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Database: UniProt
Entry: A0A388KLW2_CHABU
LinkDB: A0A388KLW2_CHABU
Original site: A0A388KLW2_CHABU 
ID   A0A388KLW2_CHABU        Unreviewed;       964 AA.
AC   A0A388KLW2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Protein-serine/threonine phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CBR_g8330 {ECO:0000313|EMBL:GBG71031.1};
OS   Chara braunii (Braun's stonewort).
OC   Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC   Chara.
OX   NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG71031.1, ECO:0000313|Proteomes:UP000265515};
RN   [1] {ECO:0000313|EMBL:GBG71031.1, ECO:0000313|Proteomes:UP000265515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S276 {ECO:0000313|EMBL:GBG71031.1,
RC   ECO:0000313|Proteomes:UP000265515};
RX   PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA   Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA   Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA   Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA   Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA   Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA   Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA   Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA   Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA   Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA   Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA   Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA   Rensing S.A.;
RT   "The Chara Genome: Secondary Complexity and Implications for Plant
RT   Terrestrialization.";
RL   Cell 174:448-464(2018).
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:GBG71031.1}.
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DR   EMBL; BFEA01000139; GBG71031.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A388KLW2; -.
DR   STRING; 69332.A0A388KLW2; -.
DR   EnsemblPlants; GBG71031; GBG71031; CBR_g8330.
DR   Gramene; GBG71031; GBG71031; CBR_g8330.
DR   Proteomes; UP000265515; Unassembled WGS sequence.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14498; DSP; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.40.20.10; Severin; 2.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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; PTHR46381; MKPA PROTEIN; 1.
DR   PANTHER; PTHR46381:SF4; MKPA PROTEIN; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 2.
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:UP000265515}.
FT   DOMAIN          271..413
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          330..391
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..762
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  102545 MW;  0BF11498E56D877A CRC64;
     MCFTALEGER GGGNSRKRER ADEAGASLAG ASGSRRMVMA AGGHEVHHKH RRSLSDMNLP
     STLLSPRATP GSPMDVESAL GVYQKGVVKA GGVGGFPSPT KSMAAGLVLN VANGGGGCDA
     KGSIDGGGES IVGRNGERAG ASSVGNAACV FANGVGGGKT APSVRNGRAP LRSLLIVRPS
     SMAKLEVASP RTRMWIEGNN VDRQVGGGGY RIPLSPLALR REASCLARGV VGVRAGVQLD
     LATLARNCDV GCGELSELKM RRDKMAFFEK QCSRVTDHIY VGSDFVARNR ETLRAAGITH
     VLNCVGFVCT EYFPGDLKYK TLWLEDTPGE DILSILYDVF DFLEEVREIG GRVFVHCCQG
     VSRSTALVIA YLMWKEGRSY DDVFRDVKTA RGVTNPNMGF ACQLLQWQKR VLGGVGVGVG
     VGRAIGGGGG GGGGGSPRFF RIAPHSHYDP LHLVHKLVPK AGVESLDTRG AFLLADPTGG
     LFVWKGTECP GVIAMAGEKA AKQMMKYEKL GGPVRFVNEG EEMAEFWAAF RNASSSPSSL
     SASPRVGVGI GSRLLRVPAY DADYDAVAEA LSHLGSEQVV AAEAPAAQTG GTGVRRRGWN
     DVSVYIAQVE FCNGEGLTPS RSYGKNNDWV GKRGGSSESV DRGGGMAIET ETSAVAVVSS
     SCEAAGVMEG GKGNGSCCSS PGTSGRGGIG RGKRSERRGE EDRENSCKAL RRGLDGGPES
     PTMSQRRRFE ESSTTTVDSE RRGVGSGGVQ EDDRRAREMA DKNPVEGGTA MVETASTRQV
     GVEECVSTAR LKKVGGEQRE EMGGEEDKAA SPSARSKAVR RGGAGGGIGR EEDKVASNLN
     NGALSRLFEW PSRDEVHGFG ADVLQSHKVF VLWILRPRGE EAAEGRSELV VWVGGECSSK
     ASDVEDSQEV EEEEERKHGR LAWERRWWRA GDEFRLWKSV PEGTCIQVVE EGKEPDDFWA
     YFSQ
//
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