ID A0A074XPD3_AURPU Unreviewed; 762 AA.
AC A0A074XPD3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=M438DRAFT_331943 {ECO:0000313|EMBL:KEQ87418.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ87418.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ87418.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ87418.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584976; KEQ87418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XPD3; -.
DR STRING; 1043002.A0A074XPD3; -.
DR HOGENOM; CLU_007860_1_0_1; -.
DR OrthoDB; 2728187at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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; 2.
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:UP000030706};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 430..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..282
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 601..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 85238 MW; 8D99CC1ED90F5219 CRC64;
MAPPRKSKSS FWPNFIYDAW LWTFSVLVDL FFREVHPRSS WKVPRNGPVI IVAAPHANQF
VDPLILMRVL RMDAYRRVCW LIAEKSMKRR FIGWGARMVG SVPVGRALDS KKPVEGRIYL
PDPKDDPTLV KGIDTDFGNK DIYMVGGLLA LPSFKNKFAN TEIKEILGPN EIRLKKPFSG
NVALRQLTGQ EVKDEKAEAK LTEGFEGTEF EVAPHVDQGE VYSSVFKKLH EGGCIGIFPE
GGSHDRTELL PLKAGVAIMA LGALAEDPNC GVKIVPCGMN YFHAHKFRSR AVVEFGTPVE
IPNELVEMYK NGQKREAVGQ VLETVYQALV SVTVTSPDYD TLMLIQAVRR LYNPKGKKLP
LPMIVELNRR LVKGYTTYKD DPRIVNLKKS ILAYNKELMM LNIRDHQVSY AKFSIFKVLL
TLFYRLGKLL VLAIAVLPGL VLFAPVFITG KVYSIKKSRE ALAASTVKIQ GRDVMATWKL
LVSLVVAPLL YNFYNIILAI WTHYNRIGGR VPNWVPLWAV FAFGYILFPA ITFAALRFGE
VGMDIAKSLR PLILSLGPSS GNTLVKLRAK RASLVEQVTE VINELGPELY PDFDHQRIVS
DPSHPLSPSY SQPQTPRSRR SSEYDRMSMT SPDLTSYFSR TGTAGASIGG GSGQNTTHLP
RNESFGNIGG FGFFSSRPHT PNRSRSRNRS RTSSDGGMGF TAMKPMTTID SKGGYEEVTE
KIRDAMKQRG RRRRSEDASA VDNGWEMADA DEEVEDEDKK VV
//
