ID A0A0D2HDV7_9EURO Unreviewed; 512 AA.
AC A0A0D2HDV7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=Z520_03766 {ECO:0000313|EMBL:KIY00081.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY00081.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY00081.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY00081.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PIRNR:PIRNR000439}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|PIRNR:PIRNR000439}. 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 ECO:0000256|PIRNR:PIRNR000439}.
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DR EMBL; KN848067; KIY00081.1; -; Genomic_DNA.
DR RefSeq; XP_016634203.1; XM_016774276.1.
DR AlphaFoldDB; A0A0D2HDV7; -.
DR STRING; 1442371.A0A0D2HDV7; -.
DR GeneID; 27709512; -.
DR VEuPathDB; FungiDB:Z520_03766; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
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.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000439};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000439};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW Transferase {ECO:0000256|PIRNR:PIRNR000439};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 218..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 449
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 512 AA; 59186 MW; B2CE44E84BB21393 CRC64;
MALPRSTSQE RNILRPRPTR ALPEALRASG QVQSLSTARK AARAQAKHRL FYTIDYVSRV
SYFDARSEYR DFRGFFVLFW ISLTIMVITT CLRNIKETGH PLRVEVYALL SRNVISLGLS
DAAMVASTAL SLPIQKVARG TNGVLRWRRA GIWIQSTFQA LWLALWVSWP FLLGWTWTAQ
VFFALHTLTF LMKMHSYAFY NGHLAETERR LRALDKPETA DRGKAVKYPS SPSRLRQMDS
ESSEEEKEEE QDLAQLRRDL ATELTSPLGQ VTYPQNLTLY NYIDYVLCPT LCYELEYPRT
PKIRWDELFY KTLAVFGCIF LMITISEEFI MPVLAESAAR LRLTTSLSEM ALILAETTSM
MLFPFMITFL LVFLVIWEYI LGAFAEITCF GDRHFYSDWW NSSDWLEFSR EWNIPVYHFL
RRHVFFSSKT YFSTPVAMAI TFLVSALGHE LIMGCITKKL RGYGFFAMML QLPIVALQRS
KLVRGRWVLN NAAFWGSMIL GLSTMCSLYV LV
//