ID   PP2A_TOBAC              Reviewed;         312 AA.
AC   Q9XGH7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Serine/threonine-protein phosphatase PP2A catalytic subunit;
DE            EC=3.1.3.16;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. SR1;
RA   Remus M., Stitt M., Zrenner R.;
RT   "Molecular analysis of protein phosphatase 2A in tobacco.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ007496; CAB46506.1; -; mRNA.
DR   RefSeq; NP_001312211.1; NM_001325282.1.
DR   RefSeq; XP_016462375.1; XM_016606889.1.
DR   AlphaFoldDB; Q9XGH7; -.
DR   SMR; Q9XGH7; -.
DR   STRING; 4097.Q9XGH7; -.
DR   GeneID; 107779504; -.
DR   GeneID; 107785560; -.
DR   KEGG; nta:107779504; -.
DR   KEGG; nta:107785560; -.
DR   OrthoDB; 808922at2759; -.
DR   PhylomeDB; Q9XGH7; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..312
FT                   /note="Serine/threonine-protein phosphatase PP2A catalytic
FT                   subunit"
FT                   /id="PRO_0000058865"
FT   ACT_SITE        121
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  35639 MW;  B24F1ABEC2793315 CRC64;
     MDPVPSSASH GNLDEQIAQL MQCKPLSEQE VRGLCEKAKE ILMEESNVQP VKSPVTICGD
     IHGQFHDLAE LFRIGGKCPD TNYLFMGDYV DRGYYSVETV TLLVALKVRY PQRITILRGN
     HESRQITQVY GFYDECLRKY GNANVWKTFT DLFDYFPLTA LVESEIFCLH GGLSPSIETL
     DNIRNFDRVQ EVPHEGAMCD LLWSDPDDRC GWGISPRGAG YTFGQDISEQ FNHTNNLKLI
     ARAHQLVMEG FNWAHDQKVV TIFSAPNYCY RCGNMASILE VDDSRERTFI QFEPAPRRGE
     PDVTRRTPDY FL