ID A0A200QFE0_9MAGN Unreviewed; 504 AA.
AC A0A200QFE0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:OVA09107.1};
GN ORFNames=BVC80_9097g204 {ECO:0000313|EMBL:OVA09107.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA09107.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA09107.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA09107.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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:OVA09107.1}.
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DR EMBL; MVGT01002224; OVA09107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QFE0; -.
DR STRING; 56857.A0A200QFE0; -.
DR InParanoid; A0A200QFE0; -.
DR OrthoDB; 383266at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06551; LPLAT; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.1440.100; SG protein - dephosphorylation function; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR15486; ANCIENT UBIQUITOUS PROTEIN; 1.
DR PANTHER; PTHR15486:SF25; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE RAM2; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF12710; HAD; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:OVA09107.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Transferase {ECO:0000313|EMBL:OVA09107.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 305..406
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 504 AA; 55400 MW; AD96488ACBDC42AC CRC64;
MAKTNSLMFP TINKCASIGR EKHTVVADMD GTLLRGRSSF PYFALIAYEA GGVLRLLFLL
LLAPLAGFLY YLVSESAGIQ ILIFATFTGM KVSDIESVAR AVLPKFYSND LHPESWRVFS
SCGKRCVLTA NPRIMVEAFL KDYLGADMVI GTEIRTYKGV ATGLVCSPGI LVGTKKADAL
RDAFGETIPD IGLGDRHTDF PFMTLCKESY VVPANPEVEA VSRDKLPKPV VFHDGRLVLK
PTPLKALIII LWIPVGIILA CLRIAAGSLL PMQLVYYAFW ALGVRVYIKG TPPPPAKKST
SQTGVLFICS HRTLLDPIFL STALGRPIAA VTYSVSRLSE IISPIKTVRL TRDRVNDAAM
IKKLLEEGDL VICPEGTTCR EPFLLRFSAL FAELTDQIVP VAMANRMSMF HGTTARGWKG
MDPFYFFMNP SPAYEVTFLN KLPEDLSCSA GKSSHEVANY IQRVIAASLS YECTSFTRKD
KYRALAGNDG IVVEQPKLAP NKKT
//
