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Genome polyprotein

 B6VJA8_9FLAV            Unreviewed;      3392 AA.
B6VJA8;
16-DEC-2008, integrated into UniProtKB/TrEMBL.
16-DEC-2008, sequence version 1.
05-DEC-2018, entry version 87.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Dengue virus 1.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=11053 {ECO:0000313|EMBL:ACJ04302.1, ECO:0000313|Proteomes:UP000129678};
[1] {ECO:0000313|EMBL:ACJ04302.1, ECO:0000313|Proteomes:UP000126609, ECO:0000313|Proteomes:UP000129678}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-1/VN/BID-V1811/2007 {ECO:0000313|EMBL:ACL99144.1}, and
DENV-1/VN/BID-V1932/2008 {ECO:0000313|EMBL:ACJ04302.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Microbial Sequencing Center;
Genome Resources in Dengue Consortium;
Henn M.R., Young S., Kodira C., Koehrsen M., Jaffe D., Berlin A.,
Heiman D., Hepburn T., Sykes S., Borenstein D., Engels R.,
Freedman E., Gellesch M., Howarth C., Jen D., Larson L., Lewis B.,
Montgomery P., Park D., Pearson M., Richards J., Roberts A., Sisk P.,
Stolte C., White J., Zeng Q., Yandava C., Oleary S., Alvarado L.,
Alvarez P., Brockman W., Butler J., Gnerre S., Grabherr M., Kleber M.,
Mauceli E., MacCallum I., Vu H.T., Nguyen Q.H., Nguyen Q.T.,
Duong P.H., Tran H.T., Nguyen L.T.M., Nguyen L.P.H., Lander E.,
Galagan J., Nusbaum C., Simmons C.P., Birren B.;
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Proteomes:UP000101656, ECO:0000313|Proteomes:UP000107954, ECO:0000313|Proteomes:UP000119658}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-1/VN/BID-V3861/2008 {ECO:0000313|EMBL:ACY70595.1},
DENV-1/VN/BID-V3870/2008 {ECO:0000313|EMBL:ACY70604.1},
DENV-1/VN/BID-V3885/2008 {ECO:0000313|EMBL:ACY70614.1},
DENV-1/VN/BID-V3945/2008 {ECO:0000313|EMBL:ACY70636.1},
DENV-1/VN/BID-V3984/2008 {ECO:0000313|EMBL:ACY70656.1},
DENV-1/VN/BID-V4005/2008 {ECO:0000313|EMBL:ACY70668.1},
DENV-1/VN/BID-V4041/2008 {ECO:0000313|EMBL:ACY70697.1}, and
DENV-1/VN/BID-V4070/2008 {ECO:0000313|EMBL:ACY70718.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Genome Sequencing Center for Infectious Disease;
Genome Resources in Dengue Consortium;
Henn M.R., Young S., Koehrsen M., Lennon N., Erlich R., Anderson S.,
Rizzolo K., Green L., Ryan E., Yu Q., Berlin A., Heiman D.,
Hepburn T., Sykes S., Borenstein D., Engels R., Freedman E.,
Gellesch M., Heilman E., Howarth C., Jen D., Larson L., Lewis B.,
Montgomery P., Park D., Pearson M., Richards J., Roberts A., Sisk P.,
Stolte C., White J., Alvarado L., Champion M., Godfrey P., Shenoy N.,
Yandava C., Zeng Q., Vu H.T., Nguyen Q.H., Nguyen Q.T., Duong P.H.,
Simmons C.P., Wills B., Nguyen M.D., Tran V.N., Tran H.T.,
Nguyen L.T.M., Nguyen L.P.H., Nusbaum C., Birren B.;
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:AEF01516.1, ECO:0000313|Proteomes:UP000120760, ECO:0000313|Proteomes:UP000122705}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-1/VN/BID-V4045/2008 {ECO:0000313|EMBL:AEF01516.1}, and
DENV-1/VN/BID-V4079/2008 {ECO:0000313|EMBL:AEF01519.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Genome Sequencing Center for Infectious Disease;
Genome Resources in Dengue Consortium;
Henn M.R., Young S., Koehrsen M., Lennon N., Erlich R., Anderson S.,
Rizzolo K., Green L., Ryan E., Yu Q., Berlin A., Heiman D., Sykes S.,
Borenstein D., Engels R., Freedman E., Gellesch M., Heilman E.,
Howarth C., Jen D., Larson L., Neiman D., Park D., Pearson M.,
Roberts A., Sisk P., Stolte C., White J., Alvarado L., Godfrey P.,
Shenoy N., Yandava C., Zeng Q., Vu H.T., Nguyen Q.H., Nguyen Q.T.,
Duong P.H., Simmons C.P., Wills B., Nguyen M.D., Tran V.N., Tran H.T.,
Nguyen L.T.M., Nguyen L.P.H., Nusbaum C., Birren B.;
Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
Evidence={ECO:0000256|SAAS:SAAS00368577};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
Evidence={ECO:0000256|SAAS:SAAS00368620};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
ChEBI:CHEBI:83400; Evidence={ECO:0000256|SAAS:SAAS00383097};
-!- SUBCELLULAR LOCATION: Host endoplasmic reticulum
{ECO:0000256|SAAS:SAAS00941764}. Virion membrane
{ECO:0000256|SAAS:SAAS00980400}; Multi-pass membrane protein
{ECO:0000256|SAAS:SAAS00980400}.
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EMBL; FJ410260; ACJ04302.1; -; Genomic_RNA.
EMBL; FJ432742; ACL99144.1; -; Genomic_RNA.
EMBL; GU131696; ACY70595.1; -; Genomic_RNA.
EMBL; GU131705; ACY70604.1; -; Genomic_RNA.
EMBL; GU131715; ACY70614.1; -; Genomic_RNA.
EMBL; GU131737; ACY70636.1; -; Genomic_RNA.
EMBL; GU131757; ACY70656.1; -; Genomic_RNA.
EMBL; GU131769; ACY70668.1; -; Genomic_RNA.
EMBL; GU131798; ACY70697.1; -; Genomic_RNA.
EMBL; GU131819; ACY70718.1; -; Genomic_RNA.
EMBL; JF937613; AEF01516.1; -; Genomic_RNA.
EMBL; JF937616; AEF01519.1; -; Genomic_RNA.
MEROPS; S07.001; -.
Proteomes; UP000101656; Genome.
Proteomes; UP000107954; Genome.
Proteomes; UP000119658; Genome.
Proteomes; UP000120760; Genome.
Proteomes; UP000121855; Genome.
Proteomes; UP000122705; Genome.
Proteomes; UP000126609; Genome.
Proteomes; UP000129678; Genome.
Proteomes; UP000131697; Genome.
Proteomes; UP000138521; Genome.
Proteomes; UP000163901; Genome.
Proteomes; UP000165798; Genome.
GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
CDD; cd00079; HELICc; 1.
Gene3D; 1.10.10.930; -; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF101257; SSF101257; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
4: Predicted;
Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00445756};
ATP-binding {ECO:0000256|SAAS:SAAS00058020};
Capsid protein {ECO:0000256|SAAS:SAAS00969288};
Complete proteome {ECO:0000313|Proteomes:UP000101656,
ECO:0000313|Proteomes:UP000107954, ECO:0000313|Proteomes:UP000119658,
ECO:0000313|Proteomes:UP000120760};
Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3,
ECO:0000256|SAAS:SAAS00139753};
Fusion of virus membrane with host endosomal membrane
{ECO:0000256|SAAS:SAAS00489633};
Fusion of virus membrane with host membrane
{ECO:0000256|SAAS:SAAS00489633};
Helicase {ECO:0000256|SAAS:SAAS00058020};
Host membrane {ECO:0000256|SAAS:SAAS00445977};
Host-virus interaction {ECO:0000256|SAAS:SAAS00445756,
ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00941647};
Hydrolase {ECO:0000256|SAAS:SAAS00058020};
Inhibition of host innate immune response by virus
{ECO:0000256|SAAS:SAAS00941647};
Membrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAAS:SAAS00445977, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4,
ECO:0000256|SAAS:SAAS00940329};
Methyltransferase {ECO:0000256|SAAS:SAAS00817755};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00058020};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
RNA-binding {ECO:0000256|SAAS:SAAS00076745};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Transferase {ECO:0000256|SAAS:SAAS00510600,
ECO:0000256|SAAS:SAAS00817755};
Transmembrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995};
Viral immunoevasion {ECO:0000256|SAAS:SAAS00941647};
Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489633};
Viral RNA replication {ECO:0000256|SAAS:SAAS01108918};
Virion {ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00969288};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00445995,
ECO:0000256|SAAS:SAAS00489633};
Zinc {ECO:0000256|PIRSR:PIRSR003817-4}.
TRANSMEM 101 118 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 724 748 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 754 773 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1158 1177 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1201 1221 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1259 1282 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1442 1469 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2149 2168 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2175 2192 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2198 2215 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2227 2244 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1346 1475 FLAVIVIRUS_NS2B.
{ECO:0000259|PROSITE:PS51527}.
DOMAIN 1476 1653 Peptidase S7.
{ECO:0000259|PROSITE:PS51528}.
DOMAIN 1656 1812 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1822 1988 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2495 2756 MRNA cap 0-1 NS5-type MT.
{ECO:0000259|PROSITE:PS51591}.
DOMAIN 3020 3169 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
ACT_SITE 1526 1526 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1550 1550 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1610 1610 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
METAL 2930 2930 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2934 2934 Zinc 1; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 2939 2939 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2942 2942 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3204 3204 Zinc 2; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 3220 3220 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3339 3339 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
BINDING 2549 2549 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2579 2579 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2580 2580 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2597 2597 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2598 2598 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2624 2624 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2625 2625 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2711 2711 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
DISULFID 283 310 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 340 396 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 354 385 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 372 401 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 465 565 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 582 613 {ECO:0000256|PIRSR:PIRSR003817-3}.
SEQUENCE 3392 AA; 378909 MW; 24026ADFB9FED133 CRC64;
MNNQRKKTAR PSFNMLKRAR NRVSTVSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP
PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR SVTMLLMLMP TALAFHLTTR
GGEPHMIVTK QERGKSLLFK TSAGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC
WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQRVETW
ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGSRD FVEGLSGATW
VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA
TLMEEQDANF VCRRTFVDRG WGNGCGLFGK GSLITCAKFK CVTKLEGKIV QYENLKYSVI
VTVHTGDQHQ VGNESTEHGT TATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT
MKEKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM
HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV
LVQIKYEGTD APCKIPFSTQ DEKGVTQNGR LITANPIVTD KEKPVNIEAE PPFGESYIVI
GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSVGGVFT SVGKLVHQIF
GTAYGVLFSG VSWTMKIGIG VLLTWLGLNS RSTSLSMTCI AVGLVTLYLG VMVQADSGCV
INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRLEN
IMWKQISNEL NHILLENDMK FTVVVGDVVG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG
ADVQNTTFII DGPNTPECPD DQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQVCDHRLMS
AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW PKSHTLWSNG VLESEMIIPK
IYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG
KIIHEWCCRS CTLPPLRFKG EDGCWYGMEI RPVKEKEENL VKSMVSAGSG EVDSFSLGLL
CISIMIEEVM RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMVGAN ASDRMGMGTT
YLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLVAS VELPNSLEEL GDGLAMGIMI
LKLLTDFQSH QLWATLLSLT FIKTTLSLHY AWKTMAMVLS IVSLFPLCLS TTSQKTTWLP
VLLGSLGCKP LTMFLITENK IWGRKSWPLN EGIMAVGVVS 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 NSGYEWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVIQ
LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA
GPMPVTVASA AQRRGRIGRN HNKEGDQYIY 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 NQLSKSEFNI
YKRSGIMEVD RSEAKEGLKR GETTRHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW
SYYCAGLKKV TEVKGYTKGG PGHEEPIPMA TYGWNLVKLH SGKDVFFTPP EKCDTLLCDI
GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN
PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE
PEVANLDIIG QRIENIKHEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVKLL
TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPKAKR GTAQIMEVTA RWLWGFLSRN
KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVQKE RELHKQGKCA
TCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE
GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME PEHALLATSI
FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEAQ LIRQMESEGI
FLPSELETPN LAERVLDWLE KYGVERLKRM AISGDDCVVK PIDDRFATAL TALNDMGKVR
KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL
RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED
MLSVWNRVWI EENPWMEDKT HVSSWGDVPY LGKREDQWCG SLIGLTARAT WASNIQVAIN
QVRRLIGNEN YLDYMTSMKR FKNEGDPEGA LW


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