ID A0A200QGL6_9MAGN Unreviewed; 948 AA.
AC A0A200QGL6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE SubName: Full=Dual specificity phosphatase {ECO:0000313|EMBL:OVA09658.1};
GN ORFNames=BVC80_9101g193 {ECO:0000313|EMBL:OVA09658.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA09658.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA09658.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA09658.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OVA09658.1}.
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DR EMBL; MVGT01002051; OVA09658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QGL6; -.
DR STRING; 56857.A0A200QGL6; -.
DR InParanoid; A0A200QGL6; -.
DR OrthoDB; 325201at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0043622; P:cortical microtubule organization; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IEA:InterPro.
DR CDD; cd14498; DSP; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR015275; Actin-fragmin_kin_cat_dom.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR035010; PHS1.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR47100; DUAL SPECIFICITY PROTEIN PHOSPHATASE PHS1; 1.
DR PANTHER; PTHR47100:SF5; DUAL SPECIFICITY PROTEIN PHOSPHATASE PHS1; 1.
DR Pfam; PF09192; Act-Frag_cataly; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402}.
FT DOMAIN 700..845
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 765..821
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 573..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 105779 MW; 80026EC36E437B3A CRC64;
MSHHEKEKPS IIITRTHHHH HQDINLLQER GDQEDKDLNL AVGSRVLYLL GDITAGPAYR
FAQWLDSVRK RSGQYRSSGF PNRPPKLETM LLSAGEPIAE SKSLQHLEQV SEISLWDRLG
RATMLDIEST DFSWDMLSSL HRTEHNSSTE HSEDEMNKAL EVTVNSGGVV FFALFNGPVN
DESFQQEAAA VIKISSSRMA TQSERLGYEF AKWLGVRTPQ ARVVHNSSPE WQQIKQAAEK
ARDAAILVGD DAGEMTCSEL LEALELSRCL FLMNYVHGSP LLESSSAFDS LEASEKTAAA
LGRILMLDLV IRNEDRLPCR QLRWRGNSAN LLFSSKALSE DMDVLDEDFG PGVIGTLQKE
RRASSVDGRL SVCDPELISQ SSDISSLMSP KSTDWNLKDQ GLNELKYGDF DIVAIDSGVP
RRPPAGKRAN DHAHYPKLVE LLLNSAEYSS SLLYDITGGK VGCPLPEEAD EQTDLCLLDI
TAVVREFRSG FRAALKDLQG FYIFLLTLYQ KLDSLLRMFL TIIDKNSSGD FDKEDSVVSE
PPSHAAATGF NCVSPVTKER VFTEAHADLG DMEFQRTHPR PSPPGHKESP DSVSPISREN
WHGRYHKGSG DPLRSLRLTA KLRDFNKYAK VDAELHRELE QWNELLRTDA IKLCQDNNFN
TGFFEGSENN SVVDAYELKV RLEHILERIA LISEAASTEK PSFITGNLFI GGALAAKAVY
TLQHLGITHI LCLCSNEIGQ SDSQYPDLFE YKNFSIFDNE DTKISNIFEE ASDFIERVEH
SGGKVLVHCF EGKSRSATVV LAYLMLRKNF TLLEAWNTLK RAHRRAQPND GFAKILLDLD
KKLHGKVSMA WQQKRPRMKV CPVCGKNAGL SSSSLKLHLQ KSHRMISSAS VDSAMKSHRV
LSSGSVDSAM TMEIHKVLDT IKLSRGGSAS PTEKQSQSML DGLLDLDQ
//