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Database: UniProt
Entry: M1C1E8_SOLTU
LinkDB: M1C1E8_SOLTU
Original site: M1C1E8_SOLTU 
ID   M1C1E8_SOLTU            Unreviewed;       881 AA.
AC   M1C1E8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400057635, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400057635}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400057635};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001482};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; M1C1E8; -.
DR   STRING; 4113.M1C1E8; -.
DR   PaxDb; 4113-PGSC0003DMT400057635; -.
DR   EnsemblPlants; PGSC0003DMT400057635; PGSC0003DMT400057635; PGSC0003DMG400022380.
DR   Gramene; PGSC0003DMT400057635; PGSC0003DMT400057635; PGSC0003DMG400022380.
DR   eggNOG; KOG0323; Eukaryota.
DR   InParanoid; M1C1E8; -.
DR   OMA; GWFPAEE; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1C1E8; baseline.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR039189; Fcp1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR23081:SF0; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1; 1.
DR   PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT   DOMAIN          133..381
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   DOMAIN          701..767
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          515..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  98915 MW;  7AB17B1D19E31421 CRC64;
     MFKSTVVLYE GERLVGEVEI YCEKGVLWGE KVIRISHYSP SSERCPPLAV LHTVTTGLSF
     KLEPTKSKPL TQDSPLTLLH STCLRDNKTA VMSLGREELH LVAMQSKNIG GQCPCFWGFK
     VASGLYDSCL TMLNLRCLGI VFDLDETLIV ANTMRSFEDR IEALQRKINS ESDPQRASVM
     LAEVKRYQED KIILKQYAEN DQVVDNGKVI KSQSEVFPAL SDNHQPIVRP LIRLQDRNII
     LTRINPMIRD TSVLVRLRPA WEDLRSYLTA RGRKRFEVYV CTMAERDYAL EMWRLLDPDS
     NLINSQELLD RIVCVKSGLR KSLFNVFQDG NCHPKMALVI DDRLKVWDDK DQPRVHVVPA
     FAPYFAPQAE GNNSVPVLCV ARNVACNVRG GFFKDFDEGL LQRISEVAYE DDIKQVPSAP
     DVSNYLISED DPSAVNGNKD SLGFDGMADS EVERRLKEAM LASTSVPSQM TNLDPRLVPA
     LQYPVPPVIS QPSIQSPVVP FPTQHLPQVT SVLKSSVTQI SPQDTSLQSS PAREEGEVPE
     SELDPDTRRR LLILQHGQDT RDQVSSEPKF PMGTPLQVSV PPRVQPHGWF PAEEEMSPRQ
     LNRPLPPKEF PLNPESMHIN KHRPPHPPFL PKMETSMPSD RVLFENQRLP KEVIPRDDRM
     RFSQSQPSFR PPGEEVPLGR SSSSNRVLDL EPGHYDPYLE TPAGALQDIA FKCGAKVEFR
     SSFLSSPELQ FSLEVLFAGE KVGEGTGRTR REAQRRAAEE SLMYLADKYL SCIKPDSSST
     QGDGFRFPNA SDNGFVDNMS PFGYQDRVSH SFASEPPRVL DPRLEVFKKS VGSVGALREL
     CAIEGLGLAF QTQPQLSANP GQKSEIYAQV AHLLPFLLCY C
//
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