ID   Y2105_DICDI             Reviewed;         958 AA.
AC   Q54T01;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Probable protein phosphatase DDB_G0282105;
DE            EC=3.1.3.16;
GN   ORFNames=DDB_G0282105;
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=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=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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PP2C family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000045; EAL66378.1; -; Genomic_DNA.
DR   RefSeq; XP_640354.1; XM_635262.1.
DR   AlphaFoldDB; Q54T01; -.
DR   SMR; Q54T01; -.
DR   STRING; 44689.Q54T01; -.
DR   PaxDb; 44689-DDB0235260; -.
DR   EnsemblProtists; EAL66378; EAL66378; DDB_G0282105.
DR   GeneID; 8623409; -.
DR   KEGG; ddi:DDB_G0282105; -.
DR   dictyBase; DDB_G0282105; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_308254_0_0_1; -.
DR   InParanoid; Q54T01; -.
DR   OMA; QNIGMIS; -.
DR   PRO; PR:Q54T01; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   CDD; cd00890; Prefoldin; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
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:SF873; PROTEIN PHOSPHATASE DDB_G0282105-RELATED; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW   Protein phosphatase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..958
FT                   /note="Probable protein phosphatase DDB_G0282105"
FT                   /id="PRO_0000369246"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          675..958
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          312..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          142..330
FT                   /evidence="ECO:0000255"
FT   COILED          613..666
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        312..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         722
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         722
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         723
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         905
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         949
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   958 AA;  106617 MW;  D5B23D9AB572162B CRC64;
     MVLMMDIKIM SAFSILFLSL MVSNEFLEFL ANTVYAAILF IIILFFYQNR QHFFTTSSSS
     KDSLTSTTTT TTTTSITSSL IQQQQEKEQQ QQLEQQQQQQ SIKLITKEIT IENDSEKNTS
     TTTSIITKEQ SPGSVRLIQN YSASQQSELT NTTIKQLQQK NQELQEQINN QIEKSRKDQL
     KYFNSNNKSQ SEIKEQIEKI IKLTEKNDDL LNSIVILNST IDGNRIKMQE ITKDRDSIYS
     SEQKLLSRLT AFEKKEKEYQ DNEKQLQKKL SDQKDQYSTL KKEFDEKVKK SNKLENSIQS
     LESQIQKLLQ KQEKEKQKLE KDKERERSSS FSSDISSSST TSTTASTFLS SSPSKSIPIP
     IPIKTSNAIS DLKRNNSNDS VNGLIGNGNS SVSPPSSSYL RESSDDSDNQ SSSSPSEPKF
     KSLFNKVKSE SSKIVNKAQK GINKHLGSDF FTPANTTTST TTTTSTTSTS TTTPITSASA
     TAAAISSSSI ITSPTTNTTN DILSSSSSSS SSSSSLLTTN AILSPPVGNE QQMEVINDKT
     EVNQSPVKPL IFFDDLGNDK LLDSTTEEQI QSKMTISPRD KDRILIDKEQ SLSDLFINSK
     ENISNISVSN LDNFLKTNNN NNKNNIEESN NNNNNNNNNN NNNNNNNNNN NNNNKNDNKE
     VNSKLEFSIK DEENKIGLRR AKKKLSPGCS TMMEDVSIAI YPFLKEKKLS NCSNIGLFGV
     FDGHAGRGAA DSASKLFPKE IEKLLESGNY SLTEQDDGGD NNHNQSKLLN DLFSNVDNKM
     KDHEYEGCTA TLALIWSDGE EQQQQQQRYL QVGNVGDSSA FLCRGNESIE LTFDHKANDP
     SEKQRIKDQG IPVSDNQTRI NGVAVSRSLG NHFIKEQNIG MISTPHISNR YLLTPQDKFV
     IIASDGLWDV INGKDAIEKV SSLYDQGATA DSMASCLLET AIQSSLCKDN VTVIIVKL
//