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Unplaced genomic scaffold K443scaffold_47, whole genome shotgun sequence

 A0A0C9Y554_9AGAR        Unreviewed;      1596 AA.
A0A0C9Y554;
29-APR-2015, integrated into UniProtKB/TrEMBL.
29-APR-2015, sequence version 1.
05-DEC-2018, entry version 37.
RecName: Full=Pentafunctional AROM polypeptide {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 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=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {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};
ORFNames=K443DRAFT_483232 {ECO:0000313|EMBL:KIK03208.1};
Laccaria amethystina LaAM-08-1.
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Agaricomycetidae; Agaricales; Tricholomataceae;
Laccaria.
NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK03208.1, ECO:0000313|Proteomes:UP000054477};
[1] {ECO:0000313|EMBL:KIK03208.1, ECO:0000313|Proteomes:UP000054477}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK03208.1,
ECO:0000313|Proteomes:UP000054477};
DOE Joint Genome Institute;
Kuo A., Kohler 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., 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:UP000054477}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
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:
Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712185};
-!- CATALYTIC ACTIVITY:
Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
carboxyvinyl)-3-phosphoshikimate + phosphate;
Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701,
ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712174};
-!- CATALYTIC ACTIVITY:
Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
dehydroquinate + phosphate; Xref=Rhea:RHEA:21968,
ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394;
EC=4.2.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858949};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
EC=2.7.1.71; Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00287328};
-!- CATALYTIC ACTIVITY:
Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
EC=1.1.1.25; Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
-!- 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 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:SAAS00336886}.
-!- 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; KN838582; KIK03208.1; -; Genomic_DNA.
EnsemblFungi; KIK03208; KIK03208; K443DRAFT_483232.
UniPathway; UPA00053; UER00089.
Proteomes; UP000054477; 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_00222; Shikimate_DH_AroE; 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; IPR022893; Shikimate_DH_fam.
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; 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; 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:SAAS00415286};
Complete proteome {ECO:0000313|Proteomes:UP000054477};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415327};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415285};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00415747}; 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:SAAS00415250};
NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00415286};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172};
Reference proteome {ECO:0000313|Proteomes:UP000054477};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415285};
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 79 364 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 416 844 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1314 1395 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 1432 1485 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 45 47 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 882 889 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 390 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 196 199 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 270 274 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1309 1596 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 266 266 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 281 281 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 832 832 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1198 1198 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1226 1226 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 277 277 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 293 293 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 256 256 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 277 277 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 293 293 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 362 362 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1596 AA; 172897 MW; 2CEA8FC3A7B075AD CRC64;
MADADVLKVS ILGKDSIHCG FHLIPYITQT VLSNLPSSTY VLVTDTNVAN FHLTAFEKEF
ERRISSLPTS PTKPRFLSLV IPPGETSKSR EGKANIEDFL LLHRCTRDSV ILALGGGVIG
DLVGFVAATF MRGVRFVQIP TTLLAMVDSS VGGKTAIDTP HGKNLIGAFW QPEFIFIDAA
FLETLPSREF SNGMAEVVKT AAIWNEAEFI SLESRSAEIF AAIQTPSTDY AGRSNQTRSI
AQELLLSIIV GSISVKAHIV TIDERETGLR NLVNFGHTIG HAIEAVLTPT ILHGECVSVG
MILEGEISRQ MGILSQVGVG RLNRCLKAYN LPVTLADPRI ASLPAAKLLT VERLLDIMRI
DKKNSGPEKK IVILSRIGAT YEPKATVVPD SIIAKTLSEA AKVIPGVPKH HPVKMATPGS
KSISNRALVL AALGKGTCRL KNLLHSDDTQ VMMAALNELK GASFAWEDAG ETLVVKGGEG
SLSVPPKGKE LYLGNAGTAA RFLTTVCTLV QSSPQDDAEY TVITGNARMK QRPIGPLVTA
LKANGSRIDF LESEGCLPLA IAPQGLKGSR LQLAASVSSQ YVSSILLCAP YAKEPITLEL
IGGQVISQPY IDMTVAMMKT FGVDVVRRKD PASGKFLDVY EIPKAVYTNP PEYNIESDAS
SATYPLAIAA ITGTSCTIQN IGSASLQGDA KFAKEVLEKM GCQVSQTATE TTVQGLPVGK
LKAIEEVDME VMTDAFLTAT ALAAVANGKT RIIGIANQRV KECNRIRAMI DELAKFGVET
VELDDGLEII GKPISDLKRG VSVHCYDDHR VAMAFSVLST VVEDTIIEEK RCVEKTWPNW
WDDLENKIGL TVQGVNLASV ASEASASGTI NHDSAASIIL IGMRGTGKTF VGNQAAATLS
WTCLDADAYF ETKYEMGVRE FVHQKGWQAF RDAEFEVLRE LIAEKTQGHV ISLGGGVVET
PAARELLKEY AATKGPVVHI VRPIDEVVRY LDEEASRPAY NEAIVDVFRR REPWFGECCS
HDFFNRFGDL PYSSAKTTSN EIARFFNHIT GHRPNLSQNL TSSQRSYFLC LTYPDVTQSF
PVIHELTQGV DAIELRVDLL RTSKDYDTIE YSIPSMAYVS SQVAALRRVT SLPIVFTVRT
QSQGGSFPDA AEEEAVELLK LALRLGVEYV DVEISLSEKK IKELVSLKGS SRIIASWHDW
SGNMIWDGPV VKEKYDAAAR FGDIIKIVGK ANTIQDNFAL YNFVSKVNSI AGSKPIIAIN
MGLEGQMSRV LNSTLTPVSH PLLPSKAAPG QLSFKQIQNA LHLLGLLPAQ RFYLFGTPIA
HSMSPTLHNT GFEILGLPHH YELLETKEVG EEIKIAIGDS AFGGASVTIP YKLDVIPLLD
KLSPAAEAIG AVNTIIPRTI GSGRMLVGDN TDWLGIKACI TEQLSSSRPI HAALVIGAGG
TARAAIYALS ALNIGDIYLY NRTASKAYEL AHAFPHAPVH VLEQLGQWPN GAVPPCVIVS
TVPASATTTE EETSGILLPS KLFDYRDGPA VVIDMAYKPA ETPLLKLAKA AGDNWATVPG
LEVLLEQGYV QFEMWTGRRC PKELVAKTVR EAYNRS


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27-465 ZFP57 is a protein similar to zinc finger protein 57. It is derived from an annotated genomic sequence (NT_007592) using gene prediction method. 0.05 mg
29-191 ZFP57 is a protein similar to zinc finger protein 57. It is derived from an annotated genomic sequence (NT_007592) using gene prediction method. 0.1 mg
AB1I144 Polyclonal Antibodies: Anti-CrPV Genome polyprotein Polyclonal Antibody; Specificity: Anti-CrPV Genome polyprotein Polyclonal Antibody ; Application: IHC 0.1mg
XGC-Roche-Trans-250K Deep Sequencing of Whole Transcriptome: Shotgun Library Prep, data generation using long read(up to 1kb read length) on Roche GSFLX (Minimum 4 sample) Sample
XGC-Roche-Trans-500K Deep Sequencing of Whole Transcriptome: Shotgun Library Prep, data generation using long read(up to 1kb read length) on Roche GSFLX (Minimum 2 Sample) Sample
XGC-Roche-16SMetaG48 Deep Sequencing of 16S amplicon Metagenome: Library preparation using V3-V4 region-400-500bp (customized region), data generation using long read shotgun approach on Roche GSFLX 48 samples
XGC-Roche-16SMetaG24 Deep Sequencing of 16S amplicon Metagenome: Library preparation using V3-V4 region-400-500bp (customized region), data generation using long read shotgun approach on Roche GSFLX 24 samples
XGC-Roche-16SMetaG12 Deep Sequencing of 16S amplicon Metagenome: Library preparation using V3-V4 region-400-500bp (customized region), data generation using long read shotgun approach on Roche GSFLX 12 samples
GE-102 Equine Skeletal Muscles Genomic DNA Species: Horse Tissue Genomic DNA 0.1mg


 

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