ID M7U5N6_BOTF1 Unreviewed; 819 AA.
AC M7U5N6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE SubName: Full=Putative glycerol-3-phosphate acyltransferase protein {ECO:0000313|EMBL:EMR81908.1};
GN ORFNames=BcDW1_9463 {ECO:0000313|EMBL:EMR81908.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR81908.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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DR EMBL; KB708063; EMR81908.1; -; Genomic_DNA.
DR AlphaFoldDB; M7U5N6; -.
DR STRING; 1290391.M7U5N6; -.
DR HOGENOM; CLU_015023_0_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:InterPro.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 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:EMR81908.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMR81908.1}.
FT DOMAIN 211..338
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 788..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 92625 MW; 9A250959D392383E CRC64;
MADNKTSSPP RTSAPDLEIL GDQVTLHPSG YIEPPERPHD GEKERNLVEH MARFRSSPLE
FLREVSLHVS GTGWRAYNHF IGQPIFYPGF SENMTAAVMS TPILQTRISE LAEKRIGIEE
QEGLLNKDDP LYHSKRSQRK SAIEQSLQEL SEKLTSDMIC KMESRPFIRG AYYLCTQLLT
RAYHQGIHVS SEEVLRLRNV AEKAQKDKTS IIFLPCHRSH VDYVSLQLIC YRLGIALPTV
VAGDNLNFPV VGSFLQHAGA MWIRRSFGDD ALYTTLVQSY IDTLLQGGYN FECFIEGGRS
RTGKLLPPKF GILSFILDSI LSGRVKDTII CPVSTQYDKV IETEGYVGEL LGIPKKKENL
ADFLSASSVL SLKLGRVDVR FHEPWSLRDF ILQQQARSLG IPKTLDFESI NVPSVRQKLL
RTLGYKVLSD INAVSVVMPT ALVGTVLLTL RGRGVGKSEL IRRVEWISER VRNKGGRVAH
FAGATTSTVV ERALEVLGKD LVGRVDGLAE ETYYAVDRFQ LSFYRNMTIH LFISEALVSA
SMYMNVKRGG GKVHQNISYE ELRSQVQFLS QLFRGEFIYP TEGLVVNLDN TLHDLETDNI
VELIRDSEGK ITTVGLSDHE RSVGRENYDF YCFLIWPFVE AFWLGAVSLM GFTPPPSKPD
NVWLEVKKAH DGAQLLGKTL YHQGDLSYFE AVNKETLKNA YQRFEDEGIV IVSKSRNSKI
PPRSRLAPEW TPQRNPETSM IIAEGKLWDF IEKIAKSRRE GKNRRDGATV STRVLRLADE
LGQTLFAEGS GDMRMSEEDK EELQRREKRR QALKARAHL
//
