ID   A0A1I7RIK2_BURXY        Unreviewed;       580 AA.
AC   A0A1I7RIK2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Histidine acid phosphatase {ECO:0000313|WBParaSite:BXY_0053400.1};
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_0053400.1};
RN   [1] {ECO:0000313|WBParaSite:BXY_0053400.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000032};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   AlphaFoldDB; A0A1I7RIK2; -.
DR   WBParaSite; BXY_0053400.1; BXY_0053400.1; BXY_0053400.
DR   eggNOG; KOG3720; Eukaryota.
DR   Proteomes; UP000095284; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..580
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009304244"
FT   TRANSMEM        427..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        458..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          55..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  65095 MW;  9D3BAE33639E2019 CRC64;
     MKLPLILFLI HWIGSGSPQE QDFIVTSSQT ATSFESSISS VASTTTSTTT VRSIGNFDPL
     SDDPIPRAPE GNPTTRQTGF TDEQLAGDQG DHGVGLETLS LETTLIHVHA IWRHGKRAPE
     WFPANTPFAE RESWPGGLNS LTTKGLQQCY RLGELLRERY TALLSGRYTP NKFYVRSSDT
     DRTILSAEAM MNGLVSDEDY GVADAKLKVF PVHTIRKDTD KLLNFNIECP AREEEQARVF
     NVADYGFPAL GQKTASFMRY IQNQTGENEL DYQAAYKVWD YLYYLEADER QLPSWATADA
     RENLEYINGK INQGLMMTPK LLRLRAGPIL KEMSERLRSI AKGSYLAAEK FYGYSAHDHT
     LAFLLKILGL NFERFPEPSS ALVFELHRRH DDEHFVKGCV DEKENRRMLN FLRKPPDPKE
     EDRRVQVFAL ILIVNLLIIG VCLVVWNGNA ISNVNITCAI LVIAALSGLC MLCCMSCLLF
     CVVTKEEADR KLDVQTVYPT PEFTYFNGTM LSRLNEENGK NAAFPGSVFS MLSTAPADSP
     AKTQSLETVS SSHSSHWPRP KPPVALSANH SNESDYLRLY
//