ID YY06_CAEEL Reviewed; 454 AA. AC P48460; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 4. DT 27-MAR-2024, entry version 150. DE RecName: Full=Putative serine/threonine-protein phosphatase C27B7.6; DE EC=3.1.3.16; GN ORFNames=C27B7.6; 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; Z54236; CAA90981.4; -; Genomic_DNA. DR PIR; T19505; T19505. DR RefSeq; NP_501547.3; NM_069146.4. DR AlphaFoldDB; P48460; -. DR SMR; P48460; -. DR STRING; 6239.C27B7.6.1; -. DR PaxDb; 6239-C27B7-6; -. DR EnsemblMetazoa; C27B7.6.1; C27B7.6.1; WBGene00007763. DR GeneID; 182956; -. DR KEGG; cel:CELE_C27B7.6; -. DR UCSC; C27B7.6; c. elegans. DR AGR; WB:WBGene00007763; -. DR WormBase; C27B7.6; CE43510; WBGene00007763; -. DR eggNOG; KOG0374; Eukaryota. DR GeneTree; ENSGT00970000196421; -. DR HOGENOM; CLU_004962_0_3_1; -. DR InParanoid; P48460; -. DR OMA; TEIHELC; -. DR OrthoDB; 5586361at2759; -. DR PhylomeDB; P48460; -. DR PRO; PR:P48460; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00007763; 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 CDD; cd00144; MPP_PPP_family; 1. 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:SF285; 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..454 FT /note="Putative serine/threonine-protein phosphatase FT C27B7.6" FT /id="PRO_0000058916" FT REGION 414..454 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 424..448 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 126 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 67 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" 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 93 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 125 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 174 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 252 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 454 AA; 51597 MW; 425C550C7B010E0B CRC64; MLETEHANTE VHELCRQMIA RIEKYGTLEG FSDSDILEVL KTIKEILEPL PCLIEIIAPV VVFGDIHGQL GDLLQFTNEV GRPPDFQYLF LGDYVDRGPN SLEVTVWLFC MKILFSKKVH LLRGNHEVRR VNTMYGFKEE MMRKRNSHLW KVFNDVFAEL SICASINRKI LCMHGGISPK IESWDSLTGM TKPRVHGDCE HGLIVDLIWS DPNRKDDTIQ FNKMRGISTL FGKSVVDNLC TTLAIDLIIR AHEMKEKGHT FEFDNRLLTV FSAPYYSGHN SNLGSVATIS KSLKLRIVTL KPNKGYDRSK LDKRTLHDFE KNFQPLDENP RKNISCQFNV PPNGQKMSPF LGEYSMFAHE TQFCKKDNET PVKKPYSSNQ DEDHSVLDMI RKTQKGYGVE VSLKDKVMSL ESIRKKLGMT TSTTPPPPRT PSPDAPLAQS PPIPRSPPSS TENA //