ID A0A0U1LKF1_TALIS Unreviewed; 636 AA.
AC A0A0U1LKF1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|EMBL:CRG82886.1};
GN ORFNames=PISL3812_00233 {ECO:0000313|EMBL:CRG82886.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG82886.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG82886.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG82886.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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; CVMT01000001; CRG82886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1LKF1; -.
DR STRING; 28573.A0A0U1LKF1; -.
DR OMA; ENHSKGP; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000054383; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000054383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CRG82886.1}.
FT DOMAIN 62..613
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 636 AA; 72313 MW; 792B34781D9D02B8 CRC64;
MVQEHGNDGE KRTEEQQVCF ASRFALKLPD PESERYLTKN IGHKEDPFKG PMLRFEESLP
KLPVPPLEET AAKYLKSVQP LLSSSELAST TKAVQDFIRP DGVGHKLQEK LIARRNDPKI
RNWLYDWWND AAYLAYRDSV IYSSYFYSHR DDRKRRIPSK RAAAISTAVL EFKKQVDQGT
LEPEYAKTQP MAMDSYQWLF NVSRVPARPS DYPVKYSFTE HKHILVIRKN QLFKVLHEVD
GKQLNTAELE QQFERVYAKA EKGPALGALT TEHRDIWTDA REILLRAHPS NAKALKEVES
ASFVVCLDDA SPVTLEERAH QYWHGDGANR WYDKPAQFII NDNGTAGFMG EHAMMDGTST
LRLNEFVNNV VFKNTLDFSD SSVRSHLPDP TLIHFHVTKE LQAEIERAQK DFNEVIDAHE
LRVQAYQAYG KGLIKKLKCS PDAYVQMIIQ LAYFKMYGKN RPTYESVMTR RFQQGRTEAC
RSVSAESVAF CKAMADDSLD ASEKAVLFHK ALKAHVAYVA QASVGQGVDR HLFGLKKLLG
PDDEVPAIYQ DPAYAYSSTW FISTSQLSSE FLNGFGWSQV VDPGFGIAYM INENSINFNI
ISKKLGSDRM SFYLNEAAGD IRDLLLSTLE PAKAKL
//