ID A0A150VFZ9_9PEZI Unreviewed; 287 AA.
AC A0A150VFZ9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=M433DRAFT_150055 {ECO:0000313|EMBL:KYG49381.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49381.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG49381.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG49381.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG49381.1}.
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DR EMBL; JPDO01000025; KYG49381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VFZ9; -.
DR STRING; 766039.A0A150VFZ9; -.
DR Proteomes; UP000075602; 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 Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..287
FT /note="Phospholipid/glycerol acyltransferase domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007571620"
FT DOMAIN 65..187
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 287 AA; 33650 MW; 8BC36C0E479E5420 CRC64;
MHLFVADIVL SALFPVSFFL PDLCYDVCSR IAESVWRGIQ RIFTGTNGAQ ITVSGLKSVP
SRESAIVVSN HIEWTDFYLL QELAERSGML GRCRWFAKQE LKWVPFLGWG LWAMGMPLVS
RKWTHDQKEM DRVFDGLLKR RWPMWLIAYS EGTRFTPLKR LEAEAYCRMH NKRLGQHLLY
PRTKGFVASV QKLRHAPQMK AVYDVTLAYA KDKHFQSPPT FVQTVSLPRL GDQWKFFVHV
ERYSLESLPK TDAELMQWLE DRWIEKGERL EKLNQRLIDG IPWESIN
//
