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Database: UniProt
Entry: A0A1W5CYK1_9LECA
LinkDB: A0A1W5CYK1_9LECA
Original site: A0A1W5CYK1_9LECA 
ID   A0A1W5CYK1_9LECA        Unreviewed;       566 AA.
AC   A0A1W5CYK1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase gamma {ECO:0000313|EMBL:SLM35815.1};
OS   Lasallia pustulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC   Lasallia.
OX   NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM35815.1, ECO:0000313|Proteomes:UP000192927};
RN   [1] {ECO:0000313|Proteomes:UP000192927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma R., Thines M.;
RL   Submitted (MAR-2017) 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; FWEW01000824; SLM35815.1; -; Genomic_DNA.
DR   OrthoDB; 2906776at2759; -.
DR   Proteomes; UP000192927; 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   ECO:0000313|EMBL:SLM35815.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SLM35815.1}.
FT   DOMAIN          124..246
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  62691 MW;  35D89BCAF1E005FA CRC64;
     MSTSKLDLGA GVSNTVKEPF PPGIPGQHGE ASQFSRILAL GSYFLSGCMA INASQFLGAP
     LYLVNENWYN AWIAFTKQSF GLLTTTMTQC WAPTVIRASG DSSVRGQLLK TADGNLLCNF
     PQRLVLIANH QIYTDWMYLW YIAYTAGMHG RLFIILKESL KRIPVLGWGM QLSQFIFLKR
     NWEKDKPNMA EHLQKLNQAA DPMWLLIFPE GTNLAPDTRE KSQAYAEKRG IRDMYHQLLP
     RTTGLEFCLQ QLRQTVGYVY DCTIAYEGVP RGEYAQDIFT LRAAYVEGRP PKSVNMYWRR
     FAVSSIPIDN PKAFEVWLLN RWYEKDNLIE YFHRNGRFPA DFGIETTPSG KTRRGAGYIE
     SEIKSFRWYE FMQIFAPIGL IGLVLYSFYG SLPGNVLKAI GDKVGAAEQE QSQIQQPQKX
     PLTAPPRPAS GIAAKKAPKL PAKRTPARQA PAKATIPLKA APAANPTKQP TTNPAKKPQP
     KTKQAATPNP PKLDVKRALP PTAKKPALKP AAKPAVKPAA TKVTSDAKSE TSAAPKKLAP
     RPKPNPAVLK STAAKAAAPK KVEKKA
//
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