ID A0A0D2BPB8_9EURO Unreviewed; 811 AA.
AC A0A0D2BPB8;
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=PV06_09161 {ECO:0000313|EMBL:KIW39387.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW39387.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW39387.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW39387.1,
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}.
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; KN847340; KIW39387.1; -; Genomic_DNA.
DR RefSeq; XP_016259603.1; XM_016410581.1.
DR AlphaFoldDB; A0A0D2BPB8; -.
DR GeneID; 27361235; -.
DR VEuPathDB; FungiDB:PV06_09161; -.
DR HOGENOM; CLU_013513_4_0_1; -.
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 53..698
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 811 AA; 90332 MW; A809CE04941371E8 CRC64;
MAAEHVERAL EAAKDVKESY SKQEKEPMSA QTLPKEHTKR GITFAAQNKL PKLPIPDLDA
TMKRYLEALA PLQTIQEHNE TRASVRDFLD HEGKDLQDRL KKYATDKTSY IEQFWYDSYL
NYDNPVVLNL NPFFLLEDDP TPARNNQVTR AASLVISALC FVRAVRKEEL PPDTLRGTPL
DMYQYSRLFG TARVPTESGC IIGQDSDSKH VVVMCRGQFY WFDVLDDNHD IIMTEKDLAI
NLQVIVNDAE EIPIQEAARG ALGVLSTENR KVWSGLRDLL TRDEGSNNAD CLSIVDSALF
MICLDYTEPA DVSQLCGNML CGTNEVVRGV QVGTCTNRWY DKLQIIVCKN GSAGINFEHT
GVDGHTVLRF ASDVYTDTIL RYAKSINGQA PTLWTSQSPD PSKRDPDSFG DVKTTPHKLE
WDMTPELSIA LRFAETRLAD LINQNEFQTL DFSGYGKNFI TSMGFSPDAF VQMAFQAAYY
GLYGRVENTY EPAMTKMFYH GRTEAIRSVT PESVDFVKTF WADNTPQKKI EALKSACQKH
TAVTKEASKA QGQDRHLYAL YCVWQRKMNE EGAELASNAD FSSNGYSSPT DPSDAGSPKR
LDERPISPTR SHAGTESSRS PGPALHQMPP LFSDAGWEKI NNTILSTSNC GNPSLRHFGF
GPVSGDGFGI GYIIKEDSIS VCASSKHRQT RRFVDSLESY LNEIRRLLKA TRPRATSGGK
LTRAREAEEV GKDGRLKSRG RAIKAEATRA DGTQTPTSMD TAEVEDDGLG GYGFFDAGML
LQALKKDAPK PAEQLAQKKR TVGKKLALTE Y
//
