ID K8YP17_NANGC Unreviewed; 409 AA.
AC K8YP17;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Lysophosphatidylglycerol acyltransferase {ECO:0000313|EMBL:EKU20395.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:EKU20395.1};
GN Name=LPAT {ECO:0000313|EMBL:EKU20395.1};
GN ORFNames=NGA_0546500 {ECO:0000313|EMBL:EKU20395.1};
OS Nannochloropsis gaditana (strain CCMP526) (Green microalga)
OS (Microchloropsis gaditana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=1093141 {ECO:0000313|EMBL:EKU20395.1, ECO:0000313|Proteomes:UP000009377};
RN [1] {ECO:0000313|Proteomes:UP000009377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP526 {ECO:0000313|Proteomes:UP000009377};
RX PubMed=22353717;
RA Radakovits R., Jinkerson R.E., Fuerstenberg S.I., Tae H., Settlage R.E.,
RA Boore J.L., Posewitz M.C.;
RT "Draft genome sequence and genetic transformation of the oleaginous alga
RT Nannochloropis gaditana.";
RL Nat. Commun. 3:686-686(2012).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; JH470636; EKU20395.1; -; Genomic_DNA.
DR RefSeq; XP_005855952.1; XM_005855890.1.
DR AlphaFoldDB; K8YP17; -.
DR EnsemblProtists; EKU20395; EKU20395; NGA_0546500.
DR GeneID; 17362730; -.
DR KEGG; ngd:NGA_0546500; -.
DR OMA; DHESACV; -.
DR OrthoDB; 3012482at2759; -.
DR Proteomes; UP000009377; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:EKU20395.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKU20395.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..271
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 46811 MW; 81202AA7DBC251A4 CRC64;
MSTSLSAPPP TRESGHVGSR PNSTSQEKKE GSKRRYAKEV SDSLWADALA YLLAIVILLN
FWSAAFLELV MYVVFYPLCP SIWYVTRILG VRFGWLFPML CLKWSNVRIR MTGKGAAATS
LGAIPPSPFS FSSSWQRYRD LLTPGKLPRA LIMINHLSWA DTFVLSPWLH AHNSVNGDTC
WPMWKGFMQM PLGWIAYMSE CPVLGYGKEV DLKTIHRSVT RFFERRMTKF FLFPEGAVFR
EEMRSKSHQY ATANKLPLLD HCLLPKHGAF YRAGKELHRQ GMTTLVDLTL AYPPASSLYD
APFNVLDLVK RHAKPLYLPL HVRTFAMSEV PWDEEGKVQD WLNQRFMEKD KMLEEYYQNN
GGALVEGAVE EGSRWQDLLM DLCVWIVLQA VMYGALLYLG RRMLGYGPV
//
