ID PPX1_PARTE Reviewed; 303 AA. AC P49576; A0DR78; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 27-MAR-2024, entry version 96. DE RecName: Full=Serine/threonine-protein phosphatase PP-X homolog 1; DE EC=3.1.3.16; GN Name=Ppx1; ORFNames=GSPATT00019262001; OS Paramecium tetraurelia. OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium. OX NCBI_TaxID=5888; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Stock 51; RA Russell C.B., Johnson J., Hinrichsen R.D.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [2] 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 -!- SEQUENCE CAUTION: CC Sequence=CAK85545.1; Type=Erroneous gene model prediction; Evidence={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; U31445; AAA75081.1; -; Genomic_DNA. DR EMBL; CT868541; CAK85545.1; ALT_SEQ; Genomic_DNA. DR AlphaFoldDB; P49576; -. DR SMR; P49576; -. DR STRING; 5888.P49576; -. DR InParanoid; P49576; -. 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 1" FT /id="PRO_0000058888" 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" FT CONFLICT 16 FT /note="N -> D (in Ref. 1; AAA75081)" FT /evidence="ECO:0000305" FT CONFLICT 20 FT /note="T -> S (in Ref. 1; AAA75081)" FT /evidence="ECO:0000305" FT CONFLICT 47 FT /note="T -> A (in Ref. 1; AAA75081)" FT /evidence="ECO:0000305" FT CONFLICT 62 FT /note="L -> V (in Ref. 1; AAA75081)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="K -> E (in Ref. 1; AAA75081)" FT /evidence="ECO:0000305" FT CONFLICT 297 FT /note="V -> T (in Ref. 1; AAA75081)" FT /evidence="ECO:0000305" SQ SEQUENCE 303 AA; 34745 MW; 9A00E5F88F5C810D CRC64; MSDIDQWIET LKNGENLKET DVKILCNKAK DILNNEDNVI RVEAPVTICG DIHGQFYDLM ELFKVGGDVP ETNYLFLGDF VDRGYNSVET FLLLLALKVR YPDQITLIRG NHESRQITQV YGFYDECLRK YSTLNVWKYC TEVFDYLALA AVVNDNIFCV HGGLSPYIKT IDEIRIINRK QEVPHEGVMC DLMWSDPDEI EGWSQSARGA GFVFGADVVK EFNRRNGISL ICRAHQLAME GFKLMFDNSL VTVWSAPNYC YRCGNVASIL ELDENLKKYY KLFEAAPTDR AQNSKKVIAD YFL //