ID   A0A1Y2VP14_9PEZI        Unreviewed;       482 AA.
AC   A0A1Y2VP14;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M426DRAFT_325223 {ECO:0000313|EMBL:OTA99359.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTA99359.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTA99359.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTA99359.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR   EMBL; KZ111625; OTA99359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VP14; -.
DR   STRING; 1001833.A0A1Y2VP14; -.
DR   InParanoid; A0A1Y2VP14; -.
DR   OrthoDB; 2404758at2759; -.
DR   Proteomes; UP000242955; 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:SF14; ACID PHOSPHATASE, PUTATIVE-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   Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..482
FT                   /note="Acid phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012101722"
FT   DISULFID        62..387
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        251..264
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        413..421
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   482 AA;  52874 MW;  3839C0409510319C CRC64;
     MASSFVTELL PFAALLLGVA QPVDAASLYS TYKFNPLEHL GGVAPYFEPQ DPTTSPSAPQ
     GCTASRAVYL SRHAAIYAND YDYEAYIDPF VSKLENNTGA VDWTKVPALS FLADWTAPLS
     DAESELLTRV GKLEAAQLGV TLSFRYPNLK LPSRIWTSSA ERTVKSAQSL ARGLELDENE
     INVVSIYESE EAGANSLTPY KSCPAYSSSF GSDQSAVYLQ KFTDPITARL NAAAPGFNFT
     ADDVYGMMEL CGYESVIRGS SPFCDLDLFS PDDWLGWEYT ADVMYHYNVG YGNRISGFVG
     LPWFNASANL LLGDSTDEQD LFVSFTHREL PPMVFVAMGL FNNSEFGGTE AGINDTMPLD
     RINHRRAWKS SHLLPFLSNL AIERLNCSGS YGYEDGDYYR VLVNSAPQPL PSCADGPGTT
     CSRAGFEQYI QERADLFQGY SENCGVDYDN STDTLTIYSD TSVGNGTAVG KRYEAFQSRL
     DN
//