ID YT91_CAEEL Reviewed; 364 AA. AC P48458; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Putative serine/threonine-protein phosphatase C06A1.3; DE EC=3.1.3.16; GN ORFNames=C06A1.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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}. 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; Z49886; CAA90052.1; -; Genomic_DNA. DR PIR; T18972; T18972. DR RefSeq; NP_496276.1; NM_063875.3. DR AlphaFoldDB; P48458; -. DR SMR; P48458; -. DR BioGRID; 39942; 1. DR STRING; 6239.C06A1.3.1; -. DR EPD; P48458; -. DR PaxDb; 6239-C06A1-3; -. DR PeptideAtlas; P48458; -. DR EnsemblMetazoa; C06A1.3.1; C06A1.3.1; WBGene00007354. DR GeneID; 174626; -. DR KEGG; cel:CELE_C06A1.3; -. DR UCSC; C06A1.3; c. elegans. DR AGR; WB:WBGene00007354; -. DR WormBase; C06A1.3; CE02116; WBGene00007354; -. DR eggNOG; KOG0374; Eukaryota. DR GeneTree; ENSGT00970000196438; -. DR HOGENOM; CLU_004962_0_0_1; -. DR InParanoid; P48458; -. DR OMA; LQISFQQ; -. DR OrthoDB; 2872963at2759; -. DR PhylomeDB; P48458; -. DR PRO; PR:P48458; -. DR Proteomes; UP000001940; Chromosome II. DR Bgee; WBGene00007354; Expressed in adult organism and 1 other cell type or tissue. 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 PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF194; SERINE_THREONINE-PROTEIN PHOSPHATASE-RELATED; 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..364 FT /note="Putative serine/threonine-protein phosphatase FT C06A1.3" FT /id="PRO_0000058915" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..24 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 154 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 93 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 95 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 121 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" 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 153 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 202 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 277 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 364 AA; 41208 MW; 1384EAB0C9729913 CRC64; MSTDGNNNKK GSKEGPKSSE ISKFDLAKEN PKLAEWMDDC IKRMNSLYKD TNINICNVMT GHEIISIIRM VEAIFMEESN LCEAEAPIKV IGDIHAQYQD MNRLFDLIGR VPEEKLMFLG DYVDRGPQGI EVLILLFCLK IRYRDRIYLL RGNHETPSVN KIYGFYVECQ YKYGIGLWWD FQSCFNRMPM SGLISKRVLC MHGGLSPELI NLDTIRNIPR PCEPLDRGLL IDLLWSDPTN KGEGWFHSIR GISYMFGKGV VEQACKSLEI DLIIRAHQVV QDGYEMMTGR RLITVFSVPN YCAQFTNAAA VVCLNANLQI SFQQMIPPPL PEGTKAKAAP AIAIDPNIDA ARADKDAIKP FVKE //