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Database: UniProt
Entry: F0ZAQ2_DICPU
LinkDB: F0ZAQ2_DICPU
Original site: F0ZAQ2_DICPU 
ID   F0ZAQ2_DICPU            Unreviewed;       361 AA.
AC   F0ZAQ2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=DICPUDRAFT_27831 {ECO:0000313|EMBL:EGC38927.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC38927.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   EMBL; GL870966; EGC38927.1; -; Genomic_DNA.
DR   RefSeq; XP_003284492.1; XM_003284444.1.
DR   AlphaFoldDB; F0ZAQ2; -.
DR   STRING; 5786.F0ZAQ2; -.
DR   EnsemblProtists; EGC38927; EGC38927; DICPUDRAFT_27831.
DR   GeneID; 10506218; -.
DR   KEGG; dpp:DICPUDRAFT_27831; -.
DR   eggNOG; KOG1505; Eukaryota.
DR   InParanoid; F0ZAQ2; -.
DR   OMA; CPRIHIH; -.
DR   OrthoDB; 2906776at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IBA:GO_Central.
DR   CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR   InterPro; IPR032098; Acyltransf_C.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10983:SF76; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE EPSILON; 1.
DR   PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF16076; Acyltransf_C; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..204
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   361 AA;  42376 MW;  2BC5F853BAED625C CRC64;
     MEPKVLLRRF VSIAGLLISS LYAAIFLMIP VIIIEPFFKK LAFTLHYKIA SIWFRLVLFV
     FEVVNNIEIR FYGDDIPEGE SMIMMMNHPS EVDWLFSFSV AYRKKALSKI KVILKNEVRL
     VPGVGWGCDN LDYIYLSRDW NFDEKHMEYK LNKYIENDFK PWLVIFPEGT DIDEEKLKKS
     HAFAEKNGYP KFNNVLLPRH KGLHACVEPL RNTIDSVYDV TIGYESKPTI LSCVSGSNPK
     VVNMHFKRYS LNEVPSNEDD LQKWLFKIYA EKDKMLQDLK ENGQYSMPYT KTKFEPSFLL
     TALAWFYYLI IPATHLLIRS NFVKLYFVAS IIYYILNSKV EILRKLRGLQ NSVYIPKPKQ
     H
//
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