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Database: UniProt
Entry: S8E9J2_9LAMI
LinkDB: S8E9J2_9LAMI
Original site: S8E9J2_9LAMI 
ID   S8E9J2_9LAMI            Unreviewed;       314 AA.
AC   S8E9J2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
DE   Flags: Fragment;
GN   ORFNames=M569_02216 {ECO:0000313|EMBL:EPS72538.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS72538.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS72538.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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:EPS72538.1}.
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DR   EMBL; AUSU01000795; EPS72538.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8E9J2; -.
DR   OrthoDB; 25293at2759; -.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd03390; PAP2_containing_1_like; 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:SF35; RE23632P; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          150..290
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   NON_TER         314
FT                   /evidence="ECO:0000313|EMBL:EPS72538.1"
SQ   SEQUENCE   314 AA;  35912 MW;  C8F201F96B28D335 CRC64;
     MPWPDFRSVF RSINSTISFV SENRNSFERT GDSPSHVQSP LIGFEVLQSD MQETQLGRHT
     LRSHGIKLAR KHKHDWLILL LLGIFLHILS LISPYHRFVG KDMISDLKYP MKTNTVPFWF
     VTAFSVLFPT AVSLLFYLRQ RNVYDLHHSI LGLLFSVLVT EAITDVIKVA VGRPRPDFFW
     RCFPDGKDAY DQWGNVVCHG DPEIIKQGHK SFPSGHTAFA FAGLGFLSLY LSAKIRLFDR
     RGHISKLCVP LLPLLAASLI GISRLCNYKH HWQDVLTGGF LGFVVATLSY LQFFPPPYHP
     QGFMTHEYLH LTDQ
//
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