ID A0A0V1I7C4_9BILA Unreviewed; 322 AA.
AC A0A0V1I7C4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Lipid phosphate phosphohydrolase 1 {ECO:0000313|EMBL:KRZ18384.1};
DE Flags: Fragment;
GN Name=Ppap2a {ECO:0000313|EMBL:KRZ18384.1};
GN ORFNames=T11_3237 {ECO:0000313|EMBL:KRZ18384.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ18384.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ18384.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ18384.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ18384.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDP01000003; KRZ18384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1I7C4; -.
DR STRING; 268475.A0A0V1I7C4; -.
DR Proteomes; UP000055024; 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:SF103; FI04477P-RELATED; 1.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 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:KRZ18384.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..256
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT NON_TER 322
FT /evidence="ECO:0000313|EMBL:KRZ18384.1"
SQ SEQUENCE 322 AA; 36903 MW; 316A22091381174E CRC64;
MITYSPVQIS IHILLFGLVS LPILIFNKFV WPYRRGFYCD DESIRYPFKE STVSMTVLNL
IIFPVPILTI CLVEMYRVMK FEPATLSRPA EKVEVLFGYK LHPIFSRLYY YSGFFLLGAA
ATQTITDIGK YSIGRLRPHF LAICQPDIDL KSCAGHTYIE NFSCTNYDDW LSKDARLSFP
SGHSSLVAYG MLFIVMYLQI RVQWDIYNRL IKPFIQFIFI CLAIAIGLSR ISNYKHHWSD
VLCGLALGFF TASLLMGKEE IWHFGVTDDK STTGIEAGKD SVNLQTIQTN TNIDASRDLV
VLLQYRKTYR GISVTSCYAF HI
//
