ID A0A395RSW5_FUSSP Unreviewed; 708 AA.
AC A0A395RSW5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=FSPOR_8787 {ECO:0000313|EMBL:RGP63205.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP63205.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP63205.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP63205.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
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:RGP63205.1}.
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DR EMBL; PXOF01000135; RGP63205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RSW5; -.
DR STRING; 5514.A0A395RSW5; -.
DR Proteomes; UP000266152; 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; -; 2.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR014390; Acid_Pase_Asper.
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:SF159; PURPLE ACID PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR PIRSF; PIRSF000900; Acid_Ptase_Asper; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 18..708
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5017105097"
FT DOMAIN 87..177
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 486..562
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 591..654
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 708 AA; 78194 MW; 1FF5C2E0155EA946 CRC64;
MRSPYLLAAL LAAPAQSAPT VDETYPYRGP KIPIGDWVDP TINGNGKGFH RLVELPAVKP
ASANPSNNIN VISLSYIPAK HEHTTVGINI HYQTPFGLGV PPSVQWGTSA SALDNLATGL
STTYDRTPPC SLISIVTQCS QFFHNVQIEH LDPGTTYYYR IPAANGTTQS DVLSFTTAQA
KGDPSEFSIA INNDMGYTNA GGTHKYIKRA VEDGLAFVWH GGDLSYADDW YSGVVPCNSG
WPVCYNGSSS QLPNNTTNPD YSTPLPAGEI PNQGSPRGGD VSVLYESNWD LWQQWMNNIT
LKVPYIVLPG NHEATCADHD NPPYVLSAYL DEDIANGTSP TSSLNYYSCP PSQRNFTAFQ
KRFHMAGEKS GGVGNFWHSF DYGLAHFISI DTETDYAHSP DKTFVEDLEK AKQEEDCLGR
DKDLPKCKCK GKEKDTAECQ EEKCECKKIK MEDETDSVAE ETYLLSDKTH PLANMTHITD
AGPFGAIHGS YKDNKAYEQY QWVKKDLASV DRCKTPWIII MGHRPMYSSK CGDYHEHLRE
AFEKLFLKHK VDLYIAGHVH WYERLKPIRN CFVDNTAIVN NNTYKVNPGN SMVHLINGAA
GNIESHSTTN NKTMPDITAV RNLTSFGFSK LTVHNATTLS WEFIQGEDGL SGDSLTVLKD
RSSTCEVFDS SSSPGPSCSS ECSGSGSGWL LWLYCSISCS SFWNSLKH
//
