ID   A0A1I8BR85_MELHA        Unreviewed;       369 AA.
AC   A0A1I8BR85;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:MhA1_Contig499.frz3.gene1};
OS   Meloidogyne hapla (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig499.frz3.gene1};
RN   [1] {ECO:0000313|WBParaSite:MhA1_Contig499.frz3.gene1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   AlphaFoldDB; A0A1I8BR85; -.
DR   WBParaSite; MhA1_Contig499.frz3.gene1; MhA1_Contig499.frz3.gene1; MhA1_Contig499.frz3.gene1.
DR   OMA; CNIDRTY; -.
DR   Proteomes; UP000095281; Unplaced.
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; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006349; PGP_euk.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR   NCBIfam; TIGR01452; PGP_euk; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF83; PHOSPHOGLYCOLATE PHOSPHATASE HOMOLOG; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3}.
FT   ACT_SITE        58
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        60
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         60
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   369 AA;  40788 MW;  1A39089CCCF891CE CRC64;
     MPAYNDEIFN NTNIEQNVLP KLVVFETDTP VPKIKKSRKI DSQKSSELFK NIDTFIFDAD
     GVLWLGENAI SGSPSFIEHV AKLGKRIIVL TNNATKSRAV YAKKLAGLGY GRYINEHNIV
     NPAAVVADVI HRSDLARHGK KVYLIGSQGV KDELKLLNIE YFGDGIDPVD AQPASKGQAF
     LYELELEEHP ENVGAVVVGY EKYFNYLKLM KAANYLQNED CLFLATNEDE TCPGPNPETI
     IPDAGPLVAA VKTACGREPL TVGKPNSPAF EYICRRWGVD SIDPSRTLMI GDRVNTDVKF
     GRDHGLRTLL VLSGCHGLDE IEDGILQSRE DLVPEFYADS LGSLIPPKEK INKKNKAEEG
     GERRKAVCV
//