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Database: UniProt
Entry: A0A2V0NV29_9CHLO
LinkDB: A0A2V0NV29_9CHLO
Original site: A0A2V0NV29_9CHLO 
ID   A0A2V0NV29_9CHLO        Unreviewed;       570 AA.
AC   A0A2V0NV29;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=MAP kinase phosphatase {ECO:0000313|EMBL:GBF91494.1};
GN   ORFNames=Rsub_04234 {ECO:0000313|EMBL:GBF91494.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF91494.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF91494.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF91494.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily.
CC       {ECO:0000256|ARBA:ARBA00008601}.
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:GBF91494.1}.
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DR   EMBL; BDRX01000024; GBF91494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0NV29; -.
DR   STRING; 307507.A0A2V0NV29; -.
DR   InParanoid; A0A2V0NV29; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14498; DSP; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF537; TYROSINE-PROTEIN PHOSPHATASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00498; FHA; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Kinase {ECO:0000313|EMBL:GBF91494.1};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW   Transferase {ECO:0000313|EMBL:GBF91494.1}.
FT   DOMAIN          137..281
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          197..270
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          486..538
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   REGION          331..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  60836 MW;  C5F1333429762E2E CRC64;
     MPLDARTIDA DGVFRAVYAA CPNDPKVLLV DVRPLGHFKK GHAVRAYCVR LSADGGALLD
     YSQASYDTAW SKDVWWGRPV IVYGPPALSR DHPVAAFLSR EGRAASLAVY RDGLEGLAAA
     YPFLVTASVK QGCFKHYPSM ILPRWLFLGD WGDAEAAERL AELGVKRIVS IHNHPENLKP
     RAGVRHLKLE LPDVETADIS AHFNAAYEFI DEGRRLKQPT LVHCGAGVSR SAALVAAYLM
     RSRPGTTAAA ALAEVRAARS MVQPNDGFYR TLCALEHGLG IPEHERSDPN ALTGFAGADA
     GEVKLSADAA GAKVAVVQLD AAGRALGAGA PAAPAAAPAA GVVGRGDEAQ RRRRSRSRSR
     SREGERGWRD RARDRERERE RDRRRSRSRE REGRDGGRRD RSGSRERRRG RSRSRSRERD
     GHGGGGGRAR DAPAPPPTAP ADPVAAAAAA AAAAGKKGFL LAIRISKPDG QVGQLVLGPV
     GLHQRVVFGR APPPAADVAL EHASASRQHA ALTVDAAGAV SLTDLGSSHG SKVGDAWIKP
     HAPKEVPLGA VMRFGASTRA YKLERVERVG
//
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