ARO1_PARBA
ID ARO1_PARBA Reviewed; 1598 AA.
AC C1H8L1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 81.
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 ORFNames=PAAG_07102;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN294013; EEH36684.2; -; Genomic_DNA.
DR RefSeq; XP_015700561.1; XM_015846126.1.
DR AlphaFoldDB; C1H8L1; -.
DR SMR; C1H8L1; -.
DR STRING; 502779.C1H8L1; -.
DR EnsemblFungi; EEH36684; EEH36684; PAAG_07102.
DR GeneID; 9094185; -.
DR KEGG; pbl:PAAG_07102; -.
DR VEuPathDB; FungiDB:PAAG_07102; -.
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; UP000002059; Partially assembled 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..1598
FT /note="Pentafunctional AROM polypeptide"
FT /id="PRO_0000406728"
FT REGION 1..384
FT /note="3-dehydroquinate synthase"
FT REGION 397..842
FT /note="EPSP synthase"
FT REGION 867..1059
FT /note="Shikimate kinase"
FT REGION 1060..1280
FT /note="3-dehydroquinase"
FT REGION 1293..1598
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 1183
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1211
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 874..881
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
SQ SEQUENCE 1598 AA; 173890 MW; 572906F610D9AC8F CRC64;
MGVPTKISIL GRESIVADFG IWRNYVAKDL LSSCASSTYI LISDTNLTPL YLAGFQQSFE
NAAAGLSPKP RLLTYEIPPG ESSKSRETKA DIEDWMLTRQ PPCGRDTVII ALGGGVIGDL
IGFVAATYMR GVRFVQVPTT LLAMVDSSIG GKTAIDTPNG KNLIGAIWQP QRIYLDMEFL
NTLPEREFIN GMAEVIKTAA ISSEEKFAAL ENDADVILAA VKSKNTPERL RFSNIQETLK
RTILSSAEFK AQVVSADERE GGLRNLLNFG HSIGHAIEAI LAPQVLHGEC VSIGMVKEAE
LARHLGILNN VSVARIVKCL ASYELPTSLK DERIKRLTAG KHCSVEQIIA YMGVDKKNDG
PKKKVVLLSA IGRTYEPRAC TVSNEDLQVV LAPSIEVYPG FPKSLNVTCT PPGSKSISNR
ALVLAALGSG TCRIKNLLHS DDTEVMLTAL ERLGAATFSW ENQGEVLVVN GNGGRMVASP
KELYLGNAGT ASRFLTTVAT LAQNGSVASS VLTGNARMKQ RPIGDLVDAL KANGADIEYL
ENPKSLPLKI TASGGFAGGE IRLSAKVSSQ YVSSLLMCAP YAKEPVTLRL VGGNPVSQLY
IDMTTAMMRS FGIDVKKSET EEHTYHIPRG VYKNPAEYVV ESDASSATYP LAIAAMTGTS
CTVPNIGSKS LQGDARFAID VLRPMGCTVN QTDFSTSVTG PAGGKLKSIP TIDMEPMTDA
FLTASVLAAV ARGQGSNHTT RICGIANQRV KECNRIKAMK DELAKFGVTC REHDDGLEID
GIDRSTLCHP PEGVFCYDDH RVAMSFSILA LAAEQPTLIL EKECVGKTWP GWWDTLAQTF
KVKLDGKEVE VEEKAETNGV AHVDKSAASI FIIGMRGAGK TTSGVWVSKA LQRPFIDLDD
ELEKNEGMTI PEMIKQRGWE GFRDSELALL RRVMTEKPMG YIFACGGGVV ELPEARELLT
QYHKTKGNVI LAMRDIKEVM DFLKIDKTRP AYVEDMMSVW LRRKPWYQEC SNIQYYSRIT
QPDGMAQVLH GFNRFLKVIT GKLDSLAQMR RKENTFFVSL TFPDLTPASN ILKEVTLGSD
AVELRVDLLK DPQSDSEIPS VDYVAEQISV LRSRVSVPLV FTIRTKSQGG RFPDDAYDAA
LRLYCLAIRM GSEFVDLELS FPEQLLRTVT EMKGFSKIIA SHHDPEGLLS WANGSWIQIY
NKALQYGDVI KLVGVAKTLD DNASLKKFKT WAEAKHDVPL IAINMGYKGQ LSRILNGFMT
PVSHPGLPFK AAPGQLSARE IRKGLSLMGE IKAKKFAVIG KPVSSSRSPA MHNALFKQMG
LPHTYGRIET DNPEDVKEFI RSPDFGGASV TIPLKLDIMP LLDEIAPEAE MIGAVNTIVS
VPAAPGDKSQ SSRLIGRNTD WQGMVRCLSD AGAYSAATPT TSSAGLIIGG GGTARAAIFA
LNSMSYSPIY IVGRSPEKLA CMASSFPADY NIRIVDDVKA LESLPMVAIG TIPGDKPIEL
HMREVLCEIL SLCEKANVEA ERRTGITPKR ILLEMAYKPS VTSLMKLASD AGWTVLPGLE
VLVAQGVYQS EYWTDITPVY ENARKAVMGV SSSDDIIS
