ID A0A0N0DEV4_FUSLA Unreviewed; 607 AA.
AC A0A0N0DEV4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=FLAG1_05440 {ECO:0000313|EMBL:KPA41684.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA41684.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA41684.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA41684.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-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}.
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:KPA41684.1}.
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DR EMBL; JXCE01000089; KPA41684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0DEV4; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000037904; 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:KPA41684.1};
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:UP000037904};
KW Transferase {ECO:0000256|PIRNR:PIRNR000439, ECO:0000313|EMBL:KPA41684.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 121..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 584..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 544
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 607 AA; 69157 MW; 71B2B22FA5D61644 CRC64;
MSSSIETLPN GNGHAGEHDH VLRPRPRKPK HSQVADVVRM TTASDGEHLM PDNASTGSAS
GLTSGRSTPV PDNAPPSVKS LSTARKQVRA EQRRRIFPTI EFASRVSHFD PESDYRDFHG
FFNLFWIGLA IMGITSMLRN LKDTGFPLRV QIWGLFTVKI WHLAIADFLM VATTAVSLPL
NRAARNAKPG SFLDWNRGGI AIQSIYQVAW LTLWIIVPFY FEWTWTSQVF FLLHTMVLLM
KMHSYAFYNG HLSQTEKRLH ALDNPFSSHD RRPAYQYPST DLPPSVTKGE STSNSAKKRR
RQRQKKQEAK QNGINGHKSN DEEPTNHDLL VPSPVASPSN SADEVDEIRE DLARELTSPI
GNVTYPNNLT WSNYTDYIFC PTLCYEIEYP RTTHINWINL ISKIIATFGC IFLLTIISED
FILPVLLDAS ERLDAVPAVS SVSEKLLILA ETISWLLFPF MITFLLVFLV IFEYVLGAFA
EITFFADRHF YSDWWNSTDW MEFSREWNIP VYSFLRRHVY SASRPRIGRG AATALTFLIS
AFGHEIVMAC ITKKFRGYGF VCQMLQLPIV MLQRTRWVRG KETLNNVCFW ASMVLGLSMI
CALYVLV
//
