ID   Q91NH1_9FLAV            Unreviewed;      3392 AA.
AC   Q91NH1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   17-JUN-2020, entry version 140.
DE   RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS01197934};
OS   Dengue virus 1.
OC   Viruses; Riboviria; 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: 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|SAAS:SAAS01122357};
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|SAAS:SAAS01122355};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.48; Evidence={ECO:0000256|SAAS:SAAS01198479};
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum
CC       {ECO:0000256|SAAS:SAAS01209087}. Host nucleus
CC       {ECO:0000256|SAAS:SAAS01249369}. Virion membrane
CC       {ECO:0000256|SAAS:SAAS01195842}; Multi-pass membrane protein
CC       {ECO:0000256|SAAS:SAAS01195842}.
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DR   EMBL; AF298808; AAK60418.1; -; Genomic_RNA.
DR   IntAct; Q91NH1; 11.
DR   MINT; Q91NH1; -.
DR   BRENDA; 3.4.21.91; 9643.
DR   Proteomes; UP000102548; Genome.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-UniRule.
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: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: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:0039503; P:suppression by virus of host innate immune response; 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; 2.60.260.50; -; 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; 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; 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:SAAS00291633};
KW   ATP-binding {ECO:0000256|SAAS:SAAS01198603};
KW   Capsid protein {ECO:0000256|SAAS:SAAS01197962};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3,
KW   ECO:0000256|SAAS:SAAS01200326};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|SAAS:SAAS01200298};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|SAAS:SAAS01200343}; Helicase {ECO:0000256|SAAS:SAAS01209034};
KW   Host endoplasmic reticulum {ECO:0000256|PROSITE-ProRule:PRU00859};
KW   Host membrane {ECO:0000256|PROSITE-ProRule:PRU00859,
KW   ECO:0000256|SAAS:SAAS00291629};
KW   Host nucleus {ECO:0000256|SAAS:SAAS01249452};
KW   Host-virus interaction {ECO:0000256|SAAS:SAAS00291630};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01198589};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|SAAS:SAAS00910833};
KW   Membrane {ECO:0000256|PROSITE-ProRule:PRU00859,
KW   ECO:0000256|SAAS:SAAS00291489, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4,
KW   ECO:0000256|SAAS:SAAS01198594};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS01198504};
KW   mRNA capping {ECO:0000256|SAAS:SAAS01198443};
KW   mRNA processing {ECO:0000256|SAAS:SAAS01198505};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS01198580};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01198562};
KW   Protease {ECO:0000256|SAAS:SAAS01200356};
KW   RNA-binding {ECO:0000256|SAAS:SAAS01198501};
KW   RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS01198530};
KW   S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS01198586};
KW   Serine protease {ECO:0000256|SAAS:SAAS01200312};
KW   Transferase {ECO:0000256|SAAS:SAAS01198537};
KW   Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00859,
KW   ECO:0000256|SAAS:SAAS00291514, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00859,
KW   ECO:0000256|SAAS:SAAS00291474, ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|SAAS:SAAS00291492};
KW   Viral immunoevasion {ECO:0000256|SAAS:SAAS00910833};
KW   Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS01200338};
KW   Viral RNA replication {ECO:0000256|SAAS:SAAS01198628};
KW   Virion {ECO:0000256|SAAS:SAAS01197947};
KW   Virus entry into host cell {ECO:0000256|SAAS:SAAS00291600};
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
//