ID B2VVT3_PYRTR Unreviewed; 420 AA.
AC B2VVT3;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase 2 {ECO:0000313|EMBL:EDU40733.1};
GN ORFNames=PTRG_01295 {ECO:0000313|EMBL:EDU40733.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU40733.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; DS231615; EDU40733.1; -; Genomic_DNA.
DR RefSeq; XP_001931628.1; XM_001931593.1.
DR AlphaFoldDB; B2VVT3; -.
DR STRING; 426418.B2VVT3; -.
DR EnsemblFungi; EDU40733; EDU40733; PTRG_01295.
DR GeneID; 6338801; -.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_3_2_1; -.
DR InParanoid; B2VVT3; -.
DR OMA; RMVMIAN; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
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; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:EDU40733.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDU40733.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 136..262
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 420 AA; 48529 MW; 3DF0D47D9D8A6D64 CRC64;
MTTKGLRLRQ PPVSVPVIEK LKAQRTKTPD PTKHPAGKVK HGLFTQTLRM YLFGVYFAIS
IIAIAITQYI GLPLYFYSRD LFYAWMAMSK QHFGSVVMTM TYWWAPVTMR VSGDESVRGQ
LRKSKDGKLE CDFPERLLYT DWVYIWWTCY TASMHGHLYI ILKESLKYIP VLGWGMKLFG
FIFLSRKWST DKERFQHRLR KLSTSHSGPL SGSKGLDPMW LLIFPEGTNL STNGRESSQR
WAAKNNMPDL RHALLPRSTG LSFCLQELKG SIGHLYDCTV AYEGVPVGQY GQDLFTLRGT
YFQGRPPKSV NMYWRRFAIA DIPLHDEKEF SDWLLARWRE KDDLLQYFVE HQRFPADDGV
TPNVNGGEPL QGPGWIETDI RPNRWWEWLQ IFVPTAALGL VVNVFVKIAG IVMKVARVRD
//
