ID   A0A0D2IM33_9EURO        Unreviewed;       505 AA.
AC   A0A0D2IM33;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=3-phytase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z520_06156 {ECO:0000313|EMBL:KIX98076.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX98076.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX98076.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX98076.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN848072; KIX98076.1; -; Genomic_DNA.
DR   RefSeq; XP_016632199.1; XM_016776657.1.
DR   AlphaFoldDB; A0A0D2IM33; -.
DR   STRING; 1442371.A0A0D2IM33; -.
DR   GeneID; 27711902; -.
DR   VEuPathDB; FungiDB:Z520_06156; -.
DR   OrthoDB; 2404758at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF18; ACID PHOSPHATASE PHO11-RELATED; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        108
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   ACT_SITE        373
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   DISULFID        97..425
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        300..313
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   505 AA;  56928 MW;  3833E4A41C5CA696 CRC64;
     MRSTTFKLTR DRGSRRLYRQ KLVLFILILF AALLAFPLLR HVQNDTCSAS PFLLRAGLCS
     TAFHALWNLL HHLGGNGPWI RKIDSVNYYD SPLPKKCSID QVHMLSRHAE RYPTKSAGFR
     HVDLLGRLQG SGVNLTGSLS FLKEWTYFTD LSNPAFENLT ATGPYAGTRQ AANTGRILRQ
     RYNHLVADGR RTNFWSCSSP RDVETAEHFA NGFFGPDWKS DGSAELVIIP EDEDRGANTL
     TPGDTCLNYR DDKVHGHDHG YAKLAEWQST FSQAIAERLA NDAEGMIFKP LEIYGMMEMC
     GFEILARGKS PWCDVFEQHE WLEFEYARDL LHYYRAGPGN KFGAVLGWLW LNATQQLMSN
     HSSKDVYFSF VHDGDIIPAL ATLGIFNEPL ELSHLPTDRL LTERKWKTSD VVPMGGRLIF
     ERITCATNGD ITTSGREHAV RLFINDGLVD LAKLTDMVPF SQVEGAVSLE SFQNTLSAKG
     TQLGDFREIC ALPDDAPDRI DFLHQ
//