ID A0A0N0P3C8_LEPSE Unreviewed; 419 AA.
AC A0A0N0P3C8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=ABL78_7449 {ECO:0000313|EMBL:KPI83517.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI83517.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI83517.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI83517.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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:KPI83517.1}.
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DR EMBL; LJSK01000362; KPI83517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0P3C8; -.
DR EnsemblProtists; KPI83517; KPI83517; ABL78_7449.
DR VEuPathDB; TriTrypDB:Lsey_0362_0050; -.
DR OMA; HPWWFGF; -.
DR OrthoDB; 5471865at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
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:SF52; LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 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 24..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..327
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 419 AA; 47446 MW; 5AA5938A2E47DE72 CRC64;
MSNQKSKRAY GVSMPYMMYG RLEGFLRIPV AMVVWYLFFR GVAAPFYDHG DSRRCTGGDC
AAAAVSLGLF TWLRVYLCAN GVFLVTLFLV ENLRCLLIPG PTRLSLTDDY VDGNPPKVDT
MEAFKYDTPL GTYERIKIGF FVVTGIVFVR FFAAITTIFL GLFSTSVTGY LDRYAHPWWF
GFWSRVSKVL VIVAFSLLGL HNIQLYGKLA SRKECKFLIS NHSCVVELVL LFIMADFPSF
VSRRENLQFA FMGSIVKFSE SILVDRDAAT SRAQTQQAIF ERARDPNAPQ LMVFPEGTTC
NQLTLFQFKK GVFAPGAPVQ MICFAFPYKH FNASWTGREV GGNGFFDILL RLSCQFVNYA
EVRALPVYYP TVEEKHDPIL YAAHCQKMMA TVLHANVSDA TYGDYKEASR RYAETKKQK
//
