ID C5KTE6_PERM5 Unreviewed; 335 AA.
AC C5KTE6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=4-nitrophenylphosphatase, putative {ECO:0000313|EMBL:EER12251.1};
GN ORFNames=Pmar_PMAR001048 {ECO:0000313|EMBL:EER12251.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER12251.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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};
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DR EMBL; GG676168; EER12251.1; -; Genomic_DNA.
DR RefSeq; XP_002780456.1; XM_002780410.1.
DR AlphaFoldDB; C5KTE6; -.
DR EnsemblProtists; EER12251; EER12251; Pmar_PMAR001048.
DR GeneID; 9061417; -.
DR InParanoid; C5KTE6; -.
DR OMA; PPMHRET; -.
DR OrthoDB; 217676at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 NCBIfam; TIGR01460; HAD-SF-IIA; 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 Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 46
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 335 AA; 36817 MW; 9F994A869919F1C4 CRC64;
MSTLSSSSQT SASSHEDRLR AGTQISTSSE ARKFLDDHDV FIFDLDGCLY DGNITFDGVG
SLLKRLYDEH KDVWCFTNNS SKTRQQYVDK VTKMYPEVDG LFKEDRVLCS AYLTGLRLEQ
LGITRVYVLG TQNLVRELES RGITVVGGGE ADSGKAMDAE SLREINVDPT IQAVISGFDV
QINYYKLAYS SLCLQLIPGC KFIATNPDAQ IPVAKGALMA PGNLCIVRAL ATASGREPDC
FIAKPEPFAM QAAIRKAHPD TPSSRMVMVG DRIDTDIHFG LNSGIQSLLV CSGVTSEERA
IAASSGQEDR KDPCVWDYWC VDLSTMEHLL EQQDN
//
