ID A0A168ATL4_CORDF Unreviewed; 626 AA.
AC A0A168ATL4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=LEL_10052 {ECO:0000313|EMBL:OAA69176.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA69176.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA69176.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA69176.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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, 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:OAA69176.1}.
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DR EMBL; AZHF01000011; OAA69176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168ATL4; -.
DR STRING; 1081108.A0A168ATL4; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000076881; 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:UP000076881};
KW Transferase {ECO:0000256|PIRNR:PIRNR000439, ECO:0000313|EMBL:OAA69176.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 563
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 626 AA; 70866 MW; A4F56ADA9BEB268F CRC64;
MATTAIDVVS NDDADSVRSR PRKAVVAAHA LLKQEAAADS NLSNPDSVAT SGRSTPVAEN
APPSTKSISS ARKTLRAEQQ QQQQQQQSRR QRRIFPTTDF ASRLSHLDPD SDYRDFHGFF
NLFWIGLAIM GITTMLRHMK DTGYPFTFEI WSLFTVKLWH LAVADFLMVA TSAVSLPLHR
LFRAAPQGGL WTWARGGMAL QSVYQVLWLG AWVAVPFWLE WTWTSQVFLL LHTMVLLMKM
HSYAFYNGHL SETEKRLRRL DEPTSRGTKD RSPPYIYPVA AANRRSSKAG IAVDMVGGKE
DIHLHHSNKT EEQTPTTPTT PTTTTTGRNK SKSAPPKPEE GKLAETKAAA AQQHECDSDD
EIELLRDALA RELTSPMGHV TYPRNLTWAN YFDFLLCPTL CYEIEYPRMP TVNWTSLISK
IVAVFGCIFL LTITSEDFIL PVLVDAESRL ASITTTQSAA LSETLLILAE TISWLLFPFM
LTFLLVFLVI FEYVLGAMAE ITRFADRRFY SDWWNSTDWM EFSREWNIPV HAFLRRHVYS
ASRPFTGRSG ATAITFFISA IGHEIVMASI TKKLRGYGFI AQMLQLPIVV LQRTKWVRGK
RTLNNVFFWS SMIMGLSMIC ALYVLL
//
