ID M2XQ82_GALSU Unreviewed; 352 AA.
AC M2XQ82;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Phospholipid/glycerol acyltransferase family protein {ECO:0000313|EMBL:EME32367.1};
GN ORFNames=Gasu_04580 {ECO:0000313|EMBL:EME32367.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME32367.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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}.
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DR EMBL; KB454486; EME32367.1; -; Genomic_DNA.
DR RefSeq; XP_005708887.1; XM_005708830.1.
DR AlphaFoldDB; M2XQ82; -.
DR STRING; 130081.M2XQ82; -.
DR EnsemblPlants; EME32367; EME32367; Gasu_04580.
DR GeneID; 17090955; -.
DR Gramene; EME32367; EME32367; Gasu_04580.
DR KEGG; gsl:Gasu_04580; -.
DR eggNOG; KOG4666; Eukaryota.
DR OMA; AKCHAIV; -.
DR OrthoDB; 5471865at2759; -.
DR Proteomes; UP000030680; 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 ECO:0000313|EMBL:EME32367.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EME32367.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..254
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 352 AA; 40249 MW; 39D09616BB98782B CRC64;
MSGELESMAM YYTDDSIVQN HSEHTKSKLL VRNPFVRRDR PWRLLGLIKV LVGLVLVPLR
LLFCFLLLVF VWILIRILAL GVSRKDLAYH PLEVNVMVRA CISFLIRRGA RLLLLIVGFV
WISDESRTVV PPDCIVVSNH VSFYDILYFL SAFAPPFVAK QGVKNIPFVG FIAEIMECIF
VDRENRTSPS ATSLIALRLE RIDLLNISFS SWMAPSALVM FPEGTTSNGD CLLRFHTGPF
VQKRTIQPIV LQYSFGDADP AFVGLSFFHF LRILSEPYYI LRVNFLPRYV PSEEEKTNGR
LFAENVRRRM ATILNRAPVD LSYQDRIRRK LSRCGLEFVS LHPDTSILGT SD
//
