ID A0A151GJ28_9HYPO Unreviewed; 694 AA.
AC A0A151GJ28;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=O-acyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DCS_04095 {ECO:0000313|EMBL:KYK57088.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK57088.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK57088.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK57088.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
CC -!- FUNCTION: Sterol O-acyltransferase that catalyzes the formation of
CC stery esters. {ECO:0000256|ARBA:ARBA00023568}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00009010}.
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:KYK57088.1}.
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DR EMBL; LAYC01000002; KYK57088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GJ28; -.
DR STRING; 98403.A0A151GJ28; -.
DR InParanoid; A0A151GJ28; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000076580; Chromosome 02.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR InterPro; IPR004299; MBOAT_fam.
DR InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR PANTHER; PTHR10408:SF26; O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1.
DR Pfam; PF03062; MBOAT; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076580};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 665..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 78..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 78388 MW; 876793AE074461D3 CRC64;
MQCQSSPSST PVSVTNHLQS ATLFPTASRF PLLSRFHGLT AARTRPTTAA RSLILTGYSP
IDSISSCSVM SPSAPPVGWD PVRTGGRDEF GNRHRRKWPR SRPWLSPVVE EAAEFQAISS
ADLAKRPFGS ARRRRERPRE VTHLPILSPS ILPLPPAYTL SLSGRSTPIP ENAPPSTKSL
SSARRLARAQ EKRRIFPTVD YASRVSHFDP ASDYRDFHGF FTLFWIGLAI MGITTMLRNF
KDTGHPMRIK IWTLFTVKLW HLAIADFLMV ASTALSLPLH RWARSAAPES LATWKYGGMA
VQSLYQSAWL ALWIGIPFWL EWTWTSQVFF LLHTMVLLMK MHSYAFYNGH LSETEKRLRA
LDNPTSGADR APAYVYPTAD LRKGSVSGIP SIPDPIISRD PPAPEALTRD DDADGIAGAD
ELEVLREDLA RELISPMGHV TYPSNLTWAN YLDFLLCPTL CYELEYPRLE TINWTSLNAK
ILATFGCIFL LTITSEEFIL PVLVDASRRL DELQASSGSL SEMLLILAES ISWLLFPFML
TFLLTFLVVF EYVLGAFAEI TRFADRHFYA DWWNSTDWME FSREWNVPVH SFLRRHVYGA
SKPHTGKTGA TFITFFISAV GHEIVMACIT KKIRGYGFVC QMLQLPIFML QRTRWVRGKE
TLKNVFFWCS MILGLSLVSS LSMPTGVYQF VLPC
//
