ID   A0A166V4R4_9AGAM        Unreviewed;       430 AA.
AC   A0A166V4R4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=FIBSPDRAFT_722715 {ECO:0000313|EMBL:KZP32349.1};
OS   Fibularhizoctonia sp. CBS 109695.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX   NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP32349.1, ECO:0000313|Proteomes:UP000076532};
RN   [1] {ECO:0000313|EMBL:KZP32349.1, ECO:0000313|Proteomes:UP000076532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP32349.1,
RC   ECO:0000313|Proteomes:UP000076532};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV417486; KZP32349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166V4R4; -.
DR   STRING; 436010.A0A166V4R4; -.
DR   OrthoDB; 2906776at2759; -.
DR   Proteomes; UP000076532; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10983:SF16; LYSOCARDIOLIPIN ACYLTRANSFERASE 1; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          138..260
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   430 AA;  46776 MW;  00E9C85F31C2CE1D CRC64;
     MTTPPAAPAL HTIPVILRPP KTWAQTANRA GFALVFNLGA GMIHLVQLCV LLPLAIIGAV
     LPGGRGRWVR GVYEDGARYC KGACATLLVL ATQWFAPTTL RLTFETTGQG ALSPAQLADL
     VVRDASGRVI KLNLPQQSVM ISNHQVYADW WYAWCFTYFC DTHRDVIIVL KKSLKWVPFL
     GWAMQFFSFI FLARSWASDR AQLASALAAA AGPPAPLALL LYPEGTLVSP HTRPVSARYA
     AQHGLAHPAH VLLPRATGLH YSLRALVGGG ARALSLVDLT IVYPGVPAAG GSEREEDYAQ
     GYYTLRSIFF DRVPPPVVHI HVRVFDVVRE VPIGEMGGGD APAATLEPAA EVEFSESERA
     AFDVWLRQLW TDKDALIARF LATGSFGPAA DATRVDVPVQ LKTRREALDA FAFFVPGVVG
     VVWARMKHLL
//