ID   A0A1E1KR93_9HELO        Unreviewed;       640 AA.
AC   A0A1E1KR93;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|EMBL:CZT00526.1};
GN   ORFNames=RCO7_02997 {ECO:0000313|EMBL:CZT00526.1};
OS   Rhynchosporium commune.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Ploettnerulaceae; Rhynchosporium.
OX   NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT00526.1, ECO:0000313|Proteomes:UP000178129};
RN   [1] {ECO:0000313|EMBL:CZT00526.1, ECO:0000313|Proteomes:UP000178129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UK7 {ECO:0000313|EMBL:CZT00526.1,
RC   ECO:0000313|Proteomes:UP000178129};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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; FJUW01000020; CZT00526.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E1KR93; -.
DR   STRING; 914237.A0A1E1KR93; -.
DR   InParanoid; A0A1E1KR93; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000178129; 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; 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:UP000178129};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          65..615
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          24..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        356
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   640 AA;  72290 MW;  E583EAAC49628663 CRC64;
     MLKAISKGRT SPLLRSSFTA TRPSLSRTLG MAPANARSNS SLPSGYKEDA SKGPMLRFEE
     SLPKLPVPTL EETSARYLKS VHPLLSPSEF ESTTKAVQDF IKPGGIGSKL QEKLLARRAD
     PKHKNWIYEW WNAAAYLTYR DPVVPYVSYF YSHRDDRRRR DPAKRAAAIS TAVLEFKKHV
     DAGTLEPEYM KKLPISMESY QWMFNCSRIP AKPADYPQKY PAKENNYIIA VRKNQFFKVY
     HEVDGKQLNT SELEQQFKSI YQRAEKVPAI GILTTENRDV WTDAREVLLK AHSSNAAALK
     TIEASSFVVC LDDASPVTLE ERAHAYWHGD GANRWFDKPL QFIINDNGTS GFTGEHSMMD
     GTPTHRLNDY VNEMTFNNKL DFSNPSIRSN LPEPSVVKFH INKEVQAEIE HATKDFTEVI
     GSHELRVQAY QGYGKGLIKK FKCSPDAYVQ MVIQLAYFKM YGKNRPTYES AATRRFQQGR
     TETCRSVSDD SVAFCKAISD HSVENETAIS AFRKAITSHV EYISAASDGK GVDRHLFGLK
     KLLGPNEELP AIYKDPAYAY SSKWFISSSQ LSSEYFNGYG WSQVVDDGWG IAYMINENSI
     QFNVVSKGLG SERMSFYLNE AAGDIRDLLI PTLEAPKAKL
//