ID A0A6A5FE03_PERFL Unreviewed; 271 AA.
AC A0A6A5FE03;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Phosphatase phospho2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFLUV_G00027460 {ECO:0000313|EMBL:KAF1392400.1};
OS Perca fluviatilis (European perch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8168 {ECO:0000313|EMBL:KAF1392400.1, ECO:0000313|Proteomes:UP000465112};
RN [1] {ECO:0000313|EMBL:KAF1392400.1, ECO:0000313|Proteomes:UP000465112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:KAF1392400.1};
RA Roques C., Zahm M., Cabau C., Klopp C., Bouchez O., Donnadieu C., Kuhl H.,
RA Gislard M., Guendouz S., Journot L., Haffray P., Bestin A., Morvezen R.,
RA Feron R., Wen M., Jouanno E., Herpin A., Schartl M., Postlethwait J.,
RA Schaerlinger B., Chardard D., Lecocq T., Poncet C., Jaffrelo L.,
RA Lampietro C., Guiguen Y.;
RT "A chromosome-scale genome assembly of the European perch, Perca
RT fluviatilis.";
RL Submitted (JUN-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:KAF1392400.1}.
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DR EMBL; VHII01000003; KAF1392400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A5FE03; -.
DR OrthoDB; 372892at2759; -.
DR Proteomes; UP000465112; Chromosome 3.
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:SF1; PYRIDOXAL PHOSPHATE PHOSPHATASE PHOSPHO2; 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:UP000465112}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT ACT_SITE 38
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ SEQUENCE 271 AA; 30810 MW; 5B2B3179B2999C74 CRC64;
MLTSCKLPQQ DEEEDGERRT NVRQTGEKMK TLMVFDFDHT VIDDNSDTWV IRCLPGQTLP
DSVKNSYRKG HWTEFMGQVM NYIGEQQISP ERVRSVMETI PFTAGMTDLL TFISEHKSTI
DCIVISDSNT MFIEWILHAS GFKAAVDQVF TNPARFNELG HMEVRGHHSH DCDRCPVNLC
KRKVLEVYLS EQSDGGVEYE RVFYAGDGGN DLCPTSCLRG RDVVMPRKGY TLEKLLARLE
QREDNASLRA KVVAWSSGTD ILEELKASMQ S
//