ID A0A1E3QY48_9ASCO Unreviewed; 715 AA.
AC A0A1E3QY48;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=BABINDRAFT_5532 {ECO:0000313|EMBL:ODQ82590.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ82590.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV454426; ODQ82590.1; -; Genomic_DNA.
DR RefSeq; XP_018987918.1; XM_019132230.1.
DR AlphaFoldDB; A0A1E3QY48; -.
DR STRING; 984486.A0A1E3QY48; -.
DR GeneID; 30150083; -.
DR OrthoDB; 2728187at2759; -.
DR Proteomes; UP000094336; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProt.
DR CDD; cd07992; LPLAT_AAK14816-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR31605; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR31605:SF0; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000094336};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 409..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..260
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 590..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 80889 MW; EB91D1D1245FE9DB CRC64;
MAEPKSQGVS TFRKFVYDIV LWIFDRIFDC FFREIRTRGA FRVPRTGAVI FVAAPHANQF
VDPGILMGQV QKEASRRISF LVADKSYRRW DIGLFSRCQL AILVKRAQDN LRKATGKIKL
DFDADPLLVR GVGTKFTKEC TVKGLIALPE SLGTTEILEI LSDTELLVRK EFKRNDKTVG
YLAKGTNFKV ADKVNQKEVY EKVFSHLSQE QCIGIFPEGG SHDRTDLLPL KAGVAIMALG
AMDHDPKCNV KIVPCGMNYF HPHKFRSRAV VEFGRPIEIN RELVQRYANP ESNREAVREL
LDTITAGLKA VTVTCTDYET LMVVQGARRL YAGNFGNKIP LPLVVEFNRR LVIGYDHFKE
NPKIQHLKDG ILHYNQQLKF LHLSDHQVEE ITDNHLMQLR MLPVFLARLF QVIVLFILAL
PGAILFAPVF IVTKRVSKKK AAEALAASTV KVRANDVLAT WKILIAMGLS PLLYIFYASI
GTYYCYYREI FASWRLSLVF CTLYISGASI TYAALIVGDQ GMDILKSLRP LYFSLTTTSS
VSELKQTRQE LSEQITEVVN ELGPELFPDF NLLEQKRKVK RGVDMGLDSD AEEEAKTQEL
RQRRAKKRAE AKRQVVPSDG GDSFSDSDGV SRINSSNDLS DIPMFSNYNK SSMMNFRAYA
SSNTSESESE MEASNGFKGQ TLLSSRIREK MFEDRKLTDL KIGADTEDED EEKEA
//