ID   A0A319AI69_9EURO        Unreviewed;       814 AA.
AC   A0A319AI69;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Carnitine acetyl transferase {ECO:0000313|EMBL:PYH46322.1};
GN   ORFNames=BP01DRAFT_397592 {ECO:0000313|EMBL:PYH46322.1};
OS   Aspergillus saccharolyticus JOP 1030-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH46322.1, ECO:0000313|Proteomes:UP000248349};
RN   [1] {ECO:0000313|EMBL:PYH46322.1, ECO:0000313|Proteomes:UP000248349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH46322.1,
RC   ECO:0000313|Proteomes:UP000248349};
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; KZ821228; PYH46322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319AI69; -.
DR   STRING; 1450539.A0A319AI69; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000248349; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PYH46322.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          62..701
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          15..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        368
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   814 AA;  90273 MW;  1EE86493F7A0C9AF CRC64;
     MSYSSVAVRY FTAPKPLGSA MDPARSQPSS DPAPKPSPAP LTVNGSIKPG LTFANQDSLP
     KLPIPELEQT CKKYLEALAP LQAPREQDET KAAVQDFLRL EGPVLQEKLK NYASSKTSYI
     EQFWYDSYLN YDSPVVLNLN PFFLLEDDPT PARNNQVTRA ASLVVSALSF VRAVRREELP
     PDTVRGTPLC MYQYSRLFGT ARVPTDNGCV ISQDPHAKHI VVLCRGQFYW FDVLDENNDL
     IMNEKDIAVN LQVIIGDAEQ TPIQDAAKGA LGVLSTENRK VWSGLRDILT KDEGSNNAEC
     LNIVDTALFV LCLDYTEPHN TSELCANMLC GTSEVIRGVQ VGTCTNRWYD KLQIIVCKNG
     SAGINFEHTG VDGHTVLRFA SDVYTDTILR FARTINGQAP SLWATSSPDP AKRDPRSFGN
     VSTTPRKLEW DMAPELSIAL RFAESHLSDL LKQHEFQVLD FTGFGKNFIT SMGFSPDAFV
     QMAFQAAYYG LYGRLENTYE PAMTKAFLHG RTEAIRTVTR ECADFVTTFW GENPAEQKIN
     ALRKATEKHT AITKECSKGQ GQDRHLYALY CLWQRSFDDG ASSASNSVSE GTNGYTSPVD
     GDSIASPKSP SPMSDDGLSS TGYSVRGVRT MPAIFSDAGW DKINTTVLST SNCGNPCLRH
     FGFGPTSADG FGIGYIIKDD TISFCASSKH RQTQRLMYTL ESYLLEIRKL LRAINQRPAS
     PRTSRAREME MISERLQIDH RRGRIVRSDT SHRGAETPTT DSGELEDDGM GGYGFFDAGM
     LLHALKGINA DRERGADKPE KRRFVGKKLR LNDY
//