ID A0A5C6PQE5_9TELE Unreviewed; 279 AA.
AC A0A5C6PQE5;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Putative phosphatase phospho1 {ECO:0000313|EMBL:TWW81874.1};
GN ORFNames=D4764_01G0016890 {ECO:0000313|EMBL:TWW81874.1};
OS Takifugu flavidus (sansaifugu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=433684 {ECO:0000313|EMBL:TWW81874.1, ECO:0000313|Proteomes:UP000324091};
RN [1] {ECO:0000313|EMBL:TWW81874.1, ECO:0000313|Proteomes:UP000324091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTHZ2018 {ECO:0000313|EMBL:TWW81874.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TWW81874.1};
RA Xiao S.;
RT "Chromosome genome assembly for Takifugu flavidus.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR031051-3};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC family. {ECO:0000256|ARBA:ARBA00008541}.
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:TWW81874.1}.
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DR EMBL; RHFK02000001; TWW81874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6PQE5; -.
DR Proteomes; UP000324091; Chromosome 1.
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; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016965; Pase_PHOSPHO-typ.
DR NCBIfam; TIGR01489; DKMTPPase-SF; 1.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR PANTHER; PTHR20889; PHOSPHATASE, ORPHAN 1, 2; 1.
DR PANTHER; PTHR20889:SF2; PHOSPHOETHANOLAMINE_PHOSPHOCHOLINE PHOSPHATASE; 1.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR031051-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR031051-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000324091}.
FT ACT_SITE 47
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ SEQUENCE 279 AA; 31831 MW; 59328D7C1D511960 CRC64;
MEFRSENGLV LDERAGTPTH THAIKMTASP HLGLAASHQK RFLVLFDFDE TIINESSDDA
VVRALPNQRL PDWLKNSYRD GHYNEFMQKV LTYMAEEGVS KESIQSAVEK ISPSPGLLNL
LEFLHSNQKH FELAVVSDAN MFFIETWLQH TGVRRLFWKI FTNPASFDDT GRLILLPFHS
HVCSRCPDNM CKQVIVREYL IGRQKERGGV PFQRVFYIGD GANDVCPSLA LGPRDTTFPR
RGFPMHVLLQ SEATFKANVV PWVRGEDIVD CLKKVVEER
//