ID   M7TD14_BOTF1            Unreviewed;       639 AA.
AC   M7TD14;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative choline carnitine o-acyltransferase protein {ECO:0000313|EMBL:EMR81316.1};
GN   ORFNames=BcDW1_10144 {ECO:0000313|EMBL:EMR81316.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR81316.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; KB708083; EMR81316.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7TD14; -.
DR   STRING; 1290391.M7TD14; -.
DR   HOGENOM; CLU_013513_5_1_1; -.
DR   Proteomes; UP000012045; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          64..614
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          25..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        355
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   639 AA;  72540 MW;  04997E1EC75FB8FC CRC64;
     MLKLLAKGRT QSPVLRNSFT STRVSRTLGM APANSRSNSS LPAGYKEDST KGPMLRFEES
     LPKLPVPTLE ETAVRYLKSV HPLLTSSELQ NTTKAVQEFI KPGGIGSKLQ EKLLARREDP
     KHKNWIYEWW NDAAYLSYRD PVVPYVSYFY SHRDDRRRRD PSKRAAAIST AVLEFKKQVD
     SGTLEPEYMK KLPISMESYQ WMFNASRVPS KPADHPVKYA AEENKHILVI RKNQFFKVMH
     EVDGNQLNTS ELEQQFKRIY EKAEKTPAVG ILTSENRDIW TDAREVLLKA NPSNAKILKD
     IESASFVVCL DDASPVTLEE RAHQYWHGDG ANRWFDKPLQ FIINDNGTSG FMGEHSMMDG
     TPTHRLNDYV NEVIFNNKLD FSDPSIRSNL PDPTPLKFHI TKEVQSEIER ATKDFNEVIA
     AHELRVQAYQ GYGKGLIKKF KCSPDAYVQM IIQLAYFKMY GKNRPTYESA ATRRFQQGRT
     ETCRSVSDDS VAFCKAISDH TVEPSKAVAA FRAAINSHVE YITAASDGKG VDRHLFGLKK
     LLEPGEELPA IYQDPTYGYS SKWFISSSQL SSEYFNGYGW SQVVDDGWGI AYMINENSIQ
     FNVVSKGLGS ERMSFYLNEA AGDIRDLLMP TLEPAKAKL
//