ID A0A109FEN3_9BASI Unreviewed; 587 AA.
AC A0A109FEN3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=RHOSPDRAFT_29797 {ECO:0000313|EMBL:KWU43104.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU43104.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU43104.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU43104.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-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; KQ954495; KWU43104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FEN3; -.
DR STRING; 1305733.A0A109FEN3; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000062823; 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; STEROL O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10408:SF9; STEROL O-ACYLTRANSFERASE 1-RELATED; 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:UP000062823};
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 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 567..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 241..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 524
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 587 AA; 67436 MW; 0769C2E1C7F29805 CRC64;
MQRAAPRYSR RTAADSDEVV AIAYDKRTGE LRPIPARSLK DEKTRRSGRT IFTPRFSHFD
RNNVASAQDP FRGLYTLFWI LLFVGGFRTI YGRWIERGGL YRWQFAELIS EDAWALALSD
AVLVGTTVLC VPFAKVIARG WVRYYWTGLI FQHIAQTAYL FTAIRWTFHR EWPWVQSGFL
TLHALTMLMK VHSYCSLNGE LAERARQMRK DEKELEKILE AESGGRRAAE VAAREAWEKA
CREETSALDD DPSSASTRPD LLAPPADPAS TFSTQPSSEE EHVQATALRQ RRVSGRRRSN
SPLKHKAVPA LSKPNPEEEP REGVETLTWH PQERIAPLAM AICDAKDALS SGGKENISFP
QNVTFLNFLD YLLVPTLVYE LEYPRTKTIR PLYVLEKTLA TFGTFTLLVL IVEHFILPNM
PRSDQTFFAS VLDLALPFCV CYLLIFFIIF EAILNVFAEM TRFSDRAFYS DWWNSTSFDE
FSRKWNRPVH TFLLRHVYAT TISTYRLSKF SAAFITFLLS AAVHELVMLV VTKKVRLYLF
LMQMAQLPLI MLGRARIFRQ YPALGNLFFW IGLMSGFPLL AALYIRC
//
