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Database: UniProt
Entry: A0A2V5I7F7_9EURO
LinkDB: A0A2V5I7F7_9EURO
Original site: A0A2V5I7F7_9EURO 
ID   A0A2V5I7F7_9EURO        Unreviewed;       500 AA.
AC   A0A2V5I7F7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE            EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN   ORFNames=BP00DRAFT_471986 {ECO:0000313|EMBL:PYI32705.1};
OS   Aspergillus indologenus CBS 114.80.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI32705.1, ECO:0000313|Proteomes:UP000248817};
RN   [1] {ECO:0000313|EMBL:PYI32705.1, ECO:0000313|Proteomes:UP000248817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI32705.1,
RC   ECO:0000313|Proteomes:UP000248817};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|RuleBase:RU361203};
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC       acid phosphatase family. {ECO:0000256|RuleBase:RU361203}.
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DR   EMBL; KZ825490; PYI32705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5I7F7; -.
DR   Proteomes; UP000248817; Unassembled WGS sequence.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd00839; MPP_PAPs; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041792; MPP_PAP.
DR   InterPro; IPR039331; PPA-like.
DR   InterPro; IPR008963; Purple_acid_Pase-like_N.
DR   InterPro; IPR015914; Purple_acid_Pase_N.
DR   InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR   PANTHER; PTHR22953; ACID PHOSPHATASE RELATED; 1.
DR   PANTHER; PTHR22953:SF156; PURPLE ACID PHOSPHATASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF14008; Metallophos_C; 1.
DR   Pfam; PF16656; Pur_ac_phosph_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361203};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361203"
FT   CHAIN           21..500
FT                   /note="Purple acid phosphatase"
FT                   /evidence="ECO:0000256|RuleBase:RU361203"
FT                   /id="PRO_5016476834"
FT   DOMAIN          33..114
FT                   /note="Purple acid phosphatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16656"
FT   DOMAIN          178..403
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          425..486
FT                   /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14008"
FT   REGION          317..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  54783 MW;  E113DC475F9CEF0E CRC64;
     MMHQSTLLKG LPWLAVAALA VDYPTLPNDL TTPYQQRLAI MGPTAVSIGW NTYEKLNSSC
     VEYGTSSNDL SQQACSTKST TYATSRTYSN AVTLTGLTPA TTYYYRIVSG NSTVERFLSP
     RTPGDTTPFN FDVVIDLGVY GADGYTISSD SSTSKRETPY VEPDLNHTTI GRMADTFDDY
     ELVIHPGDFA YADDWYLKLK NLLDGKDAYQ AILEQFYDQL APIAAGKPYM VSPGNHEADC
     DELSLLIDLC PEGQRNFTDF MHRFDETMPS AFASSSTNTS AQSLAATART LSNPPFWYSF
     EYGMVHFTMI DTETDFTDAP DGPDGSAELD GGPFGQPQQQ LEFLEADLAS VDRSVTPWVI
     VAGHRPWYST GGSSNICDAC QEAFEDLLYK YGVDLGVFGH VHNSQRFQPV YNGTADANGL
     NDPAAPMYIV AGGAGNIEGL SSVGSEPSYT AFVYADDYSY STVRVLNETH LQVDFIRSET
     GAVLDSSVLY KSHTEQFVVQ
//
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