ID A0A5N6EZH1_9EURO Unreviewed; 624 AA.
AC A0A5N6EZH1;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 22-FEB-2023, entry version 6.
DE SubName: Full=Lecithin:cholesterol acyltransferase-domain-containing protein {ECO:0000313|EMBL:KAB8222767.1};
GN ORFNames=BDV33DRAFT_56148 {ECO:0000313|EMBL:KAB8222767.1};
OS Aspergillus novoparasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=986946 {ECO:0000313|EMBL:KAB8222767.1, ECO:0000313|Proteomes:UP000326799};
RN [1] {ECO:0000313|EMBL:KAB8222767.1, ECO:0000313|Proteomes:UP000326799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 126849 {ECO:0000313|EMBL:KAB8222767.1,
RC ECO:0000313|Proteomes:UP000326799};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Petersen T.I., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Pangilinan J., Riley R., Salamov A., Simmons B.A., Magnuson J.K.,
RA Henrissat B., Mortensen U.H., Larsen T.O., De vries R.P., Grigoriev I.V.,
RA Machida M., Baker S.E., Andersen M.R.;
RT "Fungal friends and foes A comparative genomics study of 23 Aspergillus
RT species from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; ML733410; KAB8222767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6EZH1; -.
DR Proteomes; UP000326799; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR PANTHER; PTHR11440:SF97; BCDNA.GH02384; 1.
DR PANTHER; PTHR11440; LECITHIN-CHOLESTEROL ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF02450; LCAT; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:KAB8222767.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000326799};
KW Transferase {ECO:0000313|EMBL:KAB8222767.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 69839 MW; A749D0B7066DC836 CRC64;
MLRRRLAKDD NVQSASTDSS HDESKVIPAT QTATPPEKPK KESFVTKPRS KRRNGLIFVL
GGIFGIIVAA FFANQQDVIS LEALMDLNLD TLMDVIPQGI VKDVREFSQH ERDAVSYDSF
SVGLQLQSQG IQAKHPIVMI PGVISTGLES WGTEVSSRQY FRRRLWGSWS MMRALVLDKA
EWKNHIMLDK DTGLDPPGIK LRAAQGFDAT DFFITGYWIW NKILENLATI GYDPTNAFTA
AYDWRLSYLN LEIRDQYFSR LKSYIETAVL VKGEKVALAS HSMGSQVLFY FFKWVEHPEH
GKGGSDWVNR HVASWINISG CMLGAVKGLT AVLSGEMRDT AQLNAFAVYG LEKFLSKEER
AEIFRAMPGI SSMLPKGGEA VWGNATWAPD DLPGQHTSYG NLLKFQQTNS SLTAKNLTVS
ESLAYLMNSS DEWYRNQVQT SYSHGVAHTT AQVEANENDP RTWLNPLEAR LPLAPDMKIY
CFYGVGKPTE RSYYYQEERD PLVNLNVSID TTVTNSDGVD HGVVMGEGDG TVNLLSTGYM
CAKGWNIKRY NPAGVKIKVF EMPHEPDRFS PRGGPNTGDH VDILGRASLN ELILRVAGGH
GDEIEETFVS KIKEYADRVQ IFEE
//
