ID   X0CQQ8_FUSOX            Unreviewed;       478 AA.
AC   X0CQQ8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acid phosphatase {ECO:0000313|EMBL:EXK96770.1};
GN   ORFNames=FOQG_02195 {ECO:0000313|EMBL:EXK96770.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK96770.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK96770.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK96770.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; JH658364; EXK96770.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0CQQ8; -.
DR   eggNOG; ENOG502RCH9; Eukaryota.
DR   HOGENOM; CLU_023111_1_0_1; -.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   CDD; cd12087; TM_EGFR-like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF142; -; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..478
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004937171"
FT   TRANSMEM        427..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          458..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  52406 MW;  EBCEA20AC8C581E4 CRC64;
     MYCKALSLSL LFGNAASEVI HGAVVFSRHG DRTTKWYGAQ SLTSLGAEQN FQVGRDYRDR
     YLASDSQYRI LGISEDEYKP SQIFASAPDQ GILMNTATAF LQGFYPPLAD LDPEIASQTL
     NNGSESQAPL DGYQYVRLHT INDNSPDTIW IKGDDACPKY VTASKSFMKS DVFAQREEDT
     KEFYEQFYDV LSDGVYNLRP ENMTYKNAYN IFDLVNVARI HNSTSPARNV SNADLLQLRT
     LADSAELGQN WNKSDTARAI GAETLSGAIL NQLNETVTSQ GKLKFSLFAG SYDTFLAFFG
     LADLLDVSPN FYGLPDYAST MAFELFTDDN TDSFPSDPEA DLRVRWLFRN STAGDLETYP
     LFGTGEDSLS WSKFVTEIEK RAITDVGDWC TKCGAEEDFC AAYKDDDETA EGESENKTSK
     KGGMSNAVAG VIGAMVTLGV VAIVGAAAFV LLRRKRTTPA GEKSSVRSGS TDGNAAKV
//