ID   A0A0P1BHK1_9BASI        Unreviewed;       881 AA.
AC   A0A0P1BHK1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-NOV-2023, entry version 26.
DE   SubName: Full=Histone acetyltransferase {ECO:0000313|EMBL:CEH15663.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH15663.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH15663.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|ARBA:ARBA00007937}.
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DR   EMBL; CCYA01000272; CEH15663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BHK1; -.
DR   STRING; 401625.A0A0P1BHK1; -.
DR   OrthoDB; 5478811at2759; -.
DR   Proteomes; UP000054845; 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:0044255; P:cellular lipid metabolic process; IEA:InterPro.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 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|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEH15663.1}.
FT   DOMAIN          290..417
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  97614 MW;  E0E3C5CC145728CA CRC64;
     MTPSPSDPPR KPGHASVPPP APSPEAGNDS EARTRELLGK RNLAASTRGI DSPQHLSTSA
     AAQSSVTTSP FAPAVSPIHA PAAAASSSSS PGATITADRQ DKAAESAWQH KMETTGGQNL
     NVVQTYKAHF REDPWTWFGQ MYQYGQGTGW RAYTDYIGSP ILYPTQSTEV VQSLAQSKQV
     QERIHALASS RVESLFATVP PPKTEEARKE LQRFKEKRRL ELERNLTDVA RGLAETNVAR
     LDSIKFLRGF AWSVESILAR LYHQGIHISV AQVLELRRVA SYCAERKISL LFAPSHSSHI
     DYLTLSWLMF RLGIAVPHIV AGENLDLPVL GNVLKRGGAF FIRRTFAGDQ LYPIVIKEYV
     EQLLASGKNI ECFIEGTRSR TGKRLPPKLG ILKYVVEALL NERTEDVFIA PVSVQYDSVI
     ESSTYADELL GKPKEAESLF GLLGSSSSVL QLKLGRIDVR FQTPWSLKGF INEQKLRREA
     PTPDHKSKME LDLFNNDEHK ILLLKALGYR ILNDVNNASI IMPAALCGTI LLILRGRGIG
     RSDLIKRVEW LAGIIRGKGY QVADFGSLST AEVVDRAITG VMKGLVEIET DVMEPTYVPV
     KRFELSFFRN QVMHVFVSEA LLCSALYTRV KQGGETPNQF MKREALVAEA GFISHVLREE
     FVFNSADKLE NNVRATVDQL VTDDVLAFDD QNRVGLSTRE RRVGRSNFDS YLFLVFPLIE
     AYWLSACSLL LLAPPPPKGQ APGSVQSWFA AKEFEKRAQL FGKTLYAGGE ISYLEAINLA
     TLSAAMVRFQ ELGFIVRRKS DGPKPVPLVA LNPAYVPTYN AEGRVTNTGP LVSFLERLSA
     FRREGKDRRD EGSVISERIG NVVRANFAPV VELTRLGESR I
//