ID Y9461_DICDI Reviewed; 1006 AA. AC Q54WS9; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 2. DT 02-SEP-2026, entry version 99. DE RecName: Full=Probable protein phosphatase DDB_G0279461; DE EC=3.1.3.16; GN ORFNames=DDB_G0279461; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-seryl-[protein] + H2O = 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=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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: In the C-terminal section; belongs to the PP2C family. 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; AAFI02000031; EAL67669.2; -; Genomic_DNA. DR RefSeq; XP_641638.2; XM_636546.2. DR AlphaFoldDB; Q54WS9; -. DR FunCoup; Q54WS9; 141. DR STRING; 44689.Q54WS9; -. DR GlyGen; Q54WS9; 1 site. DR PaxDb; 44689-Q54WS9; -. DR GeneID; 8622044; -. DR KEGG; ddi:DDB_G0279461; -. DR dictyBase; DDB_G0279461; -. DR VEuPathDB; AmoebaDB:DDB_G0279461; -. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_298681_0_0_1; -. DR InParanoid; Q54WS9; -. DR PRO; PR:Q54WS9; -. DR Proteomes; UP000002195; Chromosome 3. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1. DR PANTHER; PTHR13832:SF534; PROTEIN PHOSPHATASE DDB_G0279461-RELATED; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. PE 3: Inferred from homology; KW Coiled coil; Hydrolase; Magnesium; Manganese; Metal-binding; KW Protein phosphatase; Reference proteome. FT CHAIN 1..1006 FT /note="Probable protein phosphatase DDB_G0279461" FT /id="PRO_0000369245" FT DOMAIN 744..1005 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 1..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 146..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 214..269 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 312..387 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 459..513 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 525..563 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 604..642 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 65..122 FT /evidence="ECO:0000255" FT COILED 450..516 FT /evidence="ECO:0000255" FT COMPBIAS 1..12 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 59..69 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 77..88 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 89..99 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 100..117 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 146..158 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..234 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 244..254 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 316..387 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 466..481 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..511 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 525..538 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 552..561 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 613..639 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 784 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 784 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 785 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 956 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 996 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 1006 AA; 111161 MW; 173B5733030E9B62 CRC64; MMVPSLSTSI SSPALFKNRE GGEEGNDGGL EQLQNQVNDL GDLNFNEEGD YNNDQQPTNE EEGTADNELE SLMSLVNDNN NNNNNTSGID DDNNNDIDDN NNNNNNNNNN NNNNNNNKEG LNDLFISSIN VSTLLNDLDQ LSDTHSHASV SNQSSNGSVR RGYDIKTQRS VGTKGQGGSS GSSPRSNSLR VYRTFPYRGD HHFSWLNNIR DVDSSEDPNS CHNSNNNNKN NKNNQPSSTH DQTNINNNNN NNCNDNEKPI KPNSTNGIRH SRKYKGLQQL DFLGSNIILP QQQQPQPIED NQQVVPQPFQ VDAESNYNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNDNE NNQHPINPVN TQNTQQNVTH SNNNNNNNNN NTAPPNQWSE LIESLGYGSQ SDEQKTFGST LDDLNNANSC SDLKDLIVDG ISINNETSPS QSQEITDFSK IDNLNKNINI NNNNNTDSQQ PLPSIDVNFS HNNNNNNNDN DNNNNNNNNN NNNNNNNNNN NIQDIQIPYH QNDQDYNIQE GNDINNDNYE IRVSNNDDDN DSSNNNNNNN SKFQENLNLL NTGMGGRICK TDQKKQLSRT ITFADPSSIL SFFGSIPTDE DQNNNNNKNK NTTTTTTTTN TTTTTTTTTS ASAAAQNKLD LLSSLSAGQS SGGVGGGNNV LNSSSTPAIK VNHQHKVTEQ NRTSSKISLS TIFPKLPPFT NQQSPPTLSP SKYYYPLLQP EPTTLIRGFS SAADINKRGL KRAKKPMEME DVYLTQYPLG DDQDSQIALF AIFDGHSGKG CAVAAKEIFP NILLKYIKST KNENGGKPIY DMRGVFLNAF KEVDAQLSKF EYEGATATVC LVWRAGHQRF VQSANVGDST AFLSYGNETL FLSKDHRATD PEEIQRIKND GITLTEGQTR INGLMVSRAL GDHFIKHLNC GLSGEPYVSP PISITPFHSH LIVASDGLWD VISGNRAMEI VKVQQTEEKM SNSLLQCAIG SIKAKDNISI IVVTLQ //