ID PPX2_PARTE Reviewed; 303 AA. AC A0DJ90; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 73. DE RecName: Full=Serine/threonine-protein phosphatase PP-X homolog 2; DE EC=3.1.3.16; GN Name=Ppx2; ORFNames=GSPATT00017464001; OS Paramecium tetraurelia. OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium. OX NCBI_TaxID=5888; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Stock d4-2; RX PubMed=17086204; DOI=10.1038/nature05230; RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R., RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., RA Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., RA Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., RA Cohen J., Wincker P.; RT "Global trends of whole-genome duplications revealed by the ciliate RT Paramecium tetraurelia."; RL Nature 444:171-178(2006). 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-4 (PP-X) CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CT868452; CAK83107.1; -; Genomic_DNA. DR RefSeq; XP_001450504.1; XM_001450467.1. DR AlphaFoldDB; A0DJ90; -. DR SMR; A0DJ90; -. DR STRING; 5888.A0DJ90; -. DR EnsemblProtists; CAK83107; CAK83107; GSPATT00017464001. DR GeneID; 5036289; -. DR KEGG; ptm:GSPATT00017464001; -. DR eggNOG; KOG0372; Eukaryota. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; A0DJ90; -. DR OMA; ANAWRWC; -. DR Proteomes; UP000000600; Partially assembled WGS sequence. 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:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central. DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR047129; PPA2-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1. DR PANTHER; PTHR45619:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC SUBUNIT; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 3: Inferred from homology; KW Hydrolase; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..303 FT /note="Serine/threonine-protein phosphatase PP-X homolog 2" FT /id="PRO_0000308174" FT ACT_SITE 112 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 51 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 53 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 79 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 79 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 161 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 235 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 303 AA; 34643 MW; 1A1C31BE0EB45BE5 CRC64; MSDIDQWIET LKNGENLKET DVKILCNKAK DILNNEDNVI RVEAPVTICG DIHGQFQDLM ELFKVGGDVP ETNYLFLGDF VDRGYNSVET FLLLLALKVR YPDQITLIRG NHESRQITQV YGFYDECLRK YSTLNVWKYC TEVFDYLALA AVVNDSIFCV HGGLSPYIKT IDEIRIINRK QEVPHEGVMC DLMWSDPDEI EGWSQSARGA GFVFGADVVK EFNRRNGISL ICRAHQLAME GFKLMFDNSL VTVWSAPNYC YRCGNVASIL ELDENLKKYY KLFEAAPTDR ASNSKKTIAD YFL //