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Database: UniProt
Entry: A0A1Q3AWT3_CEPFO
LinkDB: A0A1Q3AWT3_CEPFO
Original site: A0A1Q3AWT3_CEPFO 
ID   A0A1Q3AWT3_CEPFO        Unreviewed;       919 AA.
AC   A0A1Q3AWT3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   08-NOV-2023, entry version 27.
DE   SubName: Full=DSPc domain-containing protein/Act-Frag_cataly domain-containing protein {ECO:0000313|EMBL:GAV60178.1};
GN   ORFNames=CFOL_v3_03709 {ECO:0000313|EMBL:GAV60178.1};
OS   Cephalotus follicularis (Albany pitcher plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX   NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV60178.1, ECO:0000313|Proteomes:UP000187406};
RN   [1] {ECO:0000313|Proteomes:UP000187406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA   Fukushima K., Hasebe M., Fang X.;
RT   "Cephalotus genome sequencing.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:GAV60178.1}.
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DR   EMBL; BDDD01000137; GAV60178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3AWT3; -.
DR   STRING; 3775.A0A1Q3AWT3; -.
DR   InParanoid; A0A1Q3AWT3; -.
DR   OrthoDB; 325201at2759; -.
DR   Proteomes; UP000187406; 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:UP000187406}.
FT   DOMAIN          704..849
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          769..825
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   919 AA;  102478 MW;  FFF5E0EAFE78B5BD CRC64;
     MAKEQNQDSP PATIINTLQE KEEDKDLVLG SDEPEAPLPL TVTSRVLYML GDITAGPAYR
     FAQWLELVRK RSGRYRSPGF PYMDTMPSSA GESLVDSKSV VPLDQAQDIS LWERLGKAAI
     MDIESTSFSW DTLSSLHHSE HSISSSTDHS EDEMNKALEV TVNSGGVVFF ALFNQHGVDD
     ASTKEEAAVI KFSSSRMATQ SERLGYEFAK WLGVQTPQAR IIHNNSQEWL QIKEAAEKAR
     VMATAEGDEV GQMTCTDLLE ALELSRCLFF MSYVHGSSLL ESSNAFESWE TAEKAASALG
     RILMLDLVIR NEDRLPCRQL RWRGNPANLL LADKMTSANM DALEEAFDSA IMRYRPRVIR
     ALQKERRATS VDSRLGPHNP RLISQGSDLS DITESPNSSE TSLRSHLLDD TTFSGLHIIA
     IDSGVPRRPP AGKRTNDHAS YPRLVELLLN NSEYSSNLLH ELTGGKLGYP PLEDADTIEI
     RVTEMASVIH AFRSGFRASL RDLQGFHLFL LTIHQKLDNL LRAFLNIVNK TTCGEFDKED
     FTVPESPSYA AGGVQSSSPP SKERVLIYNN LDYSDSELQR TAPKSLSSGS KESSDSSSPM
     SREGWHGKFY KGSGEPLRSL RLTTKLRDFN KFAKIDAESS KELEQWNDML RNEVIKLCQE
     NNFNTGFFEG SDNNCVVDAY ELKVRLEHIL ERISLISEAA NTERPSLISS SLFIGGALAA
     RSIYTLQHLG ITHILCLCSN EIGQSDSQFP DLFEYKNFSI SDREDSNISS IFEDASSFID
     HVEQIGGRVL VHCFEGRSRS ATAVVAYLML KKNYTLLEAW NTLKRVHRRA QPNDGFARTL
     QDLDRKLHGK ASMEWQQRKP MMKVCPICGK NAGLSSSSLK LHLQKSHKKL SSGSVDSAMT
     MEIQKALAAL KISRAETEA
//
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