ID   A0A0N4ZC44_PARTI        Unreviewed;       447 AA.
AC   A0A0N4ZC44;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=PlsC domain-containing protein {ECO:0000313|WBParaSite:PTRK_0000509900.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000509900.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000509900.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   AlphaFoldDB; A0A0N4ZC44; -.
DR   STRING; 131310.A0A0N4ZC44; -.
DR   WBParaSite; PTRK_0000509900.1; PTRK_0000509900.1; PTRK_0000509900.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR   InterPro; IPR045252; LPCAT1-like.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR23063:SF6; PLSC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        107..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..308
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   447 AA;  51643 MW;  2057325101BF46BF CRC64;
     MYISLILKLQ YFFSPIIDNS IEVDGKYTEI IKKDHDNILF NSIEKSLYDF DLITCDNGLE
     TFALLSNKLY KTGIEAIIDD DLTRLCNQSP VKRWNLMGLP PKTKCKIKNI FLSFIALISL
     IIRYAIILPC RIFLLASSFI FIFFAAIIGS FNGLTRQQGT YVAVTVSRLY TASMGYVGLY
     RDRKYQPAGP GITVSNHLTA NDVQILWSDV NYDERKGYSL TGQKHKGIIG LFEACSSKFL
     DTLWLERSNE SERQNFQKNV LKAARDENFK SILLFPEGYC SNNTAVCQFK KSLFVDDVNI
     YPIAIKQDPR LGDAFWYEDD FLSYTFRLLT SWATIYHVHY LPSQIKRPSE NEIEFAYRIQ
     ELIASAVSIK CIKNPSTELL KKEKARQKQL MLTRENFGCF IIEQWKKYEI SKSNNSFEEE
     SYSSRQSFKE PFQNDGFYNN IIATSTN
//