ID G0W3U7_NAUDC Unreviewed; 736 AA.
AC G0W3U7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 22-FEB-2023, entry version 39.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN Name=NDAI0A03280 {ECO:0000313|EMBL:CCD22485.1};
GN OrderedLocusNames=NDAI_0A03280 {ECO:0000313|EMBL:CCD22485.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22485.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD22485.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE580267; CCD22485.1; -; Genomic_DNA.
DR RefSeq; XP_003667728.1; XM_003667680.1.
DR AlphaFoldDB; G0W3U7; -.
DR STRING; 1071378.G0W3U7; -.
DR GeneID; 11495509; -.
DR KEGG; ndi:NDAI_0A03280; -.
DR eggNOG; ENOG502QQ2N; Eukaryota.
DR HOGENOM; CLU_007860_1_0_1; -.
DR OMA; IMALGCM; -.
DR OrthoDB; 2728187at2759; -.
DR Proteomes; UP000000689; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProt.
DR CDD; cd07992; LPLAT_AAK14816-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR31605; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR31605:SF0; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 442..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..300
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 REGION 637..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 82837 MW; 5BF5011893103467 CRC64;
MDKPLVSRSE KSAPPASNIT NNKPKKDTTT QSSSLEEYKY EEPSRFRKFC YDTIVFILSN
IFSCFFREIK SRNAYKIPSD GPIIFVAAPH ANQFVDPVIL MEQVKKVVNR RISFLIAEKS
LHQPAIGFFA RCVMAIGVVR AQDNLKLVPN GAKIFIKDPK ENPRKITGVN THFLTAFHAK
GLIGLPKNMG TAEILSIESD TELTLRKEFK NFANKPDLQN LLLKGTSFKY TDKVNQSSVY
HKVFEHLANN DCIGIFPEGG SHDRTDLLPL KAGVAIMALG CMDKHPDVNV KIVPCGMNYF
HAHKFRSRGV VEFGDPIDIP KELAAKYSNS DTNKEAVKEL LDTISEGLRA VTVTCSDYET
LMVVQAMRRL YSAHFASKLP LPLIVEMNRK MVKGYETYRD DPVVIKLRED VMKYNANLSH
YNIPDHQVED AKMSFTTNLG LLVYRAIFLT ITFILALPGI IMFSPVFILA NRISKRKARE
ALAASSVKIK ANDVIATWKI LIGMGAAPLL YIFWSVLISY YFSKRGSTYD KIFLFVSTYI
CCVIVTYSAL IVGDLGMDIL KSLRPLYLSL TSPKALKELR NERELLAARI IEVVNTFGTE
LFPEFQPELL REEYGSDEDT KEDRKTAELK RRRLLKKKRA KMERRKQENE NSDDNIDNHG
QESDGVSLVN SDNSLSNIPI FSTPTGFGSE ISITRSDSSV SDFEIEDDVI GGKGNLAAKI
AQAVLNSRSQ QNEHID
//