ID A0A1I7RP27_BURXY Unreviewed; 349 AA.
AC A0A1I7RP27;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=(pine wood nematode) hypothetical protein {ECO:0000313|EMBL:CAD5232300.1};
GN ORFNames=BXYJ_LOCUS12391 {ECO:0000313|EMBL:CAD5232300.1};
OS Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS xylophilus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0246700.1};
RN [1] {ECO:0000313|WBParaSite:BXY_0246700.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:CAG9124484.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ka4C1 {ECO:0000313|EMBL:CAD5232300.1};
RA Kikuchi T.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CAJFDI010000005; CAD5232300.1; -; Genomic_DNA.
DR EMBL; CAJFCV020000005; CAG9124484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7RP27; -.
DR WBParaSite; BXY_0246700.1; BXY_0246700.1; BXY_0246700.
DR eggNOG; KOG2882; Eukaryota.
DR Proteomes; UP000095284; Unplaced.
DR Proteomes; UP000582659; Unassembled WGS sequence.
DR Proteomes; UP000659654; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000659654}.
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 57
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 349 AA; 38856 MW; 5F428FC023EDD94F CRC64;
MPPIGLSIAE CEQLKSRVFD DFQNEPTLQK RTISTFMDST SFKSLVKEID TFIFDADGVL
WLGEDAIPGS PAFIEYLIRL KKRIIILTNN ATKSRAVYAK KLAKLGYNES VSNKNTIVNP
AAVVADTLHR SGIKDSNKKV YLIGGQGVKD ELTELDIEYF GDGPDPIENQ ESSKGAAFLY
DIELEEEVNQ VGAVVVGYEK HFNYLKLMKA ANYLQEGDCL FVATNEDETC PGPNPNTIIP
DAGPLVAAVK TASGRDPLVV GKPNTPAFEY IQRRWNVDPS RTMMIGDRTN TDVKFGRDHG
LRTMLVLSGC HQVEDIQENF ENQRLDMVPD FYAKNLGSLV PKRPTTAYY
//
