ID   A0A1E3HMX0_9TREE        Unreviewed;       489 AA.
AC   A0A1E3HMX0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L202_04839 {ECO:0000313|EMBL:ODN77692.1};
OS   Cryptococcus amylolentus CBS 6039.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN77692.1, ECO:0000313|Proteomes:UP000094065};
RN   [1] {ECO:0000313|EMBL:ODN77692.1, ECO:0000313|Proteomes:UP000094065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN77692.1,
RC   ECO:0000313|Proteomes:UP000094065};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODN77692.1}.
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DR   EMBL; AWGJ01000007; ODN77692.1; -; Genomic_DNA.
DR   RefSeq; XP_018992928.1; XM_019138985.1.
DR   AlphaFoldDB; A0A1E3HMX0; -.
DR   STRING; 1295533.A0A1E3HMX0; -.
DR   GeneID; 30156148; -.
DR   OrthoDB; 2404758at2759; -.
DR   Proteomes; UP000094065; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd07061; HP_HAP_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   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF12; ENDOCYTOSIS PROTEIN 3; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094065}.
FT   REGION          328..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        51..432
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        267..280
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        454..462
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   489 AA;  55446 MW;  FDE35E95788C418B CRC64;
     MLWQLLVLPL AVASPSQTPF APKHINPLKH LSAISPFFIP NQEPTPLPPT CEYTRISLLV
     RHTSIQGNDD EYEDTMEPFI EKIKAMDKNK MPSDGEWAFL RNWESPISED VLEKVSQRGE
     DDSTFFGRRL STQYAKLFPP REKSEKTKKK SKHTVPFKVW SASSERDIVT AKAWIKGAFP
     AAQAGPHGEG DGKQLQLVSV PNKAKDWDRS LTPHKACDAF EKQSSLEPAR VWLKTYAPPI
     RERLSQIIPD VAVELVDDDI LAMQMLCGYE TISQGWSPFC NLFTDNEWLD GEYYFDVRFH
     YMMGYGNHLS PYLGAPWVKT AKHLLDGKDT GDGAGEPHGD EGEVEANKEK HKLPKPNLPP
     NATHTQLFHP SFTHRESPAF VATFLNLYNS TYAHPASLSP PLTYRPPKSE RAWRTSHVVS
     FLGHVALERF HCGEDGGDYV RAKVNGKQEK MGGCEDGLEG SCRWETFYKW VDERALRWSG
     WEEVCAKKD
//