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Database: UniProt
Entry: A0A0M4ERB9_DROBS
LinkDB: A0A0M4ERB9_DROBS
Original site: A0A0M4ERB9_DROBS 
ID   A0A0M4ERB9_DROBS        Unreviewed;       690 AA.
AC   A0A0M4ERB9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=CG33120 {ECO:0000313|EMBL:ALC39407.1};
GN   ORFNames=Dbus_chr2Lg1492 {ECO:0000313|EMBL:ALC39407.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC39407.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC39407.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC39407.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC         + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00001039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester +
CC         CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75;
CC         Evidence={ECO:0000256|ARBA:ARBA00029340};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004771}.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the long-chain O-
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00024360}.
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DR   EMBL; CP012523; ALC39407.1; -; Genomic_DNA.
DR   RefSeq; XP_017835216.1; XM_017979727.1.
DR   AlphaFoldDB; A0A0M4ERB9; -.
DR   STRING; 30019.A0A0M4ERB9; -.
DR   GeneID; 108594523; -.
DR   OMA; APDHTII; -.
DR   OrthoDB; 3680232at2759; -.
DR   Proteomes; UP000494163; Chromosome 2l sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0045017; P:glycerolipid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR   InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR   InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR   PANTHER; PTHR31650:SF23; GH11223P; 1.
DR   PANTHER; PTHR31650; O-ACYLTRANSFERASE (WSD1-LIKE) FAMILY PROTEIN; 1.
DR   Pfam; PF06974; WS_DGAT_C; 1.
DR   Pfam; PF03007; WS_DGAT_cat; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
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        370..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          110..253
FT                   /note="O-acyltransferase WSD1-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03007"
FT   DOMAIN          545..686
FT                   /note="O-acyltransferase WSD1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06974"
SQ   SEQUENCE   690 AA;  79796 MW;  AD70310065455515 CRC64;
     MESVWLECVS FLKTLLCFIV ALMLMPLLLL SFLCAHFGNE LANYLLSIKY PNLTISKSKK
     IRTLIDTPKN AGIFHFLLQV EGPCEFEHIN RAYSTQLIEL KDKTGVLRYP MLRQQLVTCW
     GHYAWVNDSS GFNINNHVLL STPKYRGRAV SESNIQEYVS ELAAKYIPSD LPQWQVTVIP
     NSDDTQPYYI LIKVHHLIIA EEQDLHVSEM LLLQDPEKKS FVDALTATTP AVSKQLSHFV
     RQPEHISKLL QHVQHLISCR WQQFIYEFES LDTPDGVKSQ PDARNLSQLL SLSLIVLVNV
     SLSYWRQRAL RRKLKHRSGH SYRHDVGMLQ TIYILLVREL EQRNLNWTVA RAALTHSLQP
     LNMVKCWTRF IWHLLLHNFI LLPYYVYYEL LALRDVLLRG QTSYSDTHCA RLYLYVPLLF
     YAQLELVKIC YELFMAPRNI YDVLFVQPTK ELNILHQKSY AGRKIVSFSR SIDGSQLRER
     HEHMFGQQLR ESDFSLACLA GAVHDYFNTY TDKAAVPALL NTTCRTIAQG YFTDRSGDKS
     SHIGGVIFLQ LPLGPPDALK ALQLHEIVER IRKQQIMIYL ASIGQTKYSL LTSLLPHVLT
     KIFINFFSYN FPVTITEVYG PADPQFQAAW GQRVQDVLLF RPPQSKTCLS LNLHRYGDRY
     RLAVMADTHL APDHTLLTRS FERYMETVAL
//
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