ID   Q32ZD3_9FLAV            Unreviewed;      3405 AA.
AC   Q32ZD3;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-NOV-2024, entry version 140.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS   Sepik virus.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus sepikense.
OX   NCBI_TaxID=44026 {ECO:0000313|EMBL:AAV34159.1, ECO:0000313|Proteomes:UP000124629};
RN   [1] {ECO:0000313|EMBL:AAV34159.1, ECO:0000313|Proteomes:UP000124629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16223950; DOI=10.1128/CMR.18.4.608-637.2005;
RA   Kuno G., Chang G.J.;
RT   "Biological transmission of arboviruses: reexamination of and new insights
RT   into components, mechanisms, and unique traits as well as their
RT   evolutionary trends.";
RL   Clin. Microbiol. Rev. 18:608-637(2005).
CC   -!- FUNCTION: Component of the viral RNA replication complex that functions
CC       in virion assembly and antagonizes the host immune response.
CC       {ECO:0000256|ARBA:ARBA00024317}.
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: Required cofactor for the serine protease function of NS3.
CC       May have membrane-destabilizing activity and form viroporins.
CC       {ECO:0000256|ARBA:ARBA00035601}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); 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 + phosphate + H(+); 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   -!- SUBUNIT: Forms a heterodimer with serine protease NS3. May form
CC       homooligomers. {ECO:0000256|ARBA:ARBA00046942}.
CC   -!- SUBUNIT: Forms heterodimers with envelope protein E in the endoplasmic
CC       reticulum and Golgi. {ECO:0000256|ARBA:ARBA00035667}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with serine protease NS3.
CC       {ECO:0000256|ARBA:ARBA00025871}.
CC   -!- SUBCELLULAR LOCATION: 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}. 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; AY632543; AAV34159.1; -; Genomic_RNA.
DR   MEROPS; S07.001; -.
DR   Proteomes; UP000124629; 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:0016020; C:membrane; IEA:UniProtKB-KW.
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: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:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0052170; P:symbiont-mediated suppression of host innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:symbiont-mediated suppression 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   GO; GO:0019049; P:virus-mediated perturbation of host defense response; 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   FunFam; 3.30.70.2840:FF:000004; Genome polyprotein; 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; 3.
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; 2.40.10.10; Trypsin-like serine proteases; 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; 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-like.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; 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:ARBA00023258};
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        39..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        719..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        750..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1154..1176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1227..1245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1319..1343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1350..1371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1377..1395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1446..1473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2152..2175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2182..2198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2204..2222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2234..2251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2286..2307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1350..1479
FT                   /note="Flavivirus NS2B"
FT                   /evidence="ECO:0000259|PROSITE:PS51527"
FT   DOMAIN          1480..1659
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000259|PROSITE:PS51528"
FT   DOMAIN          1664..1820
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1815..1992
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          2500..2764
FT                   /note="MRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000259|PROSITE:PS51591"
FT   DOMAIN          3028..3180
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          1937..1958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1531
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT   ACT_SITE        1555
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT   ACT_SITE        1616
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT   BINDING         2938
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         2942
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         2947
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         2950
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         3215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         3231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         3350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
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        462..560
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT   DISULFID        577..607
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
SQ   SEQUENCE   3405 AA;  379445 MW;  B27D0C3D46A90304 CRC64;
     MATRGASKSR VTTRGVNMVT AKAKSLAVKI KNKTKQNTRG LRGFLLFLVA QIFWARKLTP
     QVKKLWRMVD KVQGLKILKK LRNIVTNLMK GLSGRRKRRS PPASIILLLL PLMAYSASVT
     RQHGAGLLLN VTFADVGKTF EVQGGNCSVN TLEAGKWCDD YVEYACVTLT EGEEPDDLDC
     WCYGVDNVRV TYGRCKGGGS RRSRRSALIT PHVDKGLTTR QEKWLPSKIG EQQLQKVEKW
     IIRNPLYALG AIALAYFIGT SVVQKVVIAI LLLGIGPAYS THCLGIPKRD FIRGLDGNTW
     VSVVLEQGGC VTLIADNKPS VDVWLSSIVV DTPTLVRKIC YESSVTGSKA EGACPTMGDA
     HLTEEGNEEW ECKRSFSDRG WGNGCGLFGK GSIVACAKFS CTKEMEVYQI DSTKIEYTIS
     AQVHSGAKKE DWVNHTKLIK FVPTTGTSTV TFTGYGNFGL ECHVQMMVDL GNSYLVKVGT
     DAWLVNKQWA HDITLPWQSG TGGHWRDKHF MVDFEQPHAV TMKALVLGSQ EGALRTALSG
     AMVVEVSSNR YTLKGGHVTC KAYMNDLTLK GSTYPMCKKG MSFVKQPVET DHGTAVMQVK
     VTNGAPCRIP VIASDSMAGT ENRGSVITTN PIAALNNDEV LVEISPPFGE SYIIVGSGDD
     KLTYHWQRSG STIGNLFTET MKGAQRMIIT GEHSWDFGST GGFFASVGKA IHTVFGTAFH
     AMFGGLSWMT KILIGGLMVW LGLNSRSSSL SMAFICLGAL LLVLATGVGA EVGCSLNWKQ
     REVKCGDGMF VFKDTDDWFT KYQYIPEDPK TMAGLIAQAH EEGLCGLNSV GDLEHRMWVS
     RVDEINAILE ENDIDLTVVV QDSASIYQRG SHAFPRPKGE LKYGWKTWGK NIIFSPSRKN
     GTFIIDGKSK SECPFNKRVW NSIKVEEFGT GIYQTRVFMR PDYDYSKLCD TGMLGAAAKG
     DASVHGDPLF WMESQNVNDT WTITSLEALN YRECEWPSSH TLDGSRVIES DMFMPRSLAG
     PVSRHNHIPG YKVQSSGPWH NTPLEVKREE CPGTHVTVEE TCDDRGKSVR STTDSGKIIP
     EWCCRSCTMP PVSFWGPDGC WYSMEVRPKH TNEGHLVKSW VVASKGDVDP FSLGLLMLFL
     CSDMFLMKRF SMRALIAGSI IMLGAMTLGS LTYLDLLRYV VTVGMYMAEA NSGGDVTHLA
     LIAVFRVRAG FVSVLALKQM WSPRERFVAA CGIVMVQIAL GDIMNTNLME WLNAAGMSIL
     VIKSIVDPRK CNVVLPLLCL LTPLTTTEIQ RAVMLFCSVV ISVTVLQTDS VSTRKSIPLI
     ALTICSFFKW TSPFLGLVCY LAFTRIPQRS WPLGETMAAV GLVGVLAGMG LKDMNGMLGP
     VAVGGVLLIV MSLSGKVDGL VIKKISDIGW DEDAEISGAS HRYDVEQTET GEFKIRNEEP
     APWTQVMILT IAIVSAAVHP ACLAVVTLGW FFWQKTATRS GVLWDIPTVV PPEEVGYLED
     GVYTINQKNV LGMAQKGVGV VKDGVFHTMW HVTRGAFLLF EGKRLTPAWA NVKEDLISYG
     GGWKLEAKWD GTEEVQLIAV APGKNPMNIQ TTPSIFQLTN GKEIGAVNLD FPSGTSGSPI
     VNKNGEVIGL YGNGILIGNN TYVSAITQSE SSLEQDNDQL QDIPNMLRKG MLTVLDFHPG
     AGKTRVYLPQ ILKECERLRL KTLVLAPTRV VLSEMKEAMP KMSIKFHTQA FSNTATGKEI
     IDAMCHATLT HRMLEPTRVT NWEVVIMDEA HFMDPASIAA RGWAAHRSRA RECATIFMSA
     TPPGTSNEFP ESNGTIEDIR KDIPSEPWTK GHEWILEDRR PTAWFLPSIR VANSIANCLR
     KAERTVVVLN RKTFEKEYPT IKSKRPDFIL ATDIAEMGAN LRVERVIDCR TAYKPFLVDD
     GTKVMVKGPL KISASSAAQR RGRVGRDPNR DTDTYVYGDS TTEDNGHYVC WTEGSMLLDN
     MEIKNGMIAP LYGIEGTKTT TVPGETRLRD EQRKVFRELV KRLDMPVWLS WHVAKAGLKV
     QDRSWCFDGE DDNTLLNDNG EPIFARSPGG GKKPLKPRWV DTRVCSDNSA LIDFIKFAEG
     RRSINGLLIG LQGFPKYLSG RMKEAVDTLT VLYNSEAGSR AYKHALAMMP EAVTIFLLIM
     LTIICTSGIV MFFLAPKGLS RMSMAMMTML VSAYLMSLGG MNPVQVSCVM LVFFIFMVVL
     IPEPGTQRST YDNQLIYLLV GVMSVILMVT ANEMGMLEKT KRDIFGTTVV EEGKKWTFPE
     LDLHPGAAWT VYVGLVTLVT PMLHHWIKVD YGNISLSGIT QNAQVLGLMD KGIPFIKMNM
     SVVILLLSAW NGITLLPLFA GMGAAALHWG FILPGLRAQA AKAAQKRVYH GVAKNPVVDG
     NPTADIDDAP GMPAMYEKKL ALIILFILAT VNLILTRTPF SIAELVVLGS AALGPLLEGN
     TNAYWNGPIA VAFTGLMRGN YYATIGLMYN GWLAKQTRRG RAAGVTLGEV WKRQLNMMGK
     QEFEKYKISD IMEVDRSVAQ RYLKEGRNDV GISVSRGTAK MRWLHERGYV KLSGRVIDLG
     CGRGGWSYYS AAQKEVMSVK GYTLGINGHE KPVHMQTLGW NIIKFKDKSD VFTMPAEPCE
     TLLCDIGESS SNFLIEKDRT LKVLENFERW KHVNTENFCV KVLCPYHPDV IEKLERMQLR
     FGGGLVRIPF SRNSTHEMYY ISGARNNITH MVNTTSRSLL RRMFRPTGKA LVESDVFLPT
     GTRSVASEAG PVDHDALQLR VDQIKHEYSK TWTIDLNHPY RTWHYLGSYL CKATGSSSSM
     LNGIVKMLSM PWDKFESVTL LAMTDTTPFG QQRVFKEKVD TRAPSPPPGT RAIMRVVNSW
     LFKHLAREMR PRICTKEEFI SKVRSHAAIG AYLEEHENWR SASEAVQDPR FWKLVDEERK
     LHLQGKCRTC VYNMMGKREK KPAEFGKAKG SRAIWYMWLG ARFLEFEALG FLNEDHWVSR
     GNSGGGVEGT GLQYLGYILK RLGEKPGGRM YADDTAGWDT RITEEDLEDE QEILKYMTKD
     HKKLAWAVTE LAYKNKVVKV MRPGPGGLTF MDIISRRDQR GSGQVVTYAL NTVTNLKVQL
     IRMAESEHVI TRHDVESVSP STLRGLEDWL ERFGTDRLSR MAVSGDDCVV KPIDDQFADA
     LYHLNAMSKI RKDIDDWKPS TGWDSWEAVP FCSHHFHEII LKDGRTIIAP CRDQDELIGR
     ARVSPGNGWM IRETACLSKA YAQMWLLMYF HRRDLRVMGN AICSAVPVDW VPTGRTTWSI
     HGKGEWMTTE NMLDVWNRVW IMENPYQADK TPVTEWRDVP YLPKSIDKTC NSLVGTTQRA
     TWARDVKHTV HRIRKLVGNE KFYDYMSTMD RYRELDEEGP GEILW
//