ID H2BGT4_9FLAV Unreviewed; 3425 AA.
AC H2BGT4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Tembusu virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus tembusu.
OX NCBI_TaxID=64293 {ECO:0000313|EMBL:AEX15510.1, ECO:0000313|Proteomes:UP000134869};
RN [1] {ECO:0000313|Proteomes:UP000134869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22354945; DOI=10.1128/JVI.07132-11;
RA Yun T., Zhang D., Ma X., Cao Z., Chen L., Ni Z., Ye W., Yu B., Hua J.,
RA Zhang Y., Zhang C.;
RT "Complete genome sequence of a novel flavivirus, duck tembusu virus,
RT isolated from ducks and geese in china.";
RL J. Virol. 86:3406-3407(2012).
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 -!- 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=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC EC=3.4.21.91; Evidence={ECO:0000256|ARBA:ARBA00024468};
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}.
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DR EMBL; JF270480; AEX15510.1; -; Genomic_RNA.
DR Proteomes; UP000134869; 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:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent 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:0039564; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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:0046718; P:viral entry into host cell; 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; cd17931; DEXHc_viral_Ns3; 1.
DR CDD; cd12149; Flavi_E_C; 1.
DR CDD; cd17038; Flavi_M; 1.
DR CDD; cd23204; Flavivirus_RdRp; 1.
DR CDD; cd18806; SF2_C_viral; 1.
DR Gene3D; 1.10.10.930; -; 1.
DR Gene3D; 1.10.260.90; -; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.40.10.120; -; 2.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 1.10.8.970; Flavivirus envelope glycoprotein M-like; 1.
DR Gene3D; 2.60.260.50; Flavivirus polyprotein propeptide domain; 1.
DR Gene3D; 3.30.70.2840; Flavivirus RNA-directed RNA polymerase, thumb domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 3.30.67.10; Viral Envelope Glycoprotein, domain 2; 1.
DR Gene3D; 3.30.387.10; Viral Envelope Glycoprotein, domain 3; 1.
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; IPR011492; Flavi_DEAD.
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; IPR011998; Flavi_Glycoprot_E_cen/dimer.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR001850; Flavi_NS3_S7.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR046811; Flavi_NS5_thumb.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR038688; Flavi_propep_sf.
DR InterPro; IPR047530; Flavi_RdRp.
DR InterPro; IPR000208; Flavi_RdRp_fingers/palm.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR014412; Gen_Poly_FLV.
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; IPR049486; NS3-hel_C_flaviviridae.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR04240; flavi_E_stem; 1.
DR Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF21659; Flavi_E_stem; 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; PF20483; Flavi_NS5_thumb; 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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF101257; Flavivirus capsid protein C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 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 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 Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW 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 Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00022883};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW 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 740..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1139..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1172..1194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1214..1235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1302..1323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1335..1357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1369..1389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1396..1415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2171..2189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2196..2214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2220..2237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2249..2266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2304..2322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2329..2348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2368..2390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2438..2458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1368..1498
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 1499..1676
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 1679..1835
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1845..2011
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2521..2786
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 3050..3202
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT ACT_SITE 1549
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1573
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1633
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT BINDING 2960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2969
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2972
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT DISULFID 290..317
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 347..403
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 361..392
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 379..408
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 477..575
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 592..623
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
SQ SEQUENCE 3425 AA; 379901 MW; 4A1E58FD0F387E4A CRC64;
MSNKKPGRPG SGRVVNMLKR GTSRGNPLAR IKRTIDGVLR GAGPIRFVLA LLTFFKFTAL
RPTIGMLKRW KLVGVNEATK HLKSFKRDIG QMLDGLNKRK TKRRGGSCSW IIMLLPIVAG
LKLGNYNGRV LATLNKTDVS DLLVIPTTAG SNGCVVRALD VGLMCQDDIT YLCPKLEYGY
EPEDIDCWCN ETEIYIHYGR CTPSRHGRRS RRSVNVHHHG ESLLEAKNTP WMDSTKATKY
LTKVENWALR NPGYALAAIF IGWNLGTTRS QKIIFTIMLM LIAPAYSFSC LGMQNRDFVE
GVNGVEWTDV VLEGGSCVTI TAKDRPTIDV KMMNMEATEL AVVRSYCYEP KVSDVTTESR
CPTMGEAHNP KATYAEYICK KDFVDRGWGN GCGLFGKGSI QTCAKFDCTK KAEGRIVQKE
NVQFEVAVFI HGSTEASTYH NYSAQQSLKH AARFVITPKS PVYTAEMEDY GTVTLECEPR
SGVDMGQFYV FTMNTKSWLV NRDWFHDLNL PWTGSSAGTW QNKESLIEFE EAHATKQSVV
ALASQEGALH AALAGAIPVK YSGSKLEMTS GHLKCRVKMQ GLKLKGMTYP MCSNTFSLVK
NPTDTGHGTV VVELSYAGTD GPCRVPISMS ADLNDMTPVG RLITVNPYVS TSSTGAKIMV
EVEPPFGDSF ILVGSGKGQI RYQWHRSGST IGKAFTSTLK GAQRMVALGD TAWDFGSVGG
VLTSIGKGIH QVFGSAFKSL FGGMSWITQG MLGALLLWMG LNARDRSISM TFLAVGGILV
FLAVNVNADT GCSIDLARKE LKCGQGMFVF NDVEAWKDNY KYYPSTPRRL AKVVAEAHEA
GICGIRSVSR LEHNMWVSIK HELNAILEDN AIDLTVVVEE NPGRYRKTNQ RLPNVDGELM
YGWKKWGKSI FSSPKMSNNT FVIDGPKTKE CPDERRAWNS MKIEDFGFGV LSTKVWMEMR
TENTTDCDTA VMGTAIKGNR AVHSDLSYWI ESKNNGSWKL ERAVLGEVKS CTWPETHTLW
SDSVVESELI IPKTLGGPKS HHNTRTGYKV QSSGPWDEKE IVIDFDYCPG TTVTVTSSCR
DRGPSARTTT ASGKLITDWC CRSCTTPPLR FVTKSGCWYG MEIRPTAHGD DMLIKSKVMA
FQGGGMEPMQ LGMLVMIVAA QEILRRRMTA PIAWSALLLL MALVLFGGIT YSDLVKYVIL
VAAAFAESNT GGDIVHLAMV AAFNIQPGLL IGFLLRRKWS NQESRLLGVA LALITVAMRD
LNMSIPTLLN SGAMAWLLLR AVFEGTVSSF ALPLVSLLAP GLRIVGIDVV RIGVLTLGIL
SLLKERSNAM AKKKGGMLLG VACATAGIAS PLVFAGLHMV LKPVTRRGWP VSEALTAVGL
TFALAGGIAQ FDDSSMAIPL AVGGIMLVVA VVTGFSTDLW LEKASDISWS EEARVTGASQ
RFDVEIDQDG NMRLLNDPGV SLGVWAFRTG LILLSSYNPY FLPLTLAGYW MTNQGKKRGG
VIWDVPAPKE RKRAEVGNGV FRIMARGLLG KYQAGVGVMH EGVFHTMWHV TNGAVIQAGE
GTLVPYWASV RNDLISYGGP WKLGKQWNGV DEVQVIVVQP GKEVINVQTQ PGIFKTQYGE
VGAVSLDYPT GTSGSPIIDK EGQVVGLYGN GILVGSGDFV SMITQGEKKE EEVPQVFDEN
MLRKRQLTVL DLHPGSGKTR KVLPMILKSA IDKRLRTAVL APTRVVAAEI AEALKGLPIR
YLTPAVKREH TGTEIIDVMC HATLTARLLT PQRVPNYNLF IMDEAHFTDP ASIAARGYIS
TKVELGEAAA IFMTATPPGT TEAFPDSNSP ITDIEEQIPD RAWNSGYEWI TDFQGKTVWF
VPSVKSGNEI AVCLTKAGKK VIQLNRKSFD SEYPKCKSGE WDFVITTDIS EMGANFGAQR
VIDSRKCIKP VIIEDGEGSV QMNGPVPITS ASAAQRRGRV GRDVTQIGDE YHYSGPTSED
DHDFAHWKEA KILLDNINMP DGLVAQLYGP ERDKVDAIDG EFRLRTEQRK HFVEYLRTGD
LPVWISYKVA EAGISYNDRR WCFDGPSCNT VLEDNNPVEL WTKSGEKKIL KPRWRDGRLW
ADHQALKAFK DFASGKRSAI GILEVFRMLP DHFAHRMTES MDNIYMLTTA EKGSRAHREA
LEELPETLET FLLVFMMTVA SMGVFLFFVQ RRGLGKTGLG AMVMATVTVL LWIAEVPAQK
IAGVLLVSLL LMIVLIPEPE RQRSQTDSHL AVFMIVVLLV VGAVASNEMG WLEQTKKDLS
ALFGRKSDSH QETWSMPWPD LRPATAWAAY AGATTFLTPL LKHLIITEYV NFSLMAMTAQ
AGALFGLGKG MPFVKADLSV PLLLLGCWGQ FTMTTTVSAV MMVILHYAFL VPGWQAEAMR
SAQRRTAAGV MKNPVVDGIV ATDVPDLEAS TPITEKKLGQ CVLVGIALVA VFLTPNTLTL
TEFGMLTSAA SVTLIEGAAG RIWNATTAVA MCHLLRKNWL AGASLAWTIT RNLQAGTLRR
GGGTGRTLGE AWKAQLNQLT RQEFMEYRKD GIIEVDRAAA KRARREGNVT GGHPVSRGTA
KLRWLVERGF LKPRGKVVDL GCGRGGWSYY CATLKQVQEV RGYTKGGPGH EEPVMTQSYG
WNIVTLKSGV NVHFKPTEPS DTLLCDIGEA SPVPEIESAR TIRVLQMAEE WLARGVEEFC
IKVLCPYMPA VIKELERLQL KWGGGLVRVP LSRNSTHEMY WVSGSSGNVT NSINTVSQML
INRMHKTNRN GPRYEEDVDL GSGTRAVSCT RQRTDWGMVA DRVKNLAREY APSWHYDQDN
PYKTWNYHGS YEVKATGSAS SMVNGVVRIL SKPWDTLQNV VNMAMTDTTP FGQQRVFKEK
VDTKAPEPPA GTARVMNIVA RWMWNFVGRN KQPRMCTKEE FIEKVNSNAA LGAMFEEQHK
WASAREAVED PEFWSLVDRE RELHLQGKCE TCIYNMMGKR EKKMGEFGKA KGSRAIWYMW
LGARFLEFEA LGFLNEDHWM SRENTKGGVE GLGLQKLGYV LRDISAKEGG LMYADDTAGW
DTRITKADLE NEAIILEKME PMHRAVAEPL IKFAYMNKVV KVMRPGRDGK TVMDVISRED
QRGSGQVVTY ALNTFTNLCV QLIRCMEGEE LLLPEETERL KKGKEKRIQE WLQKNGENRL
SAMAVSGDDC VVKPADDRFA TALHFLNSMS KVRKDTQEWK PSTGWRNWQE VPFCSHHFHE
LQMKDGRKIV VPCRDQDELI GRARLSPGSG WSLTETACLS KAYAQMWLLM YFHRRDLRLM
ANAICSSVPV SWVPTGRTTW SIHGKGEWMT SEDMLAVWNR VWIEENEHME DKTPVTSWNE
VPYLGKREDS WCGSLIGHRA RSTWAENIYT PIMQIRALIG PEHYVDYMPT LNRFKPIESW
SEGVL
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