ID A0A1X0NIN2_9TRYP Unreviewed; 752 AA. AC A0A1X0NIN2; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 05-FEB-2025, entry version 29. DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273}; DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273}; GN ORFNames=TM35_000431700 {ECO:0000313|EMBL:ORC84602.1}; OS Trypanosoma theileri. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC84602.1, ECO:0000313|Proteomes:UP000192257}; RN [1] {ECO:0000313|EMBL:ORC84602.1, ECO:0000313|Proteomes:UP000192257} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|EMBL:ORC84602.1}; RA Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P., RA Matthews J., Matthews K., Carrington M.; RT "An alternative strategy for trypanosome survival in the mammalian RT bloodstream revealed through genome and transcriptome analysis of the RT ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-threonyl-[protein] + H2O = 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 Evidence={ECO:0000256|RuleBase:RU004273}; CC -!- SIMILARITY: Belongs to the PPP phosphatase family. CC {ECO:0000256|RuleBase:RU004273}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ORC84602.1}. 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; NBCO01000043; ORC84602.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1X0NIN2; -. DR STRING; 67003.A0A1X0NIN2; -. DR VEuPathDB; TriTrypDB:TM35_000431700; -. DR OrthoDB; 10267127at2759; -. DR Proteomes; UP000192257; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0140791; F:histone H2AXS140 phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:1990439; F:MAP kinase serine/threonine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0180006; F:RNA polymerase II CTD heptapeptide repeat S2 phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0180007; F:RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0180008; F:RNA polymerase II CTD heptapeptide repeat S7 phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0180005; F:RNA polymerase II CTD heptapeptide repeat T4 phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0180004; F:RNA polymerase II CTD heptapeptide repeat Y1 phosphatase activity; IEA:UniProtKB-EC. 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; IPR050341; PP1_catalytic_subunit. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF496; SERINE_THREONINE-PROTEIN PHOSPHATASE; 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 {ECO:0000256|RuleBase:RU004273}; KW Reference proteome {ECO:0000313|Proteomes:UP000192257}. FT DOMAIN 433..438 FT /note="Serine/threonine specific protein phosphatases" FT /evidence="ECO:0000259|PROSITE:PS00125" FT REGION 148..185 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 505..539 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 168..178 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 505..514 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 526..539 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 752 AA; 84233 MW; FBC6CC4D5E0F6206 CRC64; MWDKHCIVVE EGRELIVGTD PLCDVQVTLP KLRVFGSHLV VSRYHDIAHV ICSTNGVLLL SISTRSLSVY IHGIQVVPSR EPIELYPGSP VSFGGRHKGT TFCFFTSHTS PAVISPMPSA KFSPLALNLN GMKKSLPFPP LNATCNVTEQ GVSPRSPRVV RIIGPSDNDN DNDNDDNDNN GNSNKYMSTC HTSVSLLSSF KNSSKSISNY GKSITTYDTQ WKFNTENKLP SSHTIVPFVV ELWGLRATLH SVIGHNTQSR SASTRSCGVA EISGRGGNTP GDPYFTFRGC EMLKGLHLSR IETPVRSAAA SVLESLEDAY EPGEGTFLQF TTSAKNSLFQ HFLLLADHAL IELQKTPLTV RRCSPIVCCG DIHGSFSDLK TIFDNVVPFH HWSLMTMPVL FLGDYVDRGP HDVEVVLFLL AWYILCPENV ILLRGNHEDE EVNGDIQLYG ETSFRKKCWK FFNKDNGEIF WNRVNDVFAE LPIVAIIDST IFACHGGIPL LREKSSSETG EVKNGKKGFG VRQQQRKQEE NKKEEQDTDH VELMNDVPCM EFFQLLINGM PNELEEFRFR CMMPDVHDND LKAQHRRLIR ELLWNDPVPQ FSTSTYGNNG NGTADTEFTQ QDGFDVNGFR TNFGRGDHRN VIREFSASAL VSFMERWGFT LLIRAHQQKM AGIEMGLAGR ILTLFSCCNY TGDTNRAGAC IVVDGEVRLV SWRTVLGTSR DEPPPETLRS SFDDSEETQI PHYVGLRRLR FG //