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Database: UniProt
Entry: A0A0D2HC71_9EURO
LinkDB: A0A0D2HC71_9EURO
Original site: A0A0D2HC71_9EURO 
ID   A0A0D2HC71_9EURO        Unreviewed;       842 AA.
AC   A0A0D2HC71;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN   ORFNames=Z520_05056 {ECO:0000313|EMBL:KIX99480.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX99480.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX99480.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX99480.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-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; KN848069; KIX99480.1; -; Genomic_DNA.
DR   RefSeq; XP_016633603.1; XM_016775560.1.
DR   AlphaFoldDB; A0A0D2HC71; -.
DR   STRING; 1442371.A0A0D2HC71; -.
DR   GeneID; 27710802; -.
DR   VEuPathDB; FungiDB:Z520_05056; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR042572; Carn_acyl_trans_N.
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; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF29; MITOCHONDRIAL CARNITINE O-ACETYLTRANSFERASE-RELATED; 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   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          83..728
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   842 AA;  93393 MW;  AE99C1E67A1CAD81 CRC64;
     MSSTGTGTRY FAHPKSLDET LNSSPRENGD LANMSKSQEE QSFEAAKETT ASYTKKEQEP
     VSLKKEVSKP GITFAAQDKL PKLPIPELDS SMKKYLDALA PLQSPQEHND TKAAVRDFLE
     NEGKDLQERL KKYATGRTSY IEQFWYDSYL NYDNPVVLNL NPFFLLEDDP TPARNNQVTR
     AASLVISALC FVRAVRKEEL PPDTLRGTPL CMYQYSRLFG TARVPTENGC IIGQDSDSKH
     VVVMCRGQFY WFDVLDDNND VIMTEKDLAI NLQVIVDDAE QTPIQEAAKG AIGVLSTENR
     KVWSHLRDLL TRDEGSNNAE CLSIVDSALF MICLDYTEPT NVSQLAGNML CGTSVVERGV
     QVGTCTNRWY DKLQIIVCKN GSAGINFEHT GVDGHTVLRF ASDVYTDTIL RFAKSINGQA
     PTLWTSQSPD PSKRDPDSFG DVSTTPHKLE WDMIPELQIA LRFAETRLAD LINQNEFQTL
     DFAGYGKNFI TSMGFSPDAF VQMAFQAAYY GLYGRVENTY EPAMTKMFFH GRTEAIRTVT
     PECVEFVKTF WADNAAQKKV DALRAATQKH TAITKESSKA QGSDRHLYAL YCVWQRKVND
     ESAEIGSTAG FSSNGYSSPT DVSDFGSPKR LEESSSPIGR SRTGTESSRS PAPALQQMPA
     LFSDAGWDKI NNTIISTSNC GNPSLRHFGF GPTSGDGFGI GYIIKDDTIS ICASSKHRQT
     QRFVDSLESY LNEIRRLLRA TKTKDAAASK ITRAREAEEK AGKDGRLKSR GRIIKTEASK
     VDGFQTPTSL DTAEVEDDGL GGYGFFDAGM LLQALKKDQP KPSEQIAQRR KAVGKKLALS
     EY
//
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