ID G2X3Y6_VERDV Unreviewed; 411 AA.
AC G2X3Y6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-MAY-2023, entry version 41.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:EGY23285.1};
GN ORFNames=VDAG_04723 {ECO:0000313|EMBL:EGY23285.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY23285.1};
RN [1] {ECO:0000313|EMBL:EGY23285.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY23285.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; DS572702; EGY23285.1; -; Genomic_DNA.
DR RefSeq; XP_009652622.1; XM_009654327.1.
DR AlphaFoldDB; G2X3Y6; -.
DR STRING; 498257.G2X3Y6; -.
DR EnsemblFungi; EGY23285; EGY23285; VDAG_04723.
DR GeneID; 20706186; -.
DR KEGG; vda:VDAG_04723; -.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_3_2_1; -.
DR InParanoid; G2X3Y6; -.
DR OMA; RMVMIAN; -.
DR OrthoDB; 2906776at2759; -.
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:EGY23285.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 136..269
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 47363 MW; 939172E866631BE8 CRC64;
MAAELPDPAP KTTVFPALKP EAGAGGKTPE LAHPAGRAKH GTLMQIVRGF TWAAYFVCCC
VAIGTTQFLG APLYYIRRDL YYAYMALTKQ SFALLTTTMT QWWGPTKIRI SGDASVAHQM
RQQPDGMVEF DFPERLVLVA NHQIYTDWLY LWWIGYANTP RMHGHIYIIL KESLKWIPFI
GWGMMFYGFI FMSRKMATDR PRLAHRLGQL KTTQRAPDGT SFLSPMWLLL FPEGTNLALN
GRTKSAAWAE KTGLRDGEHV LLPRSTGMYF CLKELGDTVD YVYDCTVAYE GIPRGKFGQD
YFTLSSTYFQ GRPPRSVNFH WRRFKVSEIP LETADAFELW LRARWYEKDA LMEQYLSTGR
FPPLVGHKQD YIESEIRTKN WWDFSQIFVV FAAFSLLCRI FVLQWVRFTG A
//
