ID   A0A319AVN9_ASPLB        Unreviewed;       820 AA.
AC   A0A319AVN9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Carnitine acetyl transferase {ECO:0000313|EMBL:PYH58903.1};
GN   ORFNames=BO96DRAFT_443949 {ECO:0000313|EMBL:PYH58903.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH58903.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH58903.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH58903.1,
RC   ECO:0000313|Proteomes:UP000247441};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; KZ821343; PYH58903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319AVN9; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR042572; Carn_acyl_trans_N.
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; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF29; MITOCHONDRIAL CARNITINE O-ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PYH58903.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          66..705
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        372
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   820 AA;  91022 MW;  4B4F720E72C19E31 CRC64;
     MSYSSVAVRH FTAPKPLGNT MDSIRSNSPP ETKIKPSSVP MSVNGGTSEP PKKGLTFANQ
     DSLPKLPIPD LEQTCKRYLE ALAPLQTPRE QDETRAAVQD FLKSEGPILQ EKLKTYASSK
     TSYIEQFWYD SYLNYDSPVV LNLNPFFLLE DDPTPARNNQ VTRAASLVVS ALSFVRAVRR
     EELPPDTVRG TPLCMYQYSR LFGTARVPTD NGCVISQDPH AKHIVVLCRG QIYWFDVLDD
     NNDLIMNEKD IAVNLQVIIG DAEQTPIHDA AKGALGVLST ENRKVWSGLR DILTKDEGSN
     NAECLNIVDT ALFVLCLDYT EPHNTSELCA NMLCGTSEVV RGVQVGTCTN RWYDKLQIIV
     CKNGSAGINF EHTGVDGHTV LRFASDVYTD TILRFARTIN GQAPTLWATS SPDPAKRDPR
     SFGNVSTTPR KLEWDMVPEL SIALRFAESH LSDLLQQHEF QVLDFKGFGK NFITSMGFSP
     DAFVQMAFQA AYYGLYGRME NTYEPAMTKV FLHGRTEAIR TVTNECVDFV KTFWGDNPAE
     QKVSALRKAT EKHTAITKDC SKGQGQDRHL YALYCLWQRS FDDGASSANN SVISSSNGYT
     SPVETASIDS PKSSTSLSED GLSSNGYSVR GVRTMPAIFS DAGWDKINTT VLSTSNCGNP
     CLRHFGFGPT SADGFGIGYI IKDDSISFCA SSKHRQTARL MYTLESYLME IRKLLRTVTH
     RPASPRTSRA REMEMIAERL QGDHRRGRIV RGDPGQLHRG AETPTTDSGE LEDDGMGGYG
     FFDAGMLLHA LKGLNADRER GADKPEKRRF VGKKLRLNDY
//