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Database: UniProt
Entry: A0A0N4X245_HAEPC
LinkDB: A0A0N4X245_HAEPC
Original site: A0A0N4X245_HAEPC 
ID   A0A0N4X245_HAEPC        Unreviewed;       434 AA.
AC   A0A0N4X245;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647};
DE            EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647};
GN   ORFNames=HPLM_LOCUS18413 {ECO:0000313|EMBL:VDO70919.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001842101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0001842101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO70919.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO70919.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC       Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC       {ECO:0000256|RuleBase:RU003946}.
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DR   EMBL; UZAF01020558; VDO70919.1; -; Genomic_DNA.
DR   STRING; 6290.A0A0N4X245; -.
DR   WBParaSite; HPLM_0001842101-mRNA-1; HPLM_0001842101-mRNA-1; HPLM_0001842101.
DR   OMA; ISIRIFW; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; Unassembled WGS sequence.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00022622};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..434
FT                   /note="alkaline phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041041635"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         391
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   434 AA;  49098 MW;  81FABC0330A4CFD8 CRC64;
     MSLWVLNLLC LLRIPTVASS KNVESSDRYD LDDIRFWNSI GRRNIEKKLQ LNPHLLKSGL
     RRIKVTSSLD RHVTDSAASA MALFTGRKGV VRNAEYDEAE VHCARDIAKQ LLSYPASEFK
     VLMGGGRRCL MNKSRNGSRG DGRNIDLEWL RLGGSRKVLR TPSDLNQIDA ANVDKLLGKN
     SIPFKIKTER AADVFTYARP FKKKATGIFS DSHFPYYLEE RLRNKKTVPR LHEMTKKAIE
     VLQKDDQGFF LMVEGGLIDQ AQHGNSMHVT FSEMYEFEKA IRVAREMTNP NETLIIVTAD
     HGHAFTLPGY LHAKQSLFEE ISVTKGNYLE SSRVVHRGGN TVDRVENWLP TLFFAVGPGY
     RNGFKEHPSS SEIGRPFYRH PTPVPARTGY HGGEDVGIWA DGPFSEQVFL VLFGLISIRI
     FWKAIYIGLA PDQN
//
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