ID E3RT83_PYRTT Unreviewed; 427 AA.
AC E3RT83;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=PTT_12199 {ECO:0000313|EMBL:EFQ91063.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ91063.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ91063.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; GL534958; EFQ91063.1; -; Genomic_DNA.
DR RefSeq; XP_003300838.1; XM_003300790.1.
DR AlphaFoldDB; E3RT83; -.
DR STRING; 861557.E3RT83; -.
DR EnsemblFungi; EFQ91063; EFQ91063; PTT_12199.
DR KEGG; pte:PTT_12199; -.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_3_2_1; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000001067; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..269
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 427 AA; 49260 MW; EF0EE5FF9D0E6640 CRC64;
MTTKGLRLRQ PPVSIPVIEK LKAQQTKTPD PTQHPAGKIK HGFFAQTLRM YLFGVYFAIS
IVAIAISQYI GLPLYFYSTD LFYAWMAMTK QHFGSVVMTM TYWWAPVTMR VSGDESVRGQ
LRKSKDGKLE CDFPERLVLV ANHQLYTDWV YIWWTCYTAS MHGHLYIILK ESLKYIPVLG
WGMKLFGFIF LSRKWSTDKE RFQHRLRKLS TSHSGPLSGS KGLDPMWLLI FPEGTNLSTN
GRESSQKWAA KNNMPDLRHA LLPRSTGLSF CLQELQGSIG HLYDCTVAYE GVPVGQYGQD
LFTLRGTYFQ GRPPKSVNMY WRRYAIAEIP LHNEKEFSDW LLARWREKDD LLQYFVENQR
FPADHGITPN VNGGEPLKGP GWIETDIRPN KWWEWFQIFV PTAALGLVVN VFVKIAGIVM
KIARVRD
//
