ID A0A074WX05_9PEZI Unreviewed; 503 AA.
AC A0A074WX05;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=M436DRAFT_68881 {ECO:0000313|EMBL:KEQ77698.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ77698.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ77698.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ77698.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584702; KEQ77698.1; -; Genomic_DNA.
DR RefSeq; XP_013432233.1; XM_013576779.1.
DR AlphaFoldDB; A0A074WX05; -.
DR STRING; 1043004.A0A074WX05; -.
DR GeneID; 25414498; -.
DR HOGENOM; CLU_018190_2_0_1; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000027730; 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:KEQ77698.1};
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:UP000027730};
KW Transferase {ECO:0000256|PIRNR:PIRNR000439, ECO:0000313|EMBL:KEQ77698.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 440
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 503 AA; 58312 MW; 26D522E83C41A23F CRC64;
MLPLLLRHPL QSPGTPANAP PSVKATSSAR KQVRAEQKRA FPRIQYAARF SHFDPRSEYS
NFRGFFVLFW IALTIMVLTT MLRNLKETGY PLSMRQWGLF TKNIYEMAIV DLIMVATTGT
SLPLNKLFKN SKGLLQWKHQ GMNIQIVFQA CWLLLWVTWP FVRDWTWTAQ VFFTLHLLVM
FMKMHSYAFY NGHLANTLQR LSALDNPAPD ASTAAAVKYP SSQTPIADIN DELKQEETAQ
ADSLTQLRED LAMELVSPFG RLTYPQNLTV ANYFDFLLCP TLCYELEYPR TSSRSYLEIF
WKSLAVGGII FLLTITSEEF IIPVLAESAE RLEHQQNWHE GSLVFAETVS RLLFPFMVAF
LLVFLVIFEY LLGAFAEITC FADRQFYSDW WNSLDWLEFS REWNIPVHHF FRRHVYSASR
NTMSRPVATF ITFLVSSIAH ELVMGCITRK FRGYGFVAMM LQMPIVLVQR SRWIRNRTIL
NNVLFWCSMI LGLSMICALY VLI
//
