ID   A0A1V0E2C5_ZIKV         Unreviewed;      3423 AA.
AC   A0A1V0E2C5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-APR-2020, entry version 23.
DE   RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS01197934};
DE   Flags: Precursor;
OS   Zika virus (ZIKV).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=64320 {ECO:0000313|EMBL:ARB07927.1};
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH   NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1] {ECO:0000313|EMBL:ARB07927.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Zika virus/H.sapiens-wt/DOM/2016/BB-0115-URI
RC   {ECO:0000313|EMBL:ARB07927.1};
RX   PubMed=28538734; DOI=10.1038/nature22402;
RA   Metsky H.C., Matranga C.B., Wohl S., Schaffner S.F., Freije C.A.,
RA   Winnicki S.M., West K., Qu J., Baniecki M.L., Gladden-Young A., Lin A.E.,
RA   Tomkins-Tinch C.H., Ye S.H., Park D.J., Luo C.Y., Barnes K.G., Shah R.R.,
RA   Chak B., Barbosa-Lima G., Delatorre E., Vieira Y.R., Paul L.M., Tan A.L.,
RA   Barcellona C.M., Porcelli M.C., Vasquez C., Cannons A.C., Cone M.R.,
RA   Hogan K.N., Kopp E.W., Anzinger J.J., Garcia K.F., Parham L.A.,
RA   Ramirez R.M.G., Montoya M.C.M., Rojas D.P., Brown C.M., Hennigan S.,
RA   Sabina B., Scotland S., Gangavarapu K., Grubaugh N.D., Oliveira G.,
RA   Robles-Sikisaka R., Rambaut A., Gehrke L., Smole S., Halloran M.E.,
RA   Villar L., Mattar S., Lorenzana I., Cerbino-Neto J., Valim C., Degrave W.,
RA   Bozza P.T., Gnirke A., Andersen K.G., Isern S., Michael S.F., Bozza F.A.,
RA   Souza T.M.L., Bosch I., Yozwiak N.L., MacInnis B.L., Sabeti P.C.;
RT   "Zika virus evolution and spread in the Americas.";
RL   Nature 546:411-415(2017).
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; KY785415; ARB07927.1; -; Genomic_RNA.
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: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        746..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        773..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1178..1197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1273..1290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1343..1366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1378..1394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1400..1417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1473..1496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2174..2192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2199..2216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2222..2241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2253..2275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2306..2327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2334..2353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2373..2392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2442..2462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1373..1502
FT                   /note="FLAVIVIRUS_NS2B"
FT                   /evidence="ECO:0000259|PROSITE:PS51527"
FT   DOMAIN          1503..1680
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000259|PROSITE:PS51528"
FT   DOMAIN          1683..1839
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1850..2013
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          2521..2785
FT                   /note="MRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000259|PROSITE:PS51591"
FT   DOMAIN          3049..3199
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          1425..1464
FT                   /note="Interacts with and activates NS3 protease"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00859"
FT   ACT_SITE        1553
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT   ACT_SITE        1577
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT   ACT_SITE        1637
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT   METAL           2959
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   METAL           2963
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   METAL           2968
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   METAL           2971
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   METAL           3234
FT                   /note="Zinc 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   METAL           3250
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   METAL           3369
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         2576
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT   BINDING         2606
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT   BINDING         2607
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         2651
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT   BINDING         2652
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT   BINDING         2740
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT   DISULFID        293..320
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT   DISULFID        350..406
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT   DISULFID        364..395
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT   DISULFID        382..411
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT   DISULFID        480..581
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT   DISULFID        598..629
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
SQ   SEQUENCE   3423 AA;  378780 MW;  F88B5799C4F823AE CRC64;
     MKNPKKKSGG FRIVNMLKRG VARVSPFGGL KRLPAGLLLG HGPIRMVLAI LAFLRFTAIK
     PSLGLINRWG SVGKKEAMEI IKKFKKDLAA MLRIINARKE KKRRGADTSV GIVGLLLTTA
     MAAEVTRRGS AYYMYLDRND AGEAISFPTT LGMNKCYIQI MDLGHMCDAT MSYECPXLDE
     GVEPDDVDCW CNTTSTWVVY GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY
     TKHLIRVENW IFRNPGFALA AAAIAWLLGS STSQKVIYLV MILLIAPAYS IRCIGVSNRD
     FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS
     DSRCPTQGEA YLDKQSDTQY VCKRTLVDRG WGNGCGLFGK GSLVTCAKFA CSKKMTGKSI
     QPENLEYRIM LSVHGSQHSG MIVNDTGHET DENRAKVEIT PNSPRAEATL GGFGSLGLDC
     EPRTGLDFSD LYYLTMNNKH WLVHKEWFHD IPLPWHAGAD TGTPHWNNKE ALVEFKDAHA
     KRQTVVVLGS QEGAVHTALA GALEAEMDGA KGRLSSGHLK CRLKMDKLRL KGVSYSLCTA
     AFTFTKIPAE TLHGTVTVEV QYAGTDGPCK VPAQMAVDMQ TLTPVGRLIT ANPVITESTE
     NSKMMLELDP PFGDSYIVIG VGEKKITHHW HRSGSTIGKA FEATVRGAKR MAVLGDTAWD
     FGSVGGALNS LGKGIHQIFG AAFKSLFGGM SWFSQILIGT LLMWLGLNTK NGSISLMCLA
     LGGVLIFLST AVSADVGCSV DFSKKETRCG TGVFVYNDVE AWRDRYKYHP DSPRRLAAAV
     KQAWEDGICG ISSVSRMENI MXRSVEGELN AILEENGVQL TVVVGSVKNP MWRGPQRLPV
     PVNELPHGWK AWGKSYFVRA AKTNNSFVVD GDTLKECPLK HRAWNSFLVE DHGFGVFHTS
     VWLKVREDYS LXCDPAVIGT AVKGKEAVHS DLGYWIESEK NDTWRLKRAH LIEMKTCEWP
     KSHTLWTDGI EESDLIIPKS LAGPLSHHNT REGYRTQMKG PWHSEELEIR FEECPGTKVH
     VEETCGTRGP SLRSTTASGR VIEEWCCREC TMPPLSFRAK DGCWYGMEIR PRKEPESNLV
     RSVVTAGSTD HMDHFSLGVL VILLMVQEGL KKRMTTKIII STSMAVLVAM ILGGFSMSDL
     AKLAILMGAT FAEMNTGGDV AHLALIAAFK VRPALLVSFI FRANWTPRES MLLALASCLL
     QTAISALEGD LMVLINGFAL AWLAIRAMVV PRTDNITLAI LAALTPLARG TLLVAWRAGL
     ATCGGFMLLS LKGKGSVKKN LPFVMALGLT AVRLVDPINV VGLLLLTRSG KRSWPPSEVL
     TAVGLICALA GGFAKADIEM AGPMAAVGLL IVSYVVSGKS VDMYIERAGD ITWEKDAEVT
     GNSPRLDVAL DESGDFSLVE DDGPPMREII LKVVLMTICG MNPIAIPFAA GAWYVYVKTG
     KRSGALWDVP APKEAKKGET TDGVYRVMTR RLLGSTQVGV GVMQEGXFHT MWHXTKGSAL
     RSGEGRLDPY WGDVKQDLVS YCGPWKLDAA WDGHSEVQLL AVPPGERARN IQTLPGIFKT
     KDGDIGAVAL DYPAGTSGSP ILDKCGRVIG LYGNGVVIKN GSYVSAITQG RREEETPVEC
     FEPSMLKKKQ LTVLDLHPGA GKTRRVLPEI VREAIKTRLR TVILAPTRVV AAEMEEALRG
     LPVRYMTTAV NVTHSGTEIV DLMCHATFTS RLLQPIRVPN YNLYIMDEAH FTDPSSIAAR
     GYISTRVEMG EAAAIFMTAT PPGTRDAFPD SNSPIMDTEV EXPERAWSSG FDWVTDHSGK
     TVWFVPSVRN GNEIAACLTK AGKRVIQLSR KTFETEFQKT KHQEWDFVVT TDISEMGANF
     KADRVIDSRR CLKPVILDGE RVILAGPMPV THASAAQRRG RIGRNPNKPG DEYLYGGGCA
     ETDEDHAHWL EARMLLDNIY LQDGLIASLY RPEADKVAAI EGEFKLRTEQ RKTFVELXKR
     GDLPVWLAYQ VASAGITYTD RRWCFDGTTN NTIMEDSVPA EVWTRHGEKR VLKPRWMDAR
     VCSDHAALKS FKEFAAGKRG AAFGVMEALG TLPGHMTERF QEAIDNLAVL MRAETGSRPY
     KAAAAQLPET LETIMLLGLL GTVSLGIFFV LMRNKGIGKM GFGMVTLGAS AWLMWLSEIE
     PARIACVLIV VFLLLVVLIP EPEKQRSPQD NQMAIIIMVA VGLLGLITAN ELGWLERTKS
     DLSHLMGRRE EGATIGFSMD IDLRPASAWA IYAALTTFIT PAVQHAVTTS YNNYSLMAMA
     TQAGVLFGMG KGMPFYAWDF GVPLLMIGCY SQLTPLTLIV AIILLVAHYM YLIPGLQAAA
     ARAAQKRTAA GIMKNPVVDG IVVTDIDTMT IDPQVEKKMG QVLLIAVAVS SXILSRTAWG
     WGEAGALITA ATSTLWEGSP NKYWNSSTAT SLCNIFRGSY LAGASLIYTV TRNAGLVKRR
     GGGTGETLGE KWKARLNQMS ALEFYSYKKS GITEVCREEA RRALKDGVAT GGHAVSRGSA
     KLRWLVERGY LQPYGKVIDL GCGRGGWSYY AATIRKVQEV KGYTKGGPGH EEPVLVQSYG
     WNIVRLKSGV DVFHMAAEPC DTLLCDIGES SSSPEVEXAR TLRVLSMVGD WLEKRPGAFC
     IKVLCPYTST MMETLERLQR RYGGGLVRVP LSRNSTHEMY WVSGAKSNTI KSVSTTSQLL
     LGRMDGPRRP VKYEEDVNLG SGTRAVVSCA EAPNMKIIGN RIERIRSEHA ETWFFDENHP
     YRTWAYHGSY EAPTQGSASS LVNGVVRLLS KPWDVVTGVT GIAMTDTTPY GQQRVFKEKV
     DTRVPDPQEG TRQVMSMVSS WLWQELGKHK RPRVCTKEEF INKVRSNAAL GAIFEXEKEW
     KTAVEAVNDP RFWALVDKER EHHLRGECQS CVYNMMGKRE KKQGEFGKAK GSRAIWYMWL
     GARFLEFEAL GFLNEDHWMG RENSGGGVEG LGLQRLGYVL EEMSRIPGGR MYADDTAGWD
     TRISRFDLEN EALITNQMEK GHRALALAII KYTYQNKVVK VLRPAEKGKT VMDIISRQDQ
     RGSGQVVTYA LNTFTNLVVQ LIRNMEAEEV LEMQDLXLLR RSEKVTNXLQ SNGWDRLKRM
     AVSGDDCVVK PIDDRFAHAL RFLNDMGKVR KDTQEWKPST GWDNWEEVPF CSHHFNKLHL
     KDGRSIVVPC RHQDELIGRA RVSPGAGWSI RETACLAKSY AQMWQLLYFH RRDLRLMANA
     ICSSVPVDWV PTGRTTWSIH GKGEWMTTED MLVVWNRVWI EENDHMEDKT PVTKWTDIPY
     LGKREDLWCG SLIGHRPRTT WAENIKNTVN MVRRIIGEEE KYMDYLSTQV RYLGEEGSTP
     GVL
//