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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); Shikimate dehydrogenase (EC 1.1.1.25)]

 I1RK93_GIBZE            Unreviewed;      1568 AA.
I1RK93;
13-JUN-2012, integrated into UniProtKB/TrEMBL.
13-JUN-2012, sequence version 1.
22-NOV-2017, entry version 55.
RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_03143};
AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=DHQS {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=SK {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
Name=FG04287.1 {ECO:0000313|EnsemblFungi:CEF79264};
ORFNames=FGRAMPH1_01T14925 {ECO:0000313|EMBL:CEF79264.1};
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084)
(Wheat head blight fungus) (Fusarium graminearum).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
Fusarium.
NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF79264.1, ECO:0000313|Proteomes:UP000070720};
[1] {ECO:0000313|EnsemblFungi:CEF79264, ECO:0000313|Proteomes:UP000070720}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
{ECO:0000313|EnsemblFungi:CEF79264,
ECO:0000313|Proteomes:UP000070720};
PubMed=17823352; DOI=10.1126/science.1143708;
Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
"The Fusarium graminearum genome reveals a link between localized
polymorphism and pathogen specialization.";
Science 317:1400-1402(2007).
[2] {ECO:0000313|EnsemblFungi:CEF79264, ECO:0000313|Proteomes:UP000070720}
GENOME REANNOTATION.
STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
{ECO:0000313|EnsemblFungi:CEF79264,
ECO:0000313|Proteomes:UP000070720};
PubMed=20237561; DOI=10.1038/nature08850;
Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J.,
Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M.,
Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C.,
Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A.,
Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M.,
Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S.,
Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K.,
Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M.,
Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y.,
Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S.,
Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O.,
Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C.,
Rep M.;
"Comparative genomics reveals mobile pathogenicity chromosomes in
Fusarium.";
Nature 464:367-373(2010).
[3]
NUCLEOTIDE SEQUENCE.
STRAIN=PH-1;
King R., Urban M., Hassani-Pak K., Hammond-Kosack K.;
"A revised Fusarium graminearum genomic reference sequence using whole
shotgun re-sequencing.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:CEF79264.1, ECO:0000313|Proteomes:UP000070720}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PH-1 {ECO:0000313|EMBL:CEF79264.1}, and
PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
{ECO:0000313|Proteomes:UP000070720};
PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
Hammond-Kosack K.E.;
"The completed genome sequence of the pathogenic ascomycete fungus
Fusarium graminearum.";
BMC Genomics 16:544-544(2015).
[5] {ECO:0000313|EnsemblFungi:CEF79264}
IDENTIFICATION.
STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
{ECO:0000313|EnsemblFungi:CEF79264};
EnsemblFungi;
Submitted (JAN-2017) to UniProtKB.
-!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
reactions in prechorismate polyaromatic amino acid biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712173}.
-!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712185}.
-!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
= 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00858949}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00629607}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712174}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712180}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858971}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712175}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712177}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629576}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712169}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712187}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629599}.
-!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712186}.
-!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712182}.
-!- SIMILARITY: In the 4th section; belongs to the type-I 3-
dehydroquinase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712184}.
-!- SIMILARITY: In the C-terminal section; belongs to the shikimate
dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712181}.
-!- SIMILARITY: In the N-terminal section; belongs to the
dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514}.
-!- SIMILARITY: In the N-terminal section; belongs to the sugar
phosphate cyclases superfamily. Dehydroquinate synthase family.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00858969}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}.
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EMBL; HG970333; CEF79264.1; -; Genomic_DNA.
RefSeq; XP_011321330.1; XM_011323028.1.
STRING; 229533.XP_384463.1; -.
EnsemblFungi; CEF79264; CEF79264; FGRRES_04287.
GeneID; 23551545; -.
KEGG; fgr:FGSG_04287; -.
EuPathDB; FungiDB:FGRAMPH1_01G14925; -.
eggNOG; KOG0692; Eukaryota.
eggNOG; COG0128; LUCA.
eggNOG; COG0169; LUCA.
eggNOG; COG0337; LUCA.
eggNOG; COG0703; LUCA.
eggNOG; COG0710; LUCA.
KO; K13830; -.
OrthoDB; EOG092C02JU; -.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000070720; Chromosome 2.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00502; DHQase_I; 1.
CDD; cd01556; EPSP_synthase; 1.
CDD; cd00464; SK; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.65.10.10; -; 2.
HAMAP; MF_00110; DHQ_synthase; 1.
HAMAP; MF_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR018508; 3-dehydroquinate_DH_AS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR016037; DHQ_synth_AroB.
InterPro; IPR030960; DHQS/DOIS.
InterPro; IPR001381; DHquinase_I.
InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
InterPro; IPR006264; EPSP_synthase.
InterPro; IPR023193; EPSP_synthase_CS.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008289; Pentafunct_AroM.
InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
InterPro; IPR031322; Shikimate/glucono_kinase.
InterPro; IPR013708; Shikimate_DH-bd_N.
InterPro; IPR010110; Shikimate_DH_AroM-type.
InterPro; IPR000623; Shikimate_kinase/TSH1.
InterPro; IPR023000; Shikimate_kinase_CS.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
Pfam; PF01202; SKI; 1.
PIRSF; PIRSF000514; Pentafunct_AroM; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR01356; aroA; 1.
TIGRFAMs; TIGR01357; aroB; 1.
TIGRFAMs; TIGR01093; aroD; 1.
TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PROSITE; PS01128; SHIKIMATE_KINASE; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Complete proteome {ECO:0000313|Proteomes:UP000070720};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629621};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629772};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00727050};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629584};
NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172};
Reference proteome {ECO:0000313|Proteomes:UP000070720};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712179}.
DOMAIN 78 356 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 400 831 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1285 1365 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
NP_BIND 49 51 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 84 87 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 115 117 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 140 141 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 180 183 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 866 873 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 382 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 195 198 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 262 266 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1280 1568 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 258 258 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 273 273 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 819 819 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1170 1170 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1198 1198 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 195 195 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 269 269 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 285 285 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 120 120 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 131 131 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 147 147 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 153 153 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 162 162 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 163 163 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 191 191 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 248 248 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 269 269 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 285 285 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 354 354 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1568 AA; 170529 MW; F7CCFC1193266114 CRC64;
MAQASGQDPT RISILGEPNI IVNHGLWLNF VVDDLLQNIA TSTYVLITDT NLFNSYVPAF
QSRFEHASQG KDTRLLTYTI PPGEASKSRD TKAEIEDWML SQQCTRDTVI IALGGGVMGD
MIGYVAATFM RGVRFVQVPT TLLAMVDSSI GGKTAIDTPM GKNLVGAFWQ PKRIYIDLTF
LETLPVREFI NGMAEVIKTA AIWNETEFSV LEESAAHILE CVRSKGEGRL TPIKDVLKRI
VIGSAGVKAE VVSSDEREGG LRNLLNFGHS IGHAFEAILT PQLLHGEAVA IGMVKEAELA
RFLGVLRPGA VARLVKCIAS YDLPTSLQDK RVTKLTAGKK CPVDVLLEKM GVDKKNDGKK
KKIVLLSAIG KCHEPRASVV DDKTIRTILS SSVQVTPGVP KDLAVTVAPP GSKSISNRAL
VLAALGSGTC RIKNLLHSDD TQYMLSAIHQ LGGASYSWQD AGEVLVVEGK GGNLQASKEP
LYLGNAGTAS RFLTTVVALA SPGQDATTNV LTGNARMKVR PIGALVDALR SNGLEIEYLG
KENSLPLRID AAGGFKGGDI ELAATISSQY VSSILMAAPY AKNPVTLRLV GGKPISQLYI
DMTIAMMASF GIDVEVSSKE PNTYHIPKGA YKNPPEYTIE SDASSATYPL AVAAITGTKC
TIPNIGSKSL QGDARFAVDV LRPMGCSVEQ SDYSTTVTGP APGQLKALAH VDMEPMTDAF
LTASVLAAVA SGTTQITGIA NQRVKECNRI AAMKDQLAKF GVQCNELEDG IEVIGKGQDG
GVSTPEASIH CYDDHRVAMS FSVLAVASPG PVIVTERECV GKTWPGWWDI LFQVFKVDMV
GHESHADTHD EEISEKTLES SVFIIGMRGA GKTTAGNWMA KILGWKFIDL DQELERRAGC
TIPEMIRGDR GWDGFRADEL ALLRDVMERN KTGHVFSCGG GLVETPEARE LLNSYGANGG
HVLLVHRDTD QVVEYLNRDK TRPAYTSEIL QVYLRRKDFY NECSTHLYYS PHSESSGRQS
HIPHDFRQFV HSIAGKTTHF KDVLDKDHSF FVSLTVPDVD QAVNLLPEVV VGSDAVELRV
DLLQDRSIDS VIRQVSTLRA SAKKPIVFTL RTESQGGKFP DSAYDEGLEL YRLAVRMGME
YIDVEMTLPD EMIKTVTESR GYSRIIASHH DPKGTMSWKN ASWIQYYNRA LQYGDIIKLV
GIARTPEDNF DLARFKSRMQ EAQKTPMISM NMGKAGKLSR VLNRFLTPVS HPALPFKAAP
GQMSAAEIRQ ALALLGDLEP HNFYLFGKPI SASRSPALHN TLFKQTGLPH QYHRLETDNI
EDVRDVLKSP DFGGASVTIP LKLDIMGKLD ELSDAARTIG AVNTVVPFGK PDDNGCRRLL
GDNTDWRGMV HALRHAGIQG QDTDNKGAAM VVGSGGTTRA AIFALHSLGF GPIYIAARNQ
EKADAIAADF PKEYQLEGLS RASDAEKVSE NLKVVISTIP ADRPIDPTLQ ELVGAVLSRP
APAGERRVLL EMAYKPSHTP IMQLADDAGN WTTIPGLEVL SSQGWYQFEL WTGITPLYKD
ARAAVLGE


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