CTDS_DICDI
ID CTDS_DICDI Reviewed; 306 AA.
AC Q9XYL0; Q54AK8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable C-terminal domain small phosphatase;
DE EC=3.1.3.16;
DE AltName: Full=Developmental gene 1148 protein;
GN Name=fcpA; Synonyms=ctdsp, DG1148; ORFNames=DDB_G0294376;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX4;
RA Iranfar N., Loomis W.F.;
RT "Dictyostelium discoideum Developmental gene DG1148. Disruption of this
RT gene results in morphological defect.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 -!- FUNCTION: May function as a phosphatase involved in the regulation of
CC cell growth and differentiation. {ECO:0000250}.
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 Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AF111941; AAD28548.1; -; Genomic_DNA.
DR EMBL; AAFI02000259; EAL60295.1; -; Genomic_DNA.
DR RefSeq; XP_628708.1; XM_628706.1.
DR AlphaFoldDB; Q9XYL0; -.
DR SMR; Q9XYL0; -.
DR STRING; 44689.DDB0229894; -.
DR PaxDb; Q9XYL0; -.
DR EnsemblProtists; EAL60295; EAL60295; DDB_G0294376.
DR GeneID; 3385372; -.
DR KEGG; ddi:DDB_G0294376; -.
DR dictyBase; DDB_G0294376; fcpA.
DR eggNOG; KOG1605; Eukaryota.
DR HOGENOM; CLU_020262_4_0_1; -.
DR InParanoid; Q9XYL0; -.
DR OMA; MYANTNT; -.
DR PhylomeDB; Q9XYL0; -.
DR PRO; PR:Q9XYL0; -.
DR Proteomes; UP000002195; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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 GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IEP:dictyBase.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..306
FT /note="Probable C-terminal domain small phosphatase"
FT /id="PRO_0000328057"
FT DOMAIN 132..290
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 198
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 236
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 306 AA; 35116 MW; 9D9A7C7BD2844099 CRC64;
MNSSPITQVS NPNDSLNHSS TNLIPSSHNS LNNYPQKSVK GNRKKKGSII NKLFCCFVPS
NDQNNGNNIN TDNGASNNDK LQQQKQYNQQ QQQQYNQHQQ QQQQQQQQQQ YINKDSSQQN
GEIPLMVPMI PRHVGLKTLV LDLDETLVHS SFKPVHNPDF IVPVEIEGTI HQVYVVKRPF
VDDFLRAIAE KFEIVVFTAS LAKYADPVLD FLDTGRVIHY RLFRESCHNH KGNYVKDLSR
LGRDLKSTII VDNSPSSYLF HPENAIPIDS WFDDKDDREL LDLLPLLDDL IKVEDVRLVL
DESRNN
