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Database: UniProt
Entry: A0A4T0FWU8_9BASI
LinkDB: A0A4T0FWU8_9BASI
Original site: A0A4T0FWU8_9BASI 
ID   A0A4T0FWU8_9BASI        Unreviewed;       737 AA.
AC   A0A4T0FWU8;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 10.
DE   RecName: Full=Phospholipid:diacylglycerol acyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=E3P99_00251 {ECO:0000313|EMBL:TIA93141.1};
OS   Wallemia hederae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1540922 {ECO:0000313|EMBL:TIA93141.1, ECO:0000313|Proteomes:UP000310189};
RN   [1] {ECO:0000313|EMBL:TIA93141.1, ECO:0000313|Proteomes:UP000310189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-5753 {ECO:0000313|EMBL:TIA93141.1,
RC   ECO:0000313|Proteomes:UP000310189};
RA   Gostincar C.;
RT   "Sequencing 23 genomes of Wallemia ichthyophaga.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TIA93141.1}.
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DR   EMBL; SPNW01000003; TIA93141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4T0FWU8; -.
DR   Proteomes; UP000310189; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR   PANTHER; PTHR11440:SF97; BCDNA.GH02384; 1.
DR   PANTHER; PTHR11440; LECITHIN-CHOLESTEROL ACYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF02450; LCAT; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000310189};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   737 AA;  82585 MW;  3461783CB7A60385 CRC64;
     MGIYQRRAKK QEEKQDSNRD RNSNSKTASN NSNAQNTHLN PTELQVKLRH DPRRKSYSVV
     APGTPLHEID LSEVSFLQHH DSHKGKGAFK RTKRVVKTRR FLLPLFLTIG FALASIILAP
     LPNGLADLPD FDLSGLGAQW EYLFDDLTTR ISDAKLWFSS RGFKTGLAAR DEGLTAHSPV
     MLFPGVITTG LESWSTDADS LGSFRQRIWG THTMFKSIFA DKNEWIRQIS LDSETGLDPP
     GVRVRPAQGL DAASMFMQGY WVWRPIIENL ACINYLEMAA YDWRLAYTNL ENRDHYFTRV
     KSRIELNKKI HGKKTTVGVC SRHDVESNKT PKLVSHSMGG TVLLYFFKWV EAQGYGGGGD
     QWVEDHIDSF INISGTLLGV PKAMTALLSG EMKDTVELNP AGAYALEKFF SKEERADLFR
     SWFGIAGMWM KGGDAVWGDE NGAPDDPANT TDTFGQFLSI RENHETVADK RNNFTMAQSN
     PYILSNTPRV WQKMMQTNYS YGIETDPKKL DDNNNDPTKW SNPLESRLPN APSMSVYCIY
     GVGKPTEVGV DLFCKATPNS YHSQRSYYYT EGPKTHQQLQ SDLEVGKCEA DDCLTTQESQ
     EDLPLTSQHA IDGDLSTDST TPSISNGVKF GQGDGTVALT SLGAMCADGW RRDDRRYNPG
     NSRIVTHEVE HQPDSLDLRG GDYTGDHVDI LGSTPLNELI LKIVAGQGHT LEDHYVSDIR
     NISARIDWDL VKRRSVL
//
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