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Database: UniProt
Entry: A0A0D2AH07_9EURO
LinkDB: A0A0D2AH07_9EURO
Original site: A0A0D2AH07_9EURO 
ID   A0A0D2AH07_9EURO        Unreviewed;       849 AA.
AC   A0A0D2AH07;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN   ORFNames=PV06_09161 {ECO:0000313|EMBL:KIW39386.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW39386.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW39386.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW39386.1,
RC   ECO:0000313|Proteomes:UP000053342};
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 Exophiala oligosperma CBS72588.";
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; KN847340; KIW39386.1; -; Genomic_DNA.
DR   RefSeq; XP_016259602.1; XM_016410580.1.
DR   AlphaFoldDB; A0A0D2AH07; -.
DR   STRING; 215243.A0A0D2AH07; -.
DR   GeneID; 27361235; -.
DR   VEuPathDB; FungiDB:PV06_09161; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000053342; 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; 2.
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:UP000053342};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          91..736
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          430..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..771
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        397
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   849 AA;  94323 MW;  73344D4A907C11EB CRC64;
     MINLLTMPIS IAGTRYFSQP ASIGDTLSRA SPKAEVDGMA AEHVERALEA AKDVKESYSK
     QEKEPMSAQT LPKEHTKRGI TFAAQNKLPK LPIPDLDATM KRYLEALAPL QTIQEHNETR
     ASVRDFLDHE GKDLQDRLKK YATDKTSYIE QFWYDSYLNY DNPVVLNLNP FFLLEDDPTP
     ARNNQVTRAA SLVISALCFV RAVRKEELPP DTLRGTPLDM YQYSRLFGTA RVPTESGCII
     GQDSDSKHVV VMCRGQFYWF DVLDDNHDII MTEKDLAINL QVIVNDAEEI PIQEAARGAL
     GVLSTENRKV WSGLRDLLTR DEGSNNADCL SIVDSALFMI CLDYTEPADV SQLCGNMLCG
     TNEVVRGVQV GTCTNRWYDK LQIIVCKNGS AGINFEHTGV DGHTVLRFAS DVYTDTILRY
     AKSINGQAPT LWTSQSPDPS KRDPDSFGDV KTTPHKLEWD MTPELSIALR FAETRLADLI
     NQNEFQTLDF SGYGKNFITS MGFSPDAFVQ MAFQAAYYGL YGRVENTYEP AMTKMFYHGR
     TEAIRSVTPE SVDFVKTFWA DNTPQKKIEA LKSACQKHTA VTKEASKAQG QDRHLYALYC
     VWQRKMNEEG AELASNADFS SNGYSSPTDP SDAGSPKRLD ERPISPTRSH AGTESSRSPG
     PALHQMPPLF SDAGWEKINN TILSTSNCGN PSLRHFGFGP VSGDGFGIGY IIKEDSISVC
     ASSKHRQTRR FVDSLESYLN EIRRLLKATR PRATSGGKLT RAREAEEVGK DGRLKSRGRA
     IKAEATRADG TQTPTSMDTA EVEDDGLGGY GFFDAGMLLQ ALKKDAPKPA EQLAQKKRTV
     GKKLALTEY
//
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