ID   A0A319FMV5_ASPSB        Unreviewed;       610 AA.
AC   A0A319FMV5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Carnitine acetyl transferase {ECO:0000313|EMBL:PYI11063.1};
GN   ORFNames=BO78DRAFT_304481 {ECO:0000313|EMBL:PYI11063.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI11063.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI11063.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI11063.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; KZ826319; PYI11063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319FMV5; -.
DR   STRING; 1448318.A0A319FMV5; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   PANTHER; PTHR22589:SF115; CARNITINE O-ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          33..587
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        324
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   610 AA;  69410 MW;  E5C9F4DC8CBFC36C CRC64;
     MAPRRKASSV PEGYKEDLSK GKMLRFEDSL PRLPVPSLEE TARRYLKSVH AVVSEAEYER
     TKKAVEVFVR PGGEGEPLQE RLLARAADPK TRNWILEWWN HAAYLGYRDP VIPYVSYFYS
     YRDDRARRNP AQRAASVTTA ALEFKRQVDD GSLEPEYMRS QPIAMSSYEY MFNCCRIPGD
     SVDYPQKYPA QANEHIVVVR KNQFFKVPLA VNGKRLNNSE LQRQFERIYE VAQPSPAVGV
     LTVANRDLWA DARKKLLAAH PANEQSLRDI ESSGFVVCLD NAAPVTLEER AHQYWHGDGT
     NRWFDKPLQF IINDNGTAGF MGEHSMMDGS PTHRLNDHLN NLIFNHKIDL SEQPVRSDLP
     DPRPITFHLD GPVLESIDAA TKEHRQQISS HELKVQAYQG YGKGLIKKFK CSPDAYVQMI
     IQLAYFKMYG KNRPTYESAS TRKFQEGRTE TIRTVSDDSV AFCNAISDPA VPREEAVRLL
     RSALAAHTKY TTEAGDGRGV DRHLFGLKKL LREGEKLPAL YEDPAFAYSS SWYLSTSQLS
     SEFFNGYGWS QVIDDGFGIA YMINENSLNF NIVCKRLGAE RMSYYLNEAA SDMRDMLMPD
     LAAQTEKAKM
//