ID   A0A0D0AM01_9AGAM        Unreviewed;      1590 AA.
AC   A0A0D0AM01;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   07-APR-2021, entry version 46.
DE   RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              Short=DHQS {ECO:0000256|HAMAP-Rule:MF_03143};
DE              EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_03143};
DE     AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              Short=SK {ECO:0000256|HAMAP-Rule:MF_03143};
DE              EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
GN   ORFNames=CY34DRAFT_804457 {ECO:0000313|EMBL:KIK42886.1};
OS   Suillus luteus UH-Slu-Lm8-n1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX   NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485};
RN   [1] {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK42886.1,
RC   ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RA   Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA   Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA   LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA   Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC       reactions in prechorismate polyaromatic amino acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC         carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:145989; EC=2.5.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00001901, ECO:0000256|HAMAP-
CC         Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC         dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
CC         ECO:0000256|PIRNR:PIRNR000514};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC         Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC         EC=2.7.1.71; Evidence={ECO:0000256|ARBA:ARBA00000172,
CC         ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00001648, ECO:0000256|HAMAP-
CC         Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
CC         ECO:0000256|PIRNR:PIRNR000514};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       2/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7. {ECO:0000256|ARBA:ARBA00004871, ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       5/7. {ECO:0000256|ARBA:ARBA00004842, ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       6/7. {ECO:0000256|ARBA:ARBA00004811, ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|ARBA:ARBA00009948}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase
CC       family. {ECO:0000256|ARBA:ARBA00006477}.
CC   -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC       family. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC       dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the dehydroquinate
CC       synthase family. {ECO:0000256|PIRNR:PIRNR000514}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase
CC       family. {ECO:0000256|ARBA:ARBA00009349}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC       cyclases superfamily. Dehydroquinate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03143}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}.
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DR   EMBL; KN835227; KIK42886.1; -; Genomic_DNA.
DR   EnsemblFungi; KIK42886; KIK42886; CY34DRAFT_804457.
DR   HOGENOM; CLU_001201_1_2_1; -.
DR   OrthoDB; 39786at2759; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000054485; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00502; DHQase_I; 1.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   CDD; cd00464; SK; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   HAMAP; MF_03143; Pentafunct_AroM; 1.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR006264; EPSP_synthase.
DR   InterPro; IPR023193; EPSP_synthase_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008289; Pentafunct_AroM.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR010110; Shikimate_DH_AroM-type.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
DR   InterPro; IPR023000; Shikimate_kinase_CS.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PIRSF; PIRSF000514; Pentafunct_AroM; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01356; aroA; 1.
DR   TIGRFAMs; TIGR01357; aroB; 1.
DR   TIGRFAMs; TIGR01093; aroD; 1.
DR   TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_03143};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_03143};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_03143};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03143};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03143};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03143};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03143};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_03143};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03143};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03143};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03143}; Reference proteome {ECO:0000313|Proteomes:UP000054485};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03143};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03143}.
FT   DOMAIN          80..363
FT                   /note="DHQ_synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
FT   DOMAIN          417..845
FT                   /note="EPSP_synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   DOMAIN          1307..1388
FT                   /note="Shikimate_dh_N"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          1424..1476
FT                   /note="Shikimate_DH"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          1553..1582
FT                   /note="SDH_C"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   NP_BIND         46..48
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   NP_BIND         84..87
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   NP_BIND         115..117
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   NP_BIND         140..141
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   NP_BIND         180..183
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   NP_BIND         884..891
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   REGION          1..389
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   REGION          195..198
FT                   /note="Substrate binding 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   REGION          269..273
FT                   /note="Substrate binding 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   REGION          1302..1590
FT                   /note="Shikimate dehydrogenase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        265
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        280
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        833
FT                   /note="For EPSP synthase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1191
FT                   /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT                   activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1219
FT                   /note="Schiff-base intermediate with substrate; for 3-
FT                   dehydroquinate dehydratase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   METAL           195
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   METAL           276
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   METAL           292
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         120
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         131
FT                   /note="Substrate 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         147
FT                   /note="Substrate 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         153
FT                   /note="Substrate 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         162
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         163
FT                   /note="Substrate 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         191
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         255
FT                   /note="Substrate 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         276
FT                   /note="Substrate 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         292
FT                   /note="Substrate 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         361
FT                   /note="Substrate 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
SQ   SEQUENCE   1590 AA;  170223 MW;  EF30A9B7658682A2 CRC64;
     MDTVPDILKV SILGRESIHC GFHLIPYIAH TVLTTLPASV YVLVTDTNVA QFYLSAFEKA
     FSAEISKLSS AKPRFLSRVI FPGETTKSRE GKADIEDFLL LERCTRDTVI LALGGGVIGD
     LVGFVAATFM RGVRFVQIPT TLLAMVDSSV GGKTAIDTPA GKNLIGAFWQ PEYIFIDAAF
     LESLPEREFS NGMAEVVKTA AIWDETEFTS LESNAQLIYN AIRTPSTGNA GRHISTRSTS
     QSLLLSVIRG SIYVKSHIVT IDERETGLRN LVNFGHTIGH AIEAVLTPHM LHGECVSIGM
     IFEAEVSRAM GILKQVAVGR LVRCLRAYGL PVSLADQRVT RCPGARGLGV DRLLDIMRVD
     KKNSGPQKKV VILSSIGATY EQKATAVDDA LIAKVLSEAV TVKVDLSTTS GIQHVKMATP
     GSKSISNRAL VLAALAQGTC RLKNLLHSDD TQVMMAALQE LKGASFAWED GGETLVVTGG
     AGSLEVPTAG KEIYLGNAGT AARFLTTVCS LVSPSAAPDA GTATIITGNA RMKQRPIGPL
     VDALRANGSE ITYNESEGCL PLSIAPKGLQ GGVIRLAASV SSQYVSSILL CAPYAREAVT
     LELVGGAVIS QPYIDMTIAM MRTFGVLVTR DPGTDVYRIP QGTYVNPAQY AIESDASSAT
     YPLAIAAITG TKCTLENIGS ESLQGDARFA VDVLARMGCE VVQTANETTV TGPKRGELKA
     IGEVDMEPMT DAFLTACALA AVAQGGEGNT TRILGIANQR VKECNRIKAM IDQLAKFGVQ
     TKELDDGLEV YGCPFNTLTR GASVHCYDDH RVAMAFSVLG TVVPDTIIEE KRCVEKTWPN
     WWDDLENKIG LKVGGIELPR AEGSNTATSG TPSPAASASV ILIGMRGSGK SHIGKLASAA
     LSRQFIDADI YFETKHNIGV REFVSVNGWP AFRAAETELL KEIIQKAGTG HVISMGGGIV
     ETPQARDVLK DYAKTGPVVH VLRDIEEIVN YLGDETARPA YGEPITEVFK RREPWFIECA
     NYDFVNHITV GDSEATNSEI SRFFKHITGQ PNLSENVAAG KRSYFVALTY PDVIPALRHM
     SDLTTGVDAV ELRVDLLRAH NALGAIPSQA YVTAQLAALR RATSLPIIFT VRTISQGGAF
     PDNSERDAFE LLALALRLGV EYIDVEISAS ERLITELAAR KGFSQIIASW HDWSGKMKWN
     EDVVRSKYTL ASRFGDIVKI VGKADTLQDN FVLHDFVAKA NLQRGAKPII AINMGVEGQM
     SRILNATLSP VTHPLLPSKA APGQLSFAQI QKALNLLGQL PAKRYFLFGN PIAHSMSPTL
     HNTGFEVLGL PHTYELLETA SVGEELKATL AAPDFGGASV TIPFKLDVIP LLDKLSPAAE
     AIGAVNTIIP VIEEGNRILY GDNTDWLGIR ESIRSRAPSI GAPAAALVIG AGGTARAAIF
     ALQSLGAQRI YLFNRTASKA QALVDAFPDA PVKLIETLDV WPAEGPAPTV IVSTVPASAT
     TTDGTSPGAV LLPLALFDAT ANGVVVDMAY KPAETPLLTL AKSAAPKWAR VMGVEVLLEQ
     GYVQFETWTG RRCPKHVVSK SVLEKYFAAA
//