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Database: UniProt
Entry: A0A0M8N208_9HYPO
LinkDB: A0A0M8N208_9HYPO
Original site: A0A0M8N208_9HYPO 
ID   A0A0M8N208_9HYPO        Unreviewed;       609 AA.
AC   A0A0M8N208;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|EMBL:KOS21487.1};
GN   ORFNames=ESCO_005267 {ECO:0000313|EMBL:KOS21487.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21487.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS21487.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOS21487.1}.
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DR   EMBL; LGSR01000008; KOS21487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8N208; -.
DR   STRING; 150374.A0A0M8N208; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000053831; 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   Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          34..587
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   609 AA;  69146 MW;  7D15F88EE9936E32 CRC64;
     MAPARRHNSS LPSGYVEDKS KGAMLRFQES LPRLPVPTLE ETAKRYLKSL HPLLSKTEFE
     ASKTTVSEFI KPGGTGSKLQ EKLIARREDP EIKNWMLEWW NDTAYLAYRD PVVPYVSYFY
     SHRDDRKRRN PAKRAAAITT AALEFKKQVD SGSLEPEYMK KLPICMDSYK WMFNASRVPA
     PSVDHPVKFS HLENKHIIVI RKNQFFKVEH EIGGKQLNTS ELEHQFNRIY QLAKPVAPIG
     ALTSENRDIW ADARVTLLQA SPKNKDALGA IESASFVVCL DDASPVTLEE RARQYWHGDG
     ANRWYDKPVQ FIVNDNGTSG FMGEHSMMDG TPTHRLNDFV MDLIFGNKID FSDPAVRSNL
     PEPQVIDFVI TPKVQGEIDR AIIDFRKVIG EHQLVVQAYQ AYGKGLIKKF KCSPDAYVQM
     IIQLAYFKMY GKNRPTYESA ATRRFQQGRT ETCRTVSDES VAWCQSMADN NLDDNTRVDL
     LHKAIKAQQE YISAASDGKG VDRHLFGLKK LLEPGQELPA IYKDPAYGYS CSWYLSTSQL
     SSEYFNGYGW SQVIDGGFGI AYMINENGIN FNIVSKNLGS DKMSYYLNEA ANDMRDLLTP
     TLEPPKAKL
//
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