ID K2S581_MACPH Unreviewed; 334 AA.
AC K2S581;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:EKG11885.1};
GN ORFNames=MPH_10927 {ECO:0000313|EMBL:EKG11885.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG11885.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG11885.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG11885.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG11885.1}.
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DR EMBL; AHHD01000465; EKG11885.1; -; Genomic_DNA.
DR AlphaFoldDB; K2S581; -.
DR STRING; 1126212.K2S581; -.
DR VEuPathDB; FungiDB:MPH_10927; -.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_6_0_1; -.
DR InParanoid; K2S581; -.
DR OrthoDB; 1289at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
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:SF24; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 3, ISOFORM E-RELATED; 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:EKG11885.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKG11885.1}.
FT DOMAIN 101..224
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 334 AA; 37579 MW; 8B2CFF0779D76C9C CRC64;
MPPPPATTRL PAPAAALAHA TRALRGVAVL SPWLAHLLAV DLILSLLLPF KWAAPTPVYN
ASSLLAYSVW AWIQAIFTRA NRADIVLSTN CPRGLPRGES AVVVANHVAW SDFYMIQEAA
RRSGMLARCR WFAKRSLRWV PFLGWGLWAM GMPLVSRKWA TDRAELEKVF RGIVCKRWPV
WLIAYSEGTR FTPTRHTAAA AFCARANKPA PSPYTLVPRP RGFVATIGAL RATPHVRAVY
DVTIAYARGR DFMRAPTFWE TVASGDLRGD GYRFYAHIER WEMDALPTEE DDLARWLEER
WVEKGRRLEG LRAQLERGEE WVGDDEVGAG KKDS
//
