ID A1CZI1_NEOFI Unreviewed; 418 AA.
AC A1CZI1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Acyltransferase, putative {ECO:0000313|EMBL:EAW24151.1};
GN ORFNames=NFIA_037250 {ECO:0000313|EMBL:EAW24151.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW24151.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; DS027686; EAW24151.1; -; Genomic_DNA.
DR RefSeq; XP_001266048.1; XM_001266047.1.
DR AlphaFoldDB; A1CZI1; -.
DR STRING; 331117.A1CZI1; -.
DR EnsemblFungi; EAW24151; EAW24151; NFIA_037250.
DR GeneID; 4592989; -.
DR KEGG; nfi:NFIA_037250; -.
DR VEuPathDB; FungiDB:NFIA_037250; -.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_3_2_1; -.
DR OMA; RMVMIAN; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000006702; 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.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:EAW24151.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAW24151.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..264
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 48618 MW; 2A9A8AEB70BADD94 CRC64;
MESPELRQRK PAPGLKGDDV VEKPRGFKDT EPRLKHGIPM QLLRSLLLAT WFNCCCIIIF
ATQLIGSPLY FINKDYYYSY MALTKQSFGL VITALTQWGC PTYVRVSGDE SVRGQIHLCK
DGRLKTEFPE RLVLIANHQV YTDWIYFWWI AYTNQMHGRI FIILKESLKY IPIIGQGMTF
YGFIFMARKW LSDKPRLQHR LEKLKTQRSG SKSESPQYDP MWLLIFPEGT NLSPNTKRRS
DEYGRKQGLP PLKHELLPRS TGLLFCLQQL KGTVDWVYDC TVAYEGPPKG SYPDKYFTLR
STYLQGRPPT SVNMYWRRFA MSDIPLDDQK EFDNWLRARW TEKDELLDEF FETGRFPTAL
AGSIDAGDVA DVQREAASKG FVEAHVRLHH WTELGRIFMV LTGMAFLCRL PKVFGLWD
//
