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Unplaced genomic scaffold scaffold_19, whole genome shotgun sequence

 A0A0C9ZVG8_9HOMO        Unreviewed;      1657 AA.
A0A0C9ZVG8;
29-APR-2015, integrated into UniProtKB/TrEMBL.
29-APR-2015, sequence version 1.
28-MAR-2018, entry version 31.
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-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=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=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
ORFNames=PISMIDRAFT_22597 {ECO:0000313|EMBL:KIK26217.1};
Pisolithus microcarpus 441.
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Agaricomycetidae; Boletales; Sclerodermatineae;
Pisolithaceae; Pisolithus.
NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK26217.1, ECO:0000313|Proteomes:UP000054018};
[1] {ECO:0000313|EMBL:KIK26217.1, ECO:0000313|Proteomes:UP000054018}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=441 {ECO:0000313|EMBL:KIK26217.1,
ECO:0000313|Proteomes:UP000054018};
DOE Joint Genome Institute;
Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
Nordberg H.P., Cantor M.N., Hua S.X.;
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Proteomes:UP000054018}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
DOE Joint Genome Institute;
Mycorrhizal Genomics Consortium;
Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
"Evolutionary Origins and Diversification of the Mycorrhizal
Mutualists.";
Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
-!- 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|PIRNR:PIRNR000514,
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|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858949}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629607}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712174}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, 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; KN833703; KIK26217.1; -; Genomic_DNA.
EnsemblFungi; KIK26217; KIK26217; PISMIDRAFT_22597.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000054018; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
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.
InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 1.
Pfam; PF01488; Shikimate_DH; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
Pfam; PF01202; SKI; 1.
PIRSF; PIRSF000514; Pentafunct_AroM; 2.
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; 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:UP000054018};
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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000054018};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712179}.
TRANSMEM 110 131 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 79 361 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 460 909 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1373 1454 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 1495 1558 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 42 44 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 85 88 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 116 118 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 141 142 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 181 184 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 948 955 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 387 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 196 199 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1368 1657 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 257 257 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 272 272 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 897 897 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1259 1259 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1287 1287 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 196 196 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 268 268 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 284 284 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 121 121 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 132 132 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 148 148 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 154 154 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 163 163 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 164 164 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 192 192 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 247 247 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 268 268 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 284 284 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 359 359 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1657 AA; 176730 MW; 5606C358AE66CF06 CRC64;
MSVQKISILG KESIHVGFNL VQHISDTLLD TLPSSTYVLI TDTNIAPLYL QPIAATFALA
TDARFPNKSD PARPRFLTYT IPPGETTKTR EGKAEIEDFL LRHRCTRDTV IIALGGGVIG
DLVGFVAATF MRGVRVVQVP TSLLAMVDSS IGGKTAVDAP LGKNLIGAFW QPSYIFVDAA
FLRTLPVREL ANGLAEVIKT AAIWDETAFA LLEANSSTLL TCLSSSSPAL DLNHPLLTLI
ISSINTKATI VSRDPREAHL RGLVNFGHSI GHAIEALVTP YVLHGECISV GMVLEAELAR
AAGVLGQVSL GRLRRCIESY GLPSTLSDKR ILEAEKRIVA TGGQPISVDT LLDRMSVDKK
NAGKLKRVVL LERIGKTREL RATGVADEDI RKVLCPAVRV VAGTPGTYAK PPLPPPMLEL
PDADPTQLSG PVPNAQIAQV SSATSAPSRK AATDIPHITL STPGSKSISN RALVLAALCK
GTCRLKNLLH SDDTQVMMAA LEQLKAATFT WTDNGETLVV TGSGGALSVP PPGTQLYLGN
AGTAARFLTT VCTIVSPPNT TDTSRAETTT ITGNARMKQR PIAPLVTALR GAGATIGYLE
SEGCLPLSIK PLGRLPGGTL TLDASLSSQY VSSILLCAPY AAQPTTLVLT GPAVISQLYI
DMTIELMRDF GIEVTRERDA ASGDLLNVYH IPRGTYRAPE SGEFVIESDA SSATYPLAIA
AITGTRCTLA NIGSSSLQGD ARFAKEVLEP MGCEVVQTET ETTVTGPPKG KLRARGEVDM
EPMTDAFLTA CAVAAVATDG GVGEGAESGE GKNVTRIRGI ANQRVKECNR IQAMIDQLAK
FGISTRELPD GLEVYGRPLP QLTRGASIHC YDDHRVAMAF AVLATVVDGT ILEEKRCVEK
TWPNWWDDLE NKLGVKVEGV QLPEPAKTVR TSPAPKTPET IPSILLVGMR GSGKTYIGEL
AAQALSLPLL DFDAEFSRVY QQPLRSFVLE RGWAEFRKAE ITLLLELMKA HARGWVVSLG
GGIVETLEAR EALKKYAKAG GCVVWVQREP EEIERYLESE TERPAYGEPV RAVLERRAPW
FEECANYVFG NHTALPGGAS ALGSGALEAE VSRFFGHISG LRPNLVSTNA NRSYFLSLTY
PDVAPALPKI PELTTGVDAV ELRADLLHES GLQIPSPSYV STQLFALRRA TTLPIVFTVR
TVSQGGAFPD DAPVEAGKLL KLALRLGVEY VDVETTLPAP LILDIVSLKG PSHIVASFHD
WTGSVKWDSV AMKAQYEAAA QIGDVVKLIS KANSVSDNFK LQDFVAKVAI ASKPLIAINM
GAAGQLSRVL NTTLTPVTHP LLPTAAAPGQ MSVSDIHRAL HLIGLLPARR FFLFGSPIAR
SPSPTLHNTG FAALGLPHTY GLLEGESITD ETRAILASPD FGGASVTIPL KLDIMSVLDG
FTAAATTIGA VNTIIPCQSP DANKPRLLLG DNTDYLGIIG AIHAVSPGLR APGSALVLGA
GGTARAAVYA LHTLGTKQIY LYNRTHSKAT AIAEAFSSIP VRVLDKLGNW PAGAPSVVIS
TVPADATTIE TGPGFESKVY LPPNLLDAST KGVVVDMAYK PAETPLLALT KRIAPTWATV
PGVEVLLEQG YAQFEHWTGR RCPREIVREK VLQWYNA


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