Y2105_DICDI
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 03-AUG-2022, entry version 93.
DE RecName: Full=Probable protein phosphatase DDB_G0282105;
DE EC=3.1.3.16;
GN ORFNames=DDB_G0282105;
OS Dictyostelium discoideum (Slime mold).
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.DDB0235260; -.
DR PaxDb; Q54T01; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 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
