ID A0A4U5VNL3_COLLU Unreviewed; 259 AA.
AC A0A4U5VNL3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Putative phosphatase phospho1 {ECO:0000313|EMBL:TKS89641.1};
GN ORFNames=D9C73_023769 {ECO:0000313|EMBL:TKS89641.1};
OS Collichthys lucidus (Big head croaker) (Sciaena lucida).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Collichthys.
OX NCBI_TaxID=240159 {ECO:0000313|EMBL:TKS89641.1, ECO:0000313|Proteomes:UP000298787};
RN [1] {ECO:0000313|EMBL:TKS89641.1, ECO:0000313|Proteomes:UP000298787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JT15FE1705JMU {ECO:0000313|EMBL:TKS89641.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TKS89641.1};
RA Cai M., Xiao S.;
RT "Genome Assembly of Collichthys lucidus.";
RL Submitted (JAN-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM014098; TKS89641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5VNL3; -.
DR STRING; 240159.A0A4U5VNL3; -.
DR Proteomes; UP000298787; Chromosome 21.
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:UP000298787}.
FT ACT_SITE 22
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT ACT_SITE 24
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ SEQUENCE 259 AA; 29468 MW; BA5E6B469C5E5748 CRC64;
MTALSNQTNA APQQQRFLVL FDFDETIINE SSDDAVVRAL PGQQLPDWLK NSYREGHYNE
HMQKVLVYMA EQGVSKDSIR SAVEKIPPSP GLLNLFQYLQ SHQQDFELAV VSDANMYFIE
TWLEHAGVRH LFRKIFTNPA SFDASGRLVL LPFHSHSCSC CPDNMCKQVI LREYLAGRQK
DRGGAPFQRV FYIGDGANDI CPSLALAPQD TAFPRRDFPM HRLLMNMQQS QGAKFKANIV
PWVSGEDIVD CLKKIMKER
//
