ID ARO1_EMENI Reviewed; 1583 AA.
AC P07547; C8VRD2; Q5BFH2;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-APR-2013, entry version 131.
DE RecName: Full=Pentafunctional AROM polypeptide;
DE Includes:
DE RecName: Full=3-dehydroquinate synthase;
DE Short=DHQS;
DE EC=4.2.3.4;
DE Includes:
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase;
DE EC=2.5.1.19;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase;
DE Short=EPSP synthase;
DE Short=EPSPS;
DE Includes:
DE RecName: Full=Shikimate kinase;
DE Short=SK;
DE EC=2.7.1.71;
DE Includes:
DE RecName: Full=3-dehydroquinate dehydratase;
DE Short=3-dehydroquinase;
DE EC=4.2.1.10;
DE Includes:
DE RecName: Full=Shikimate dehydrogenase;
DE EC=1.1.1.25;
GN Name=aromA; Synonyms=aroA, aroM; ORFNames=AN0708;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS 194 / M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R153;
RX PubMed=3515316; DOI=10.1093/nar/14.5.2201;
RA Charles I.G., Keyte J.W., Brammar W.J., Smith M., Hawkins A.R.;
RT "The isolation and nucleotide sequence of the complex AROM locus of
RT Aspergillus nidulans.";
RL Nucleic Acids Res. 14:2201-2213(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a
RT community effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 843-1473.
RC STRAIN=R153;
RX PubMed=3906567; DOI=10.1093/nar/13.22.8119;
RA Charles I.G., Keyte J.W., Brammar W.J., Hawkins A.R.;
RT "Nucleotide sequence encoding the biosynthetic dehydroquinase function
RT of the penta-functional arom locus of Aspergillus nidulans.";
RL Nucleic Acids Res. 13:8119-8128(1985).
RN [5]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Hawkins A.R.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION OF INTRON.
RX PubMed=8611179;
RA Lamb H.K., Moore J.D., Lakey J.H., Levett L.J., Wheeler K.A., Lago H.,
RA Coggins J.R., Hawkins A.R.;
RT "Comparative analysis of the QUTR transcription repressor protein and
RT the three C-terminal domains of the pentafunctional AROM enzyme.";
RL Biochem. J. 313:941-950(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-393 IN COMPLEX WITH NAD;
RP ZINC AND SUBSTRATE ANALOG, AND SUBUNIT.
RX PubMed=9685163; DOI=10.1038/28431;
RA Carpenter E.P., Hawkins A.R., Frost J.W., Brown K.A.;
RT "Structure of dehydroquinate synthase reveals an active site capable
RT of multistep catalysis.";
RL Nature 394:299-302(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-393 IN COMPLEX WITH ADP;
RP NAD; ZINC AND SUBSTRATE ANALOG.
RX PubMed=12614613; DOI=10.1016/S0022-2836(03)00086-X;
RA Nichols C.E., Ren J., Lamb H.K., Hawkins A.R., Stammers D.K.;
RT "Ligand-induced conformational changes and a mechanism for domain
RT closure in Aspergillus nidulans dehydroquinate synthase.";
RL J. Mol. Biol. 327:129-144(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-393.
RX PubMed=15103156; DOI=10.1107/S0907444904004743;
RA Nichols C.E., Hawkins A.R., Stammers D.K.;
RT "Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate
RT synthase at 1.7 A resolution from crystals grown following enzyme
RT turnover.";
RL Acta Crystallogr. D 60:971-973(2004).
CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC reactions in prechorismate polyaromatic amino acid biosynthesis.
CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
CC = 3-dehydroquinate + phosphate.
CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC NADPH.
CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC biosynthesis; chorismate from D-erythrose 4-phosphate and
CC phosphoenolpyruvate: step 2/7.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC biosynthesis; chorismate from D-erythrose 4-phosphate and
CC phosphoenolpyruvate: step 3/7.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC biosynthesis; chorismate from D-erythrose 4-phosphate and
CC phosphoenolpyruvate: step 4/7.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC biosynthesis; chorismate from D-erythrose 4-phosphate and
CC phosphoenolpyruvate: step 5/7.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC biosynthesis; chorismate from D-erythrose 4-phosphate and
CC phosphoenolpyruvate: step 6/7.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC dehydroquinate synthase family.
CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
CC family.
CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
CC family.
CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-
CC dehydroquinase family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC dehydrogenase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28836.1; Type=Erroneous gene model prediction;
CC Sequence=CAA28836.1; Type=Frameshift; Positions=534, 545, 708, 733, 743;
CC Sequence=EAA65484.1; Type=Erroneous gene model prediction;
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DR EMBL; X05204; CAA28836.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000010; EAA65484.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN001308; CBF88944.1; -; Genomic_DNA.
DR PIR; A24962; BVASA1.
DR RefSeq; XP_658312.1; XM_653220.1.
DR PDB; 1DQS; X-ray; 1.80 A; A/B=1-393.
DR PDB; 1NR5; X-ray; 2.10 A; A/B=1-393.
DR PDB; 1NRX; X-ray; 2.90 A; A/B=1-393.
DR PDB; 1NUA; X-ray; 2.85 A; A/B=1-393.
DR PDB; 1NVA; X-ray; 2.62 A; A/B=1-393.
DR PDB; 1NVB; X-ray; 2.70 A; A/B=1-393.
DR PDB; 1NVD; X-ray; 2.51 A; A/B=1-393.
DR PDB; 1NVE; X-ray; 2.58 A; A/B/C/D=1-393.
DR PDB; 1NVF; X-ray; 2.80 A; A/B/C=1-393.
DR PDB; 1SG6; X-ray; 1.70 A; A/B=1-393.
DR PDBsum; 1DQS; -.
DR PDBsum; 1NR5; -.
DR PDBsum; 1NRX; -.
DR PDBsum; 1NUA; -.
DR PDBsum; 1NVA; -.
DR PDBsum; 1NVB; -.
DR PDBsum; 1NVD; -.
DR PDBsum; 1NVE; -.
DR PDBsum; 1NVF; -.
DR PDBsum; 1SG6; -.
DR ProteinModelPortal; P07547; -.
DR STRING; 162425.CADANIAP00001961; -.
DR GeneID; 2876485; -.
DR KEGG; ani:AN0708.2; -.
DR eggNOG; COG0337; -.
DR HOGENOM; HOG000007970; -.
DR OrthoDB; EOG4PRWZT; -.
DR SABIO-RK; P07547; -.
DR UniPathway; UPA00053; UER00085.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR UniPathway; UPA00053; UER00088.
DR UniPathway; UPA00053; UER00089.
DR EvolutionaryTrace; P07547; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:EC.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:EC.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:EC.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:EC.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.720; -; 1.
DR Gene3D; 3.65.10.10; -; 2.
DR HAMAP; MF_03143; Pentafunct_AroM; 1; -.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016037; DHQ_synth_AroB.
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; IPR008289; Pentafunct_AroM.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR010110; Shikimate_DH_AroM-type.
DR InterPro; IPR000623; Shikimate_kinase.
DR InterPro; IPR023000; Shikimate_kinase_CS.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21090:SF1; PTHR21090:SF1; 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 PRINTS; PR01100; SHIKIMTKNASE.
DR SUPFAM; SSF55205; RNA3'_cycl/enolpyr_transf_A/B; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; ATP-binding; Complete proteome;
KW Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase;
KW Zinc.
FT CHAIN 1 1583 Pentafunctional AROM polypeptide.
FT /FTId=PRO_0000140859.
FT NP_BIND 44 46 NAD.
FT NP_BIND 81 84 NAD.
FT NP_BIND 114 116 NAD.
FT NP_BIND 139 140 NAD.
FT NP_BIND 179 182 NAD.
FT NP_BIND 870 877 ATP (By similarity).
FT REGION 1 384 3-dehydroquinate synthase.
FT REGION 194 197 Substrate binding 2.
FT REGION 264 268 Substrate binding 2.
FT REGION 397 842 EPSP synthase.
FT REGION 863 1055 Shikimate kinase.
FT REGION 1056 1276 3-dehydroquinase.
FT REGION 1289 1583 Shikimate dehydrogenase.
FT ACT_SITE 260 260 Proton acceptor; for 3-dehydroquinate
FT synthase activity.
FT ACT_SITE 275 275 Proton acceptor; for 3-dehydroquinate
FT synthase activity.
FT ACT_SITE 824 824 For EPSP synthase activity (Potential).
FT ACT_SITE 1179 1179 Proton acceptor; for 3-dehydroquinate
FT dehydratase activity (By similarity).
FT ACT_SITE 1207 1207 Schiff-base intermediate with substrate;
FT for 3-dehydroquinate dehydratase activity
FT (By similarity).
FT METAL 194 194 Zinc; catalytic.
FT METAL 271 271 Zinc; catalytic.
FT METAL 287 287 Zinc; catalytic.
FT BINDING 119 119 NAD.
FT BINDING 130 130 Substrate 1.
FT BINDING 146 146 Substrate 2.
FT BINDING 152 152 Substrate 2.
FT BINDING 161 161 NAD.
FT BINDING 162 162 Substrate 2.
FT BINDING 190 190 NAD.
FT BINDING 250 250 Substrate 2.
FT BINDING 271 271 Substrate 2.
FT BINDING 287 287 Substrate 2.
FT BINDING 356 356 Substrate 2.
FT CONFLICT 62 62 A -> R (in Ref. 1; CAA28836).
FT CONFLICT 77 77 A -> R (in Ref. 1; CAA28836).
FT CONFLICT 226 226 R -> T (in Ref. 1; CAA28836).
FT CONFLICT 235 235 I -> T (in Ref. 1; CAA28836).
FT CONFLICT 403 403 Q -> H (in Ref. 1; CAA28836).
FT CONFLICT 535 535 A -> P (in Ref. 1; CAA28836).
FT CONFLICT 646 646 S -> C (in Ref. 1; CAA28836).
FT CONFLICT 862 862 A -> G (in Ref. 1; CAA28836 and 4; no
FT nucleotide entry).
FT CONFLICT 984 984 T -> S (in Ref. 1; CAA28836 and 4; no
FT nucleotide entry).
FT CONFLICT 1048 1048 K -> G (in Ref. 4; no nucleotide entry).
FT CONFLICT 1093 1093 D -> N (in Ref. 4; no nucleotide entry).
FT CONFLICT 1154 1154 E -> D (in Ref. 1; CAA28836 and 4; no
FT nucleotide entry).
FT CONFLICT 1345 1349 SVTIP -> FRNNS (in Ref. 1; CAA28836).
FT STRAND 5 9
FT STRAND 12 18
FT HELIX 21 24
FT HELIX 26 33
FT STRAND 37 44
FT HELIX 45 65
FT STRAND 66 68
FT STRAND 71 77
FT HELIX 81 83
FT HELIX 86 97
FT STRAND 99 101
FT STRAND 108 114
FT HELIX 115 127
FT HELIX 128 130
FT STRAND 133 138
FT HELIX 141 145
FT TURN 146 148
FT STRAND 152 157
FT STRAND 160 167
FT STRAND 171 176
FT HELIX 177 181
FT HELIX 185 200
FT HELIX 204 222
FT STRAND 227 229
FT HELIX 233 235
FT HELIX 236 255
FT TURN 257 259
FT HELIX 263 268
FT HELIX 271 281
FT TURN 282 284
FT HELIX 287 304
FT HELIX 310 322
FT HELIX 332 337
FT TURN 338 340
FT HELIX 345 353
FT STRAND 362 365
FT STRAND 368 370
FT STRAND 373 378
FT STRAND 380 383
FT HELIX 384 390
SQ SEQUENCE 1583 AA; 172664 MW; FBC8610B961840D8 CRC64;
MSNPTKISIL GRESIIADFG LWRNYVAKDL ISDCSSTTYV LVTDTNIGSI YTPSFEEAFR
KAAAEITPSP RLLIYNAPPG EVSKSRQTKA DIEDWMLSQN PPCGRDTVVI ALGGGVIGDL
TGFVASTYMR GVRYVQVPTT LLAMVDSSIG GKTAIDTPLG KNLIGAIWQP TKIYIDLEFL
ETLPVREFIN GMAEVIKTAA ISSEEEFTAL EENAETILKA VRREVRPGEH RFEGIEEILK
ARILASARHK AYVVSADERE GGLRNLLNWG HSIGHAIEAI LTPQILHGEC VAIGMVKEAE
LARHLGILKG VAVSRIVKCL AAYGLPTSLK DARIRKLTAG KHCSVDQLMF NMALDKKNDG
PKKKIVLLSA IGTPYETRAS VVANEDIRVV LAPSIEVHPG VAQSSNVICA PPGSKSISNR
ALVLAALGSG TCRIKNLLHS DDTEVMLNAL ERLGAATFSW EEEGEVLVVN GKGGNLQASS
SPLYLGNAGT ASRFLTTVAT LANSSTVDSS VLTGNNRMKQ RPIGDLVDAL TANGASIEYV
ERTGSLPLKI AASGGFAGGN INLAAKVSSQ YVSSLLMCAP YAKEPVTLRL VGGKPISQPY
IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYVNPAEYVI ESDASSATYP LAVAAVTGTT
CTVPNIGSAS LQGDARFAVE VLRPMGCTVE QTETSTTVTG PSDGILRPLP NVDMEPMTDA
FLGASVLAAI ARGKESNHTT RIYGIANQRV KECNRIKAMK DELAKFGVIC REHDDGLEID
GIDRSNLRQP VGGVFCYDDH RVAFSFSVLS LVTPQPTLIL EKECVGKTWP GWWDTLRQLF
KVKLEGKELE EEPVAASGPD RANASIYIIG MRGAGKSTAG NWVSKALNRP FVDLDTELET
VEGMTIPDII KTRGWQGFRN AELEILKRTL KERSRGYVFA CGGGVVEMPE ARKLLTDYHK
TKGNVLLLMR DIKKIMDFLS IDKTRPAYVE DMMGVWLRRK PWFQECSNIQ YYSRDASPSG
LARASEDFNR FLQVATGQID SLSIIKEKEH SFFASLTLPD LREAGDILEE VCVGSDAVEL
RVDLLKDPAS NNDIPSVDYV VEQLSFLRSR VTLPIIFTIR TQSQGGRFPD NAHDAALELY
RLAFRSGCEF VDLEIAFPED MLRAVTEMKG FSKIIASHHD PKGELSWANM SWIKFYNKAL
EYGDIIKLVG VARNIDDNTA LRKFKNWAAE AHDVPLIAIN MGDQGQLSRI LNGFMTPVSH
PSLPFKAAPG QLSATEIRKG LSLMGEIKPK KFAIFGSPIS QSRSPALHNT LFAQVGLPHN
YTRLETTNAQ DVQEFIRSPD FGGASVTIPL KLDIMPLLDE VAAEAEIIGA VNTIIPVSTG
KNTPSRLVGR NTDWQGMILS LRKAGVYGPK RKDQEQSALV VGGGGTARAA IYALHNMGYS
PIYIVGRTPS KLENMVSTFP SSYNIRIVES PSSFESVPHV AIGTIPADQP IDPTMRETLC
HMFERAQEAD AEAVKAIEHA PRILLEMAYK PQVTALMRLA SDSGWKTIPG LEVLVGQGWY
QFKYWTGISP LYESARACSS PLI
//
