ID   A0A423WKP9_9PEZI        Unreviewed;       477 AA.
AC   A0A423WKP9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VPNG_07293 {ECO:0000313|EMBL:ROW03891.1};
OS   Cytospora leucostoma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX   NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW03891.1, ECO:0000313|Proteomes:UP000285146};
RN   [1] {ECO:0000313|EMBL:ROW03891.1, ECO:0000313|Proteomes:UP000285146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYLt {ECO:0000313|EMBL:ROW03891.1,
RC   ECO:0000313|Proteomes:UP000285146};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) 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:ROW03891.1}.
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DR   EMBL; LKEB01000048; ROW03891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423WKP9; -.
DR   STRING; 1230097.A0A423WKP9; -.
DR   InParanoid; A0A423WKP9; -.
DR   Proteomes; UP000285146; 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:UP000285146};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..477
FT                   /note="Acid phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019007531"
FT   DISULFID        55..383
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        245..258
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        409..417
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   477 AA;  51999 MW;  C1D3093B1259E14D CRC64;
     MSSKAAALLV LPGLATALAP LYSSYTFNPL EHLGGVAPYF EPVDPQTDPA PPQGCTPVRA
     AYLVRHAAIY ANDFDYEEYI SPFISKFQNK TDVNWSTIPS LSFLASWSPP VSEAEEELLT
     RVGKLEATQL GASLSFRYSN LNLPKRVWSS SAERTYESAK ALIRGFEPAG DDNTIDLVSV
     YENKKGGANS LTPYSACPKY SGSAGSDQSA VYLDKFTRPI IARLNAAAPA FNFTADDVYG
     MMELCGYETV IKGSSKFCDT SLFTPDDWLG WEYTADVQYH YNVGYGSEVS GPIGLPWVNA
     TAGLLTADAD DADVQDLYVS FTHRELPPTV LVAMGLFNNS AFGGSEATIN DTMPLDTINH
     RRAWKSSHVL PFMTNVAMER LNCSGSHGYD DGDYYRVLVN NAPQPLPDCG DGPGTTCSRA
     TFDGWVRDRA DLFSGYSEKC GTAEEYDNST DVLTIYTDST TTGNGSFVGK RSLWDQE
//