ID F0ZGZ2_DICPU Unreviewed; 1242 AA.
AC F0ZGZ2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=DICPUDRAFT_54421 {ECO:0000313|EMBL:EGC36799.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC36799.1, 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 GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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DR EMBL; GL871016; EGC36799.1; -; Genomic_DNA.
DR RefSeq; XP_003286670.1; XM_003286622.1.
DR AlphaFoldDB; F0ZGZ2; -.
DR STRING; 5786.F0ZGZ2; -.
DR EnsemblProtists; EGC36799; EGC36799; DICPUDRAFT_54421.
DR GeneID; 10504082; -.
DR KEGG; dpp:DICPUDRAFT_54421; -.
DR eggNOG; KOG1221; Eukaryota.
DR eggNOG; KOG3730; Eukaryota.
DR InParanoid; F0ZGZ2; -.
DR OMA; WDPDHHA; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0080019; F:alcohol-forming very long-chain fatty acyl-CoA reductase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:InterPro.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR CDD; cd05236; FAR-N_SDR_e; 1.
DR CDD; cd09071; FAR_C; 1.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR033640; FAR_C.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 598..726
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 805..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 141820 MW; 8435B073A845AEE7 CRC64;
MVVISNFYEG KNVLITGSTG FVGKVLLEKM VRDLPGIQKI YIIIRGNAKE RFIDDIIGSR
IWDLLKAKLG GEEEFNKLIH NKVVPVSGDL SKEGLGLSPE DTQTIIDNVN VIIHCAASID
FRERLDKAIQ SNLYASLNML DLSRKLRNIK AYVHCSTAYV NSNREGWLDE ELPVLDFNPE
EMVDLIMKQD IQTLERITPN LLGAYPNTYT FTKAITERIL ALKRGDVPLC FVRPTIVGGS
LKEPVPGWVD SVAAIGAVML YCGVGLVQFM KGDGRMVADI VPVDHVANAL IAAAVSMESQ
NSLKIFQIGT SHRNPVLWNR ISHYVTEYWR SHTPKKSVAR SSFSFHSHIM YEAHFFMKYG
IPSALLQVLA VLTGSEDTKT KAEGFKKITK AARLICDTFK HFTGHEWVFS VQTLEKIFQD
LFDGEDRIKF NCDAAEINWQ SYFCYFCYGL HKYVIKEEGV RPPTELLNTS IITKSEVNQS
GFFQWVFADI SWASTSYRHV TQTPLPPRAP TEIRSLVMNS PRVQQAMEKV SREEGVLVSE
IEKRASQIMD RMQSNLNIMV VRVLGWFLKK VWRKIYQGIH VDEKGIELIR EAIKKSPVVL
IPSHRSYIDF LIISYIFFEY NLPLPHIAAG EDFLSIIIVR WFFRNAGAFF LRRTFHGDSL
YWAIFSEYVQ RLVIDNQPME FFIEGKRSRT GKSLHPKMGL LSMVCQPYFE NRVQDVHIVP
IGISYEKVLE GELYSNELMG ESKTKESLNG LLRASKVLKM NFGRINVVFT PPISVKQYTE
QKVQEVASQR HLPAPALPAP SILSTPASIA PPSSTKNSNI SEGDFEINFN KPDSRATGAI
YDPFNNNGDR RSLISDLGYQ IVRDLNKSII ITTTSVVATI LLSFRRGINR EELITKVEWL
REEIFARGGD VAFEGPSDAL VDHSLKLISN LVSKRRNMYE PGSAQLGVTN KNYRKNVLVL
NFYRNQLLHL FLWDGLVSLV ILSILQTRDQ QSNENILNTN NVNNKQPKDT VSEETIICEV
RFLAKVLSIE FVNQPGYDTD EFIKGQINRM AIRGIINKEQ TNEQTFYGVK SEGACSFFAN
LFYPLVEGYL SGILTLFSIQ PEMMIKKNQF LQRMGWFAEK MFEEGKSNFY ESCSMEILGN
SLQLFEQMKV IQRKKLEEQV GKRTTRSSNG NKKQQKKPTR RERKQEPEEY IRLLPPYQDK
DGLLKELTER LSKYKKSPQT KHQLNDLRRT VVEDFPLLSS KL
//
