ID PPX3_PARTE Reviewed; 305 AA. AC A0C1E4; 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 3; DE EC=3.1.3.16; GN Name=Ppx3; ORFNames=GSPATT00034087001; 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; CT868032; CAK64611.1; -; Genomic_DNA. DR RefSeq; XP_001432009.1; XM_001431972.1. DR AlphaFoldDB; A0C1E4; -. DR SMR; A0C1E4; -. DR STRING; 5888.A0C1E4; -. DR EnsemblProtists; CAK64611; CAK64611; GSPATT00034087001. DR GeneID; 5017793; -. DR KEGG; ptm:GSPATT00034087001; -. DR eggNOG; KOG0372; Eukaryota. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; A0C1E4; -. DR OMA; CELITEQ; -. 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..305 FT /note="Serine/threonine-protein phosphatase PP-X homolog 3" FT /id="PRO_0000308175" FT ACT_SITE 114 FT /note="Proton donor" 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 55 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 81 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 81 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 113 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 237 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 305 AA; 34905 MW; A5305863340862C3 CRC64; MSQSDLDRQI AQLRNCENIT EGEVKALCTK AREILVEESN VQRVDAPVTI CGDIHGQFFD LMELFKVGGD CPDTNYLFLG DFVDRGFNSV ETFLLLLALK VRYPDRITLI RGNHESRQIT QVYGFYDECL RKYGSLNVWR YCTDIFDYLS LAAVIEEKIF CVHGGLSPSI KTMDDIRAID RKQEVPHDGA MCDLMWSDPD EIEGWNLSPR GAGYLFGGDV VDDFNRKNNI ELICRAHQLV MEGYRVMFNE QLVTVWSAPN YCYRCGNVAS ILELDENLTK QYKIFEAAQE NKGLPAKKPI PDYFL //