ID M1W571_CLAP2 Unreviewed; 600 AA.
AC M1W571;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=CPUR_00550 {ECO:0000313|EMBL:CCE27078.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE27078.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE27078.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE27078.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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}.
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:CCE27078.1}.
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DR EMBL; CAGA01000003; CCE27078.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W571; -.
DR STRING; 1111077.M1W571; -.
DR VEuPathDB; FungiDB:CPUR_00550; -.
DR eggNOG; KOG0380; Eukaryota.
DR HOGENOM; CLU_018190_2_0_1; -.
DR OrthoDB; 9612at2759; -.
DR PhylomeDB; M1W571; -.
DR Proteomes; UP000016801; 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 ECO:0000313|EMBL:CCE27078.1};
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:UP000016801};
KW Transferase {ECO:0000256|PIRNR:PIRNR000439, ECO:0000313|EMBL:CCE27078.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 537
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 600 AA; 68580 MW; 66E7A8CED50A3238 CRC64;
MSSSADFLPS GHHQRQGRAR KRKSHAAHDT PPMERSESDA HTGASAESPP ASGPTSGQST
PIPENAPPST KSLCSARKHI RAEQKRRIFP TIEYASRLSH FDPQSDYRDF HGFFNLFWIG
LAIMGITTML RNMKDTGYPL RIEIWTLFTI KLWHLVIAEF LMVGTTLVGL PLQKWFRNAP
SGGILTWARG GMAIQSIYQG FWLAFWIAVP FVLEWTWTSQ VFLLLHTMVM LMKMHSYAFY
NGHLSETEKR LRALDSPSDA SDRRPAYVYP ASNISRGSIS GIPTSKNPLP EKKTKKKNKN
KKHEKVDKDG GQGEQQRGSL VGFSNDGEYK TADEIQVLRE DLARELTSPM GNTTYPLNLT
WANYIDYLLC PTLCYELEYP RTAQINWTSL NAKILATFGC IFLLTVVSEE FILPVLVDAQ
RRLTPLPPYT HTPSISEALL ILAESISWLL FPFMLTFLLI FLVIFEYILG AFAEITRFAD
RHFYADWWNS TDWMEFSREW NVPVYSFLRR HVYSASRPHT GKMLATLITF LISAFMHEIV
MACISKKIRG YGFVCQMMQL PIVMLQRTKF IRARKTLNNV CFWISMILGL SLMCALYVLV
//
