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Database: UniProt
Entry: M2ZP03_PSEFD
LinkDB: M2ZP03_PSEFD
Original site: M2ZP03_PSEFD 
ID   M2ZP03_PSEFD            Unreviewed;       790 AA.
AC   M2ZP03;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=O-acyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MYCFIDRAFT_208180 {ECO:0000313|EMBL:EME80819.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME80819.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME80819.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME80819.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. 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}.
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DR   EMBL; KB446560; EME80819.1; -; Genomic_DNA.
DR   RefSeq; XP_007928193.1; XM_007930002.1.
DR   AlphaFoldDB; M2ZP03; -.
DR   STRING; 383855.M2ZP03; -.
DR   GeneID; 19336655; -.
DR   KEGG; pfj:MYCFIDRAFT_208180; -.
DR   eggNOG; KOG0380; Eukaryota.
DR   HOGENOM; CLU_018190_2_1_1; -.
DR   OrthoDB; 9612at2759; -.
DR   Proteomes; UP000016932; 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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        288..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        763..782
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          127..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  91047 MW;  B7B60BC74D7DA94A CRC64;
     MFFTFFLNSR HRWRVRRRFY IGISTGARAG SWGSGKWRGS TPRLAWSSAL VSRVKRQHPC
     PRCGTMTARH THASTCIRPA LPNKDTLDVA RLTGTLGHNG VAELPPGSPK SNKNASLNAS
     LARYPQSVQG TSDSFGHSVS LPQSDDSAVS SDIDDAIENY DQLQLDPDTL ILNTRRSLDE
     AYRPSNSKME GKEQNGEQEE SASEAKRGHK KRNSIQIRLA RTDRKGKYIL TADDPEIKAI
     LRKGIEREAE EAEGKIKKPP RINFRDLVFT RRFTTFDRQN PASADSPFFG FFTLFWICMF
     LIFFQVALRN WRDYGSWLGG NQIMRMMFTR DVFLLGVTDG VMWIATFEGY FFQKLVSRGY
     ISWGRSGWVV QNIWQMAYLG SVIGWAHFRQ WPWTHTIFVV LHGLVFLMKQ HSYAFYNGYL
     SGVYRRKRLL EQKLKDLENL EPLLSPPTSP TSPRESFIEV SSSVDLSPKT DDMKRRRPST
     GPRTSTNFKK EHSLVASVAA AIESGQSLTA DQMSTMSDIV KHEISDLEKE LRGKSDSNAK
     AYPNNLTLGN YIEYTCFPTL VYELDYPRQE RTNWWYVLEK SVATFGVLCV MQVISQGFIY
     PLVRRSLDMK ETNMPLEDRW REFPFIVSDM LFPMLIEQLL TWYVIWECIL NVLAEVTRFA
     DRGFYGDWWN SVTWDQYARD WNRPVHNFLL RHVYHSSIST FHLSRKAATF VTFLLSALVH
     EMCMALIFSK VRGYLFWMQL LQMPLVAFSR SKFMKGRTVL GNAIFWTGLF IGPALLTSLY
     LWKSGVLRFV
//
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