ID A0A4W4EFN6_ELEEL Unreviewed; 242 AA.
AC A0A4W4EFN6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Phosphatase, orphan 2 {ECO:0000313|Ensembl:ENSEEEP00000009799.1};
GN Name=phospho2 {ECO:0000313|Ensembl:ENSEEEP00000009799.1};
OS Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000009799.1, ECO:0000313|Proteomes:UP000314983};
RN [1] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24970089;
RA Gallant J.R., Traeger L.L., Volkening J.D., Moffett H., Chen P.H.,
RA Novina C.D., Phillips G.N.Jr., Anand R., Wells G.B., Pinch M., Guth R.,
RA Unguez G.A., Albert J.S., Zakon H.H., Samanta M.P., Sussman M.R.;
RT "Nonhuman genetics. Genomic basis for the convergent evolution of electric
RT organs.";
RL Science 344:1522-1525(2014).
RN [2] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28695212;
RA Traeger L.L., Sabat G., Barrett-Wilt G.A., Wells G.B., Sussman M.R.;
RT "A tail of two voltages: Proteomic comparison of the three electric organs
RT of the electric eel.";
RL Sci. Adv. 3:e1700523-e1700523(2017).
RN [3] {ECO:0000313|Ensembl:ENSEEEP00000009799.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A4W4EFN6; -.
DR STRING; 8005.ENSEEEP00000009799; -.
DR Ensembl; ENSEEET00000009918.1; ENSEEEP00000009799.1; ENSEEEG00000004987.1.
DR GeneTree; ENSGT00390000007741; -.
DR OMA; HNLADCF; -.
DR Proteomes; UP000314983; 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; 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:UP000314983}.
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ SEQUENCE 242 AA; 27324 MW; 1C233F73B56CC820 CRC64;
MAKIKTLIVF DFDHTLVDSN SDLWVVQCAP GQRLPDWLKS SYETGRWTEY MGRVLAYLGE
QSVHPEDIRT VMETIPFTDG MVELLTFISQ NKNVIDCIIV SDSNTLFIDW ILQSGGVKSA
IDCVFTNPAS INERNYIEVQ CFHSHGCEHC PVNLCKQKVL SDFREMQASS SVHYQAICYV
GDGANDLCPI KILKEGDIAM PRRGYSLEKL VSKTKTENNT LKARIVPWSS GMEILEELHA
LL
//
