204       Zinc 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR003817-4}.
FT   METAL      3220   3220       Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
FT                                4}.
FT   METAL      3339   3339       Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
FT                                4}.
FT   BINDING    2549   2549       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR003817-2}.
FT   BINDING    2579   2579       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR003817-
FT                                2}.
FT   BINDING    2580   2580       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR003817-
FT                                2}.
FT   BINDING    2597   2597       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR003817-2}.
FT   BINDING    2598   2598       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR003817-
FT                                2}.
FT   BINDING    2624   2624       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR003817-2}.
FT   BINDING    2625   2625       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR003817-
FT                                2}.
FT   BINDING    2711   2711       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR003817-2}.
FT   DISULFID    283    310       {ECO:0000256|PIRSR:PIRSR003817-3}.
FT   DISULFID    340    396       {ECO:0000256|PIRSR:PIRSR003817-3}.
FT   DISULFID    354    385       {ECO:0000256|PIRSR:PIRSR003817-3}.
FT   DISULFID    372    401       {ECO:0000256|PIRSR:PIRSR003817-3}.
FT   DISULFID    465    565       {ECO:0000256|PIRSR:PIRSR003817-3}.
FT   DISULFID    582    613       {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
//