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Database: UniProt
Entry: G3B2T4_CANTC
LinkDB: G3B2T4_CANTC
Original site: G3B2T4_CANTC 
ID   G3B2T4_CANTC            Unreviewed;       839 AA.
AC   G3B2T4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN   ORFNames=CANTEDRAFT_120712 {ECO:0000313|EMBL:EGV64756.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV64756.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; GL996515; EGV64756.1; -; Genomic_DNA.
DR   RefSeq; XP_006685562.1; XM_006685499.1.
DR   AlphaFoldDB; G3B2T4; -.
DR   STRING; 590646.G3B2T4; -.
DR   GeneID; 18248797; -.
DR   KEGG; cten:CANTEDRAFT_120712; -.
DR   eggNOG; KOG3719; Eukaryota.
DR   HOGENOM; CLU_013513_4_1_1; -.
DR   OrthoDB; 2002955at2759; -.
DR   Proteomes; UP000000707; 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:SF48; CARNITINE O-ACETYLTRANSFERASE YAT2; 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   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          13..635
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          796..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..812
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  95119 MW;  6E6BF76AE40362B2 CRC64;
     MSTYQNEQSL PSLPVPELSS TVHQLLIALQ PLVSSEEYSQ LLNESTEFLN NHLVNTIQTN
     FLAARHNPRH SCYLNCINDE FHPGIYGELR GDVLPRNPYL VLQEDPYSKF MNPPNQSQRA
     ANLVNSSLKF IVSLRNETLP PDLTPRNKNP LTMNCYRNLF GSTRVPDMAE SPHAYHQISI
     KTSRDPVHSN HIVVVSCNQF YYLPVLSEHQ EIFFNDYDLS LIFQQILDES TRFDVVESIN
     NAIGALTTQN YSHWKWGRAE LMRSNASSLD LIDKALFVVV LDPNSPTTDQ DKTMVISHGT
     SVLSSNNAQG GSCTSRWYDK LQLIVTKNSV AGVVWECTSS DSTAILRFIS DIYTDSILKL
     AKNINAIEYS LFGDVRFVSN KLPKPSFQRL VFKKTPELSN LIHLSETRLA DLINQHSYTS
     IKIKLNTELL NSYGVSTDSF LQVCIQIANY SLYGKVSNTL EPITTRKFKD SRTEMIAVQN
     DEIANLVKLF ITNSSRAEKW SLFERCCKIH LKQYTDAMQG KGFERHLTSL LHVIKSPKAS
     EFLNTLNAQA GVEKLPEFDV LRSQYVPLLS NPILNRILSP ELLISNCGNP ALYLFGIPPP
     TDQGFGIGYV IHKDKVLLTL CSKFRQNERF LSTLVKIINE VKAMVVSRSD FLVEINKDND
     YRIHELQKLR VEQELKNLNF DSPSTKHPIE ISVDSFTIPL DMSLKHQAAP DTDDELDYES
     SNSNNSAEFD YLGGYGYFDF GELDSRNIEL NRSQSFLNSP SNLSSLSSRN PSQHNLSVLA
     KNLDLKEKHD LNERIREKLN KSADDLPRFK SPESPTVKDP QIEKGNPKHK IGRPLNISK
//
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