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Database: UniProt
Entry: A0A225WUG7_9STRA
LinkDB: A0A225WUG7_9STRA
Original site: A0A225WUG7_9STRA 
ID   A0A225WUG7_9STRA        Unreviewed;       303 AA.
AC   A0A225WUG7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=4-nitrophenylphosphatase {ECO:0000313|EMBL:OWZ20707.1};
GN   ORFNames=PHMEG_0004843 {ECO:0000313|EMBL:OWZ20707.1};
OS   Phytophthora megakarya.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ20707.1, ECO:0000313|Proteomes:UP000198211};
RN   [1] {ECO:0000313|Proteomes:UP000198211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA   Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA   Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT   "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT   of cacao black pod achieved similar genome size and gene model numbers by
RT   different mechanisms.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC       Note=Divalent metal ions. Mg(2+) is the most effective.
CC       {ECO:0000256|PIRSR:PIRSR000915-3};
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:OWZ20707.1}.
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DR   EMBL; NBNE01000297; OWZ20707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225WUG7; -.
DR   STRING; 4795.A0A225WUG7; -.
DR   EnsemblProtists; OWZ20707; OWZ20707; PHMEG_0004843.
DR   OrthoDB; 217676at2759; -.
DR   Proteomes; UP000198211; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006349; PGP_euk.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR   NCBIfam; TIGR01452; PGP_euk; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF46; HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198211}.
FT   ACT_SITE        29
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        31
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         31
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   303 AA;  33069 MW;  4EDCE60D50590797 CRC64;
     MATTKSVTQR LTRESFKQWI QGLDAFLFDC DGVLWRGAAP IEGAANMITL LRLLNKRVVF
     VTNNATNSRA TYVKKLASQG ITAVEGDIVT SAWATVQYMK QHKIEGKVYM VGEEGLKTEL
     ELEGYQVSGM EHSDIKGLPH IPDIDVETKA VVCGLDRYFT YYKMAYATAC VRQIPGCRFI
     GTNPDQTFPT DGAIVPGGGS LVHMLECAIG HPPEAVCGKP SQDLLQTIIA TYNLNPARTC
     MVGDRLSTDI EFGNAGGLST LLVLTGITSE SELSSIDNDV HVPNYYIDSV DVINQLHAET
     LEN
//
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