ID F2TI38_AJEDA Unreviewed; 408 AA.
AC F2TI38;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:EGE82888.1};
GN ORFNames=BDDG_05832 {ECO:0000313|EMBL:EGE82888.1};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE82888.1};
RN [1] {ECO:0000313|EMBL:EGE82888.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE82888.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) 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; GG749440; EGE82888.1; -; Genomic_DNA.
DR AlphaFoldDB; F2TI38; -.
DR HOGENOM; CLU_041844_3_2_1; -.
DR Proteomes; UP000007802; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGE82888.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..248
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 345..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 47121 MW; 9701A995AB194F5B CRC64;
MDGVSGKVLG HVHQRPAANY GLTIQILRSL ALLTWFNCCC VCIVATQLVG APLYFINRQY
FNSYMAMTKR SFGIAITALT EWGCPTPIRV SGDKSVQGQF SLTKDGNVET SFPERMVLIA
NHQVYTDWLY LWWFSYTSQM HGHIYIILKE SLKYIPLIGQ GMMFYGFIFM ARKWISDKPR
LQHRLEKLKT VHEEGRSGSR VLDPMWLLIF PEGTNLSRNT KRISDAYGAK QGIPPLRHQI
LPRSTGLFFC LQQLKGTIDW VYDCTVGYEG PPKGSYPDAY FTIRSTYLKG RPPKVVNFYW
RRFAVAEIPL DDQKEFEAWI HERWLEKDDL LERFYETGRF PPCEWEPSSN GDLQKQNEDG
ASVKPNNPSY YESAVKLTWW GESLQIFAVL VGLGAFFCLF PRFWRVGT
//
