ARO1_ASPCL
ID ARO1_ASPCL Reviewed; 1587 AA.
AC A1CP85;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=SK {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143};
GN Name=aroM {ECO:0000255|HAMAP-Rule:MF_03143}; ORFNames=ACLA_021700;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC reactions in prechorismate polyaromatic amino acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
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:0000255|HAMAP-Rule:MF_03143};
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:0000255|HAMAP-
CC Rule:MF_03143};
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:0000255|HAMAP-Rule:MF_03143};
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:0000255|HAMAP-Rule:MF_03143};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03143};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC cyclases superfamily. Dehydroquinate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
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DR EMBL; DS027059; EAW07456.1; -; Genomic_DNA.
DR RefSeq; XP_001268882.1; XM_001268881.1.
DR AlphaFoldDB; A1CP85; -.
DR SMR; A1CP85; -.
DR STRING; 5057.CADACLAP00002756; -.
DR EnsemblFungi; EAW07456; EAW07456; ACLA_021700.
DR GeneID; 4701271; -.
DR KEGG; act:ACLA_021700; -.
DR VEuPathDB; FungiDB:ACLA_021700; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_001201_1_2_1; -.
DR OMA; YCYDDHR; -.
DR OrthoDB; 39786at2759; -.
DR UniPathway; UPA00053; UER00085.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR UniPathway; UPA00053; UER00088.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000006701; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 3.40.50.300; -; 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_00109; Shikimate_kinase; 1.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
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; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR010110; Shikimate_DH_AroM-type.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR023000; Shikimate_kinase_CS.
DR Pfam; PF01761; DHQ_synthase; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF00275; EPSP_synthase; 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; SSF53223; SSF53223; 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; PS01028; DEHYDROQUINASE_I; 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; Aromatic amino acid biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase; Zinc.
FT CHAIN 1..1587
FT /note="Pentafunctional AROM polypeptide"
FT /id="PRO_0000406703"
FT REGION 1..384
FT /note="3-dehydroquinate synthase"
FT REGION 397..842
FT /note="EPSP synthase"
FT REGION 864..1055
FT /note="Shikimate kinase"
FT REGION 1056..1276
FT /note="3-dehydroquinase"
FT REGION 1289..1587
FT /note="Shikimate dehydrogenase"
FT ACT_SITE 260
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 275
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 824
FT /note="For EPSP synthase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1179
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1207
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 44..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 81..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 114..116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 130
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 146
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 152
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 162
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 179..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 194..197
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 250
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 264..268
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 271
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 287
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 356
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 871..878
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
SQ SEQUENCE 1587 AA; 172279 MW; 8E85E51476FEECB7 CRC64;
MIEPTKISIL GQESIVADFG LWRNYVAKDL ISGCPSTTYV LITDTNIGSI YTPSFQKSFE
EAAAAVTPSP RLLTYYAPPG EVSKSRQTKA DIEDWMLSQS PPCGRDTVII ALGGGVIGDL
TGFVAATYMR GVRFVQVPTT LLAMVDSSIG GKTAIDTPLG KNLIGAIWQP ARIYIDLEFL
ETLPVREFIN GMAEVIKTAA ISSEEEFTAL EDNAETILAA VRREVKPGQR RFDGIEQILK
ARILASARHK AFVVSEDERE GGLRNLLNWG HSIGHAIEAI LTPQILHGEC VAIGMVKEAE
LARHLGVLKG VAVARIVKCI AAYGLPTSLK DARIRKLTAG KHCSVDQLLF NMALDKKNDG
PKKKVVLLSA IGRTYEPRAS VVANEDIGVV LAPSIEVFPG VSPKSTVICA PPGSKSISNR
ALVLAALGSG TCRIKNLLHS DDTEVMLNAL ERIGAATFSW EEEGEVLVVN GKGGALQAHP
SELYLGNAGT ASRFLTTVAT LATPSNVDFS ILTGNNRMKQ RPIGDLVEAL IANGAQVEYM
ESKGSLPLKI AASGGFTGGQ INLAAKVSSQ YVSSLLMCAP YAKEPVTLKL VGGKPISQPY
IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYTNPAEYVV ESDASSATYP LAIAAVTGTT
CTVPNIGSKS LQGDARFAVD VLRPMGCTVE QTDTSTTVTG PADGVLRPLP NVDMEPMTDA
FLGASVLAAI ARGEGSNHTT RIYGIANQRV KECNRIKAMH DELAKFGVVC REHEDGLEID
GIDRANLRQP AGGVFCYDDH RVAFSFSVLS LVAPKPTLIL EKECVGKTWP GWWDTLRLKF
AVKLEGRELK EAESPVLTSA EKASASVFII GMRGAGKTTS GHWVASTLNR PFIDLDDELE
RIEGMTIPDI IKERGWQGFR DAELSLLQRT MKERPTGHVF ACGGGVVEVP EARKLLINWH
KSKGNVLLIM RDIKQVMDFL NIDKTRPAYV EDMMGVWLRR KPWFQECSNI QYYSQHASSG
LTRASEDFAR FVKIVTGQVD SLGAIKKKQH SFFVSLTLPD LRPAGDILEQ ACVGSDAVEL
RVDLLKDPSS SNGIPSVDYV AEQMSFLRSH TTLPLIFTIR TKSQGGFFPD EAHEEAMQLY
QLAFRSGCEF VDLEIAFPDE LLRTVSEMKG YSKIIASHHD PKGELSWANM SWMKYYNRAL
EYGDVIKLVG VATKLDDNTA LRKFKSWAEE AHDVPLIAIN MGDNGQLSRI LNGFMTPVSH
PALPFKAAPG QLSATEICKG LSLMGQIKKK RFALFGTPIS ESRSPALHNS LFAELGLPHE
YTRLETANAE DVKEFIRAPD FGGASVTIPL KLDIMPLLDE IAPEAEIIGA VNTIVPVSDG
EGKPQRLVGH NTDWQGMVQC LRNAGAYGSN GDASALVVGG GGTCRAGIYA LHQMGYSPIY
IVGRNLGKLQ AMASTFPSSY NIRILEGNET LEHVPHVAIG TIPGDQPIDP GMREILCHMF
ARAEEADADA VRSIEGSPRV LLEMAYKPPV TALMQLATDA GWTTIPGLEV LVGQGFYQGG
ITQFQHWTGI RPLYEHARDA VLGTKAD
