ID   A0A091GJR8_9AVES        Unreviewed;       227 AA.
AC   A0A091GJR8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Lipid phosphate phosphohydrolase 3 {ECO:0000313|EMBL:KFO82218.1};
DE   Flags: Fragment;
GN   ORFNames=N303_09404 {ECO:0000313|EMBL:KFO82218.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO82218.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO82218.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO82218.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   EMBL; KL448309; KFO82218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091GJR8; -.
DR   STRING; 55661.A0A091GJR8; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd03384; PAP2_wunen; 1.
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:SF79; PHOSPHOLIPID PHOSPHATASE 3; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KFO82218.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          85..227
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO82218.1"
FT   NON_TER         227
FT                   /evidence="ECO:0000313|EMBL:KFO82218.1"
SQ   SEQUENCE   227 AA;  25594 MW;  7F7AF212C8218443 CRC64;
     AALPFLIIET STIQPYQRGF YCDDDSIRYP LKTMETINDA VLCAAGILIA ILAIITGELY
     RIHYLKEKSH SFIQNPYVAA LYKQVGCFVF GCAISQSFTD IAKVSVGRLR PHFLEVCNLD
     FSTINCTKGV YIQNYTCRGS DSKVQEARKS FFSGHASFSL YTMLYLVFYL QARFTWKGAR
     LLRPLLQFTL IMMAFYTGLS RVSDHKHHPT DVLAGFAQGA LVAYCVV
//