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Database: UniProt
Entry: A0A0D2HDV7_9EURO
LinkDB: A0A0D2HDV7_9EURO
Original site: A0A0D2HDV7_9EURO 
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
//
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