ID A0A1E5R2J7_9ASCO Unreviewed; 393 AA.
AC A0A1E5R2J7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE SubName: Full=Putative acyltransferase CST26 {ECO:0000313|EMBL:OEJ81104.1};
GN ORFNames=AWRI3579_g4212 {ECO:0000313|EMBL:OEJ81104.1};
OS Hanseniaspora osmophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ81104.1, ECO:0000313|Proteomes:UP000095728};
RN [1] {ECO:0000313|Proteomes:UP000095728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(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:OEJ81104.1}.
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DR EMBL; LPNM01000011; OEJ81104.1; -; Genomic_DNA.
DR STRING; 56408.A0A1E5R2J7; -.
DR InParanoid; A0A1E5R2J7; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000095728; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProt.
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:OEJ81104.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000095728};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OEJ81104.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..258
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 393 AA; 44841 MW; 19AC6EF0223A12E0 CRC64;
MVVYKLKKIC VLTFSIWVFL LGAVSIVSMQ AVVKLVFRSN PVYQQQCLNY TKKSFILLLL
TIFQIAAPSR IRVSTENSSV APDTVSVDPR TGRIVSKXSK SSVLIANHQI YTDWVFLWWL
NYTAKLGGNV FIMLKKSLAS IPILGSGMKN FKFIFLSRKW DLDRVCLHNS LSDINANALG
CGRISGNHPQ SVSQDGTXIW GDRMYENKNN VHWPYCLMIF PEGTNLSANT RQKSEAFAEK
IGRKPFRHVL LPHVTGLREI LTKLRVSCDV VYDVSIGYSG VAANEYGQDI YKIMDVFMKG
KQPKLVDIHI RSFKLDTIPV KDEQAFTKWL FDVWEEKDEY MEHYYKHGNF NLTNDTTSAE
AECTVSLWEY LLILAMPVXS VLIAFLLVLK KVF
//
