ID   V2YVU4_MONRO            Unreviewed;       652 AA.
AC   V2YVU4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Carnitine acetyl transferase {ECO:0000313|EMBL:ESK95814.1};
GN   ORFNames=Moror_12426 {ECO:0000313|EMBL:ESK95814.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95814.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK95814.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95814.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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:ESK95814.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWSO01000061; ESK95814.1; -; Genomic_DNA.
DR   RefSeq; XP_007844901.1; XM_007846710.1.
DR   AlphaFoldDB; V2YVU4; -.
DR   STRING; 1381753.V2YVU4; -.
DR   KEGG; mrr:Moror_12426; -.
DR   HOGENOM; CLU_013513_5_1_1; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000017559; 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:UP000017559};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ESK95814.1}.
FT   DOMAIN          66..626
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..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        360
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   652 AA;  73530 MW;  431F3F137DF4B089 CRC64;
     MLRTISRSYG YHIVTPMPAV ISSKSRSSGF KLSPSRSMSS ETPPPGYSID PKAGPMLRYQ
     ASLPRLPVPS LSSTASKYLE TVRPHVSDTE YKRTESLINA FVASPQAAEL QKRLEARAAD
     PNVKNWLADW WNEIAYMGYR DPVVVFVSYF YVHLDDRLRK DPAKRAASLI KAMLPFRELT
     ESQQLEPEKV RGAPLCMDSY KWLFHSSRYP KKPSDTARKF DPATHNHIVF VRKNKFYSIP
     LVNKSGCELS AAELEVQIER IIRHAGQTPA LPIGALTSDN RDLWTDARDA LIAASPSGIN
     VKSLETIESA MIVVCLDDKK PVTREDISWQ CWVGDGKNRF YDKHQLIVFD NGRSGFLGEH
     SCMDGTPTLR MNEFVLASIA LNKIDFGTTR AEETGSDLPE PTELKFEVND QVKRLIQEAV
     SRFDELVGKH DLHVLHYEGY GKNLIKQFKA SPDAWAQLVK QLAFHKMFGR PGVTYESAQT
     RKYQLGRTEV IRSASNESKK WAEAMLDPHE TDINRATLFR AAVKRHLQYA AWAADGQGVD
     RHLLGLKKSL KDDEPVPEVY GDPSFSKTSH WELSTSQLSS DYFDGWGYGE VVPDGYGLSY
     AIGDSYIRWT ITSLKRNTAE LKHYLAEAAT ETRAMMEKAM ASEKQNSGKE KL
//