ID   Y4753_DICDI             Reviewed;         464 AA.
AC   Q54P72;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Probable acid phosphatase DDB_G0284753;
DE            EC=3.1.3.2;
GN   ORFNames=DDB_G0284753;
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=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase 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; AAFI02000071; EAL65029.1; -; Genomic_DNA.
DR   RefSeq; XP_638386.1; XM_633294.1.
DR   AlphaFoldDB; Q54P72; -.
DR   SMR; Q54P72; -.
DR   STRING; 44689.DDB0186172; -.
DR   PaxDb; Q54P72; -.
DR   PRIDE; Q54P72; -.
DR   EnsemblProtists; EAL65029; EAL65029; DDB_G0284753.
DR   GeneID; 8624755; -.
DR   KEGG; ddi:DDB_G0284753; -.
DR   dictyBase; DDB_G0284753; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   HOGENOM; CLU_030431_5_0_1; -.
DR   InParanoid; Q54P72; -.
DR   OMA; FRTEDDM; -.
DR   PhylomeDB; Q54P72; -.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   PRO; PR:Q54P72; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..464
FT                   /note="Probable acid phosphatase DDB_G0284753"
FT                   /id="PRO_0000369256"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        347
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  53626 MW;  90176186B58DFB51 CRC64;
     MFSYFRKSQQ KVEENQNGGG GDGRGSGIKV ELQTNINSRD LKNEHSDPKF KFSPLRSTDV
     HLEDYDNEKY KLKFIQIVTR HGRRTPESNR TPLTMWMCNS MDHLISNKDS PRPNCNPGQL
     TVLGIVDQIN VGKIYRKLFI DHLGFLDSQY NKDQIFIRST NTTRTISSAR SLMHGLYGGS
     FTDEQEKSPH HSSFLVKPDN EENMYPRNSK KLVFLKNLIK QHPKVIKENQ LSELEKFTEK
     INKIFENSKP EESSFRARGF RSYAGLVNSF DCFRNNGLPI PKGLTKDIIQ RMYEESAKEF
     KSARYFPEMS ILGIGRFVDD LNKELKLKAR NDPSVKDLKL SLYSGHDTTL AALLVGYDMY
     EDKIHPVTSS TLEFLLMQDK DYKEPEVVKI TKSIEKELIN HQYVKVIYNH KPIHIGPCKD
     KEVDGMCPLS EFLKISQSII PTNYDEQSKL TQLDKKRYLS LIED