PP1_MAIZE
ID PP1_MAIZE Reviewed; 316 AA.
AC P22198;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine/threonine-protein phosphatase PP1;
DE EC=3.1.3.16;
GN Name=PP1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Smith R.D., Walker J.C.;
RL Submitted (AUG-1992) 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 -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; M60215; AAA33545.1; -; mRNA.
DR PIR; S29317; S29317.
DR RefSeq; NP_001105341.1; NM_001111871.1.
DR AlphaFoldDB; P22198; -.
DR SMR; P22198; -.
DR STRING; 4577.GRMZM2G112240_P02; -.
DR PaxDb; P22198; -.
DR PRIDE; P22198; -.
DR EnsemblPlants; Zm00001eb191230_T001; Zm00001eb191230_P001; Zm00001eb191230.
DR GeneID; 542269; -.
DR Gramene; Zm00001eb191230_T001; Zm00001eb191230_P001; Zm00001eb191230.
DR KEGG; zma:542269; -.
DR MaizeGDB; 30136; -.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR OrthoDB; 766640at2759; -.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; P22198; baseline and differential.
DR Genevisible; P22198; ZM.
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 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 InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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 Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..316
FT /note="Serine/threonine-protein phosphatase PP1"
FT /id="PRO_0000058808"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 121
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 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 316 AA; 35763 MW; ED71EB1ABF308680 CRC64;
MDPALLDDVI RRLLEVKNLK PGKNAQLSES EIKQLCAAAK EIFLQQPNLL ELEAPIKICG
DVHGQYSDLL RLFDYGGYPP QANYLFLGDY VDRGKQSLET ICLLLAYKVK YPENFFLLRG
NHECASVNRI YGFYDECKRR FSVKLWKTFT DCFNCLPVSA LIDEKILCMH GGLSPELNKL
EQILNLNRPT DVPDTGLLCD LLWSDPSNEA TGWAINDRGV SFTFGPDKVS EFLEKHDLDL
ICRAHQVVED GYEFFASRQL VTIFSAPNYC GEFDNAGAMM SVDDTLMCSF QILKPARKMM
GGSTNNKSGF KSFRGW
