ID   M2XSJ5_GALSU            Unreviewed;       566 AA.
AC   M2XSJ5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Phospholipid/glycerol acyltransferase family protein {ECO:0000313|EMBL:EME26369.1};
GN   ORFNames=Gasu_59870 {ECO:0000313|EMBL:EME26369.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME26369.1, 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; KB454551; EME26369.1; -; Genomic_DNA.
DR   RefSeq; XP_005702889.1; XM_005702832.1.
DR   AlphaFoldDB; M2XSJ5; -.
DR   STRING; 130081.M2XSJ5; -.
DR   EnsemblPlants; EME26369; EME26369; Gasu_59870.
DR   GeneID; 17085346; -.
DR   Gramene; EME26369; EME26369; Gasu_59870.
DR   KEGG; gsl:Gasu_59870; -.
DR   eggNOG; KOG2898; Eukaryota.
DR   OMA; PWNFLTR; -.
DR   OrthoDB; 1080at2759; -.
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:SF2; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 4, ISOFORM D-RELATED; 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:EME26369.1};
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:EME26369.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        126..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        527..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          213..324
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          455..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  65998 MW;  A7F4F4B1CA8CEA1A CRC64;
     MLLLRNRYIF RSVYLQLLSI ASRLIYGRDP ERTQAKDRAA QLANAVKIKK VNSALEFGGI
     GEWEGIFYEA ADHRQTERKD LIFDFPDSFT FLSEAADALV GDSLSRCFSS EPPKPWNFLT
     RNCSQVPLLL IPLWIASLWI RYLVLLPLRL AILCFGIFLF LTLFILVGFV IPRGDWRSSF
     EQRLLRFLAS VFLASWSGVV RFHGRRPERK ANQIYVANHT SLIDIIVLYK DYTFSIIGQR
     HGGFAGILQD LLMRVQNHIW FDREVGRDRH IVQELLREHV RNPNNEPMLV FPEGTCVNNE
     YCIMFKKGSF ELGAQVVPIA IKYNKRYANP YWDSSQCGFL RHVWDLMTSW AVVVDVYYLE
     PMKREPNETA SEFAKRVKRA IVHRIGLIDV EWDGFLKRHR ISSKFIQQRQ KAHAMVLLRR
     MQRNCIISDS YPLEWKETAF DSSVDLSSLS TASHLPKMRK RKSEKTRIKY NEEENKTNST
     SAENKETFMK ESSSFTSSQE NGKEQLDLDD PFDEIEGRGY KVWVDGVFLL VIMLCIVFCT
     ILSCILFFKY TSWSGITDWK WNVLFK
//