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Database: UniProt
Entry: A0A016WRI6_9BILA
LinkDB: A0A016WRI6_9BILA
Original site: A0A016WRI6_9BILA 
ID   A0A016WRI6_9BILA        Unreviewed;       201 AA.
AC   A0A016WRI6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|Pfam:PF01569};
GN   Name=Acey_s0531.g3013 {ECO:0000313|EMBL:EYC42424.1};
GN   Synonyms=Acey-T28D9.3 {ECO:0000313|EMBL:EYC42424.1};
GN   ORFNames=Y032_0531g3013 {ECO:0000313|EMBL:EYC42424.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC42424.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYC42424.1}.
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DR   EMBL; JARK01000131; EYC42424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016WRI6; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR043216; PA_PP_rel.
DR   PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF203; PHOSPHOLIPID PHOSPHATASE HOMOLOG 1.2 HOMOLOG; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          119..198
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01569"
SQ   SEQUENCE   201 AA;  22456 MW;  43FEA34F8E04A0DB CRC64;
     MEEPVLGSNS EKVINGYAFL ADTILLIGFG LIGGFLIPSI TGTFHRGFFC NDQSIQYPYK
     NDTVTPTVLF LYSFLAMILT IIATEFYRAK KSTRVSTPYH RIGNTSIHFV VVKIITYIGY
     SLIGFMCVLV LTNITKSCVG RLRPHFLDVC KPINITCHSD EYYNNYTCSG DPVKVEEARK
     SFFSGHSSIS MYASTFTAVS D
//
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