ID A0A0D2DAS4_9EURO Unreviewed; 840 AA.
AC A0A0D2DAS4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=PV05_03859 {ECO:0000313|EMBL:KIW59407.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW59407.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW59407.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW59407.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) 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; KN847318; KIW59407.1; -; Genomic_DNA.
DR RefSeq; XP_013319991.1; XM_013464537.1.
DR AlphaFoldDB; A0A0D2DAS4; -.
DR STRING; 348802.A0A0D2DAS4; -.
DR GeneID; 25325767; -.
DR HOGENOM; CLU_016735_0_0_1; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000054342; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 126..248
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 552..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 91707 MW; F7672DD7FC15E33E CRC64;
MATAQPALEP AAGFSLESRA NRPDRVPLQK GQYSIASRAV ALSTYFLSGA LAINLSQFLG
APLALVNEDW YNAWIAFTKQ SFGLLTMTLT QTFAPTKVIV SGDASVRGQL LKSVEGDLVL
DFPERLVLIA NHQIYTDWLY LWWIAYCNGM HGRLYIILKE SLKKIPILGW GMQFNQFIFL
KRNWEQDRPN MATALQKLNK LADPMWLLLF PEGTNLAPST RAKSAAWAKK NNISDTRHVL
LPRSTGLHFC LEQLKDSVDY VYDCTVAYEG VPRGQYAQDI FTLKSGYLEG RPPKSVSMHW
RRFLVKDIPL HNEKAFELWL LARWREKDVL IEQWYQTGRF PADVGVTKYK SGKTLRGCGL
MEVPIRSSHW YEFLQIFAPM GILAMVLYIF YGDLPQRFWR SINKQALQAG TEDVKKAGVQ
AGKQVKSAST SLSGLTLDSF FDPEQQKESF KAGAMAVQKL INSPSAQMLL NRADFIQQFL
SDPQGMVTES ITNKQQSFMQ QLAEEEARRQ RGRITEVNNI PSLAPNGVKR ITNGVSAKNG
TGTFWSKLDA EEKSRQGSVV SGPRSTAGKK QKGTFWHDLE AAENKRTAPI SRGKGKGNFW
DDLKTEENSR YGTVVTLSSD ASTAVASMDS TSTKGSVPKL GPRKAPSAAG LGQARQGTKI
SSASPVPVPK TAPTKTPAAK GSRMTGAATT VKKPNASMPT PAPATKSAPK PVSTQAKATS
NHRTTQTPSR PAPTGASKPT GASKLSTNNL TATPKPSNTI STTSTAKKPP QKTSTSAAAT
KIPPVKKVPN QPSARSNAAA VPKKPNSTST AVSKPPNLSN ANSITPKKTS TGRAKLKSKT
//