ID   A0A0D0AM01_9HOMO        Unreviewed;      1590 AA.
AC   A0A0D0AM01;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   30-AUG-2017, entry version 23.
DE   RecName: Full=Pentafunctional AROM polypeptide {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=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=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=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
DE              EC=1.1.1.25 {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};
GN   ORFNames=CY34DRAFT_804457 {ECO:0000313|EMBL:KIK42886.1};
OS   Suillus luteus UH-Slu-Lm8-n1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Suillineae; Suillaceae;
OC   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.,
RA   Martin F., 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.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   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       ECO:0000256|SAAS:SAAS00712173}.
CC   -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC       {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712185}.
CC   -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
CC       = 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|SAAS:SAAS00629771}.
CC   -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00629607}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC       phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC       {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712174}.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|SAAS:SAAS00712180}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629743}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712175}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712177}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629576}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712169}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712187}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629599}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
CC       family. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712186}.
CC   -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
CC       family. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712182}.
CC   -!- SIMILARITY: In the 4th section; belongs to the type-I 3-
CC       dehydroquinase family. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712184}.
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, ECO:0000256|SAAS:SAAS00712181}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_03143,
CC       ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712188}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of 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   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-HAMAP.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP.
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_00110; DHQ_synthase; 1.
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; IPR006264; EPSP_synthase.
DR   InterPro; IPR023193; EPSP_synthase_CS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008289; Pentafunct_AroM.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
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; 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|HAMAP-Rule:MF_03143,
KW   ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00756365};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00756330};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|SAAS:SAAS00629580};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629621};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
KW   ECO:0000256|SAAS:SAAS00629772};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712178};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|SAAS:SAAS00629584};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|SAAS:SAAS00629587};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
KW   ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629569};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
KW   ECO:0000256|SAAS:SAAS00712179}.
FT   DOMAIN       80    363       DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
FT   DOMAIN      417    845       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   DOMAIN     1307   1388       Shikimate_dh_N. {ECO:0000259|Pfam:
FT                                PF08501}.
FT   DOMAIN     1424   1476       Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
FT   NP_BIND      46     48       NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   NP_BIND      84     87       NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   NP_BIND     115    117       NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   NP_BIND     140    141       NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   NP_BIND     180    183       NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   NP_BIND     884    891       ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   REGION        1    389       3-dehydroquinate synthase.
FT                                {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   REGION      195    198       Substrate binding 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_03143}.
FT   REGION      269    273       Substrate binding 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_03143}.
FT   REGION     1302   1590       Shikimate dehydrogenase.
FT                                {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   ACT_SITE    265    265       Proton acceptor; for 3-dehydroquinate
FT                                synthase activity. {ECO:0000256|HAMAP-
FT                                Rule:MF_03143}.
FT   ACT_SITE    280    280       Proton acceptor; for 3-dehydroquinate
FT                                synthase activity. {ECO:0000256|HAMAP-
FT                                Rule:MF_03143}.
FT   ACT_SITE    833    833       For EPSP synthase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   ACT_SITE   1191   1191       Proton acceptor; for 3-dehydroquinate
FT                                dehydratase activity. {ECO:0000256|HAMAP-
FT                                Rule:MF_03143}.
FT   ACT_SITE   1219   1219       Schiff-base intermediate with substrate;
FT                                for 3-dehydroquinate dehydratase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   METAL       195    195       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   METAL       276    276       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   METAL       292    292       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   BINDING     120    120       NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   BINDING     131    131       Substrate 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   BINDING     147    147       Substrate 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   BINDING     153    153       Substrate 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   BINDING     162    162       NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   BINDING     163    163       Substrate 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   BINDING     191    191       NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
FT   BINDING     255    255       Substrate 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   BINDING     276    276       Substrate 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   BINDING     292    292       Substrate 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03143}.
FT   BINDING     361    361       Substrate 2. {ECO:0000256|HAMAP-Rule:
FT                                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
//