ID G0V9A8_NAUCC Unreviewed; 902 AA.
AC G0V9A8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN Name=NCAS0A15010 {ECO:0000313|EMBL:CCC68059.1};
GN OrderedLocusNames=NCAS_0A15010 {ECO:0000313|EMBL:CCC68059.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC68059.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC68059.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) 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; HE576752; CCC68059.1; -; Genomic_DNA.
DR RefSeq; XP_003674437.1; XM_003674389.1.
DR AlphaFoldDB; G0V9A8; -.
DR STRING; 1064592.G0V9A8; -.
DR GeneID; 11529220; -.
DR KEGG; ncs:NCAS_0A15010; -.
DR eggNOG; KOG3719; Eukaryota.
DR HOGENOM; CLU_013513_4_1_1; -.
DR InParanoid; G0V9A8; -.
DR OMA; YADGYYK; -.
DR OrthoDB; 2002955at2759; -.
DR Proteomes; UP000001640; Chromosome 1.
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; 2.
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.
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:UP000001640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 26..700
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 212..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 101944 MW; 94442AFE14056BBD CRC64;
MTTALEIDTN IDTVHTFSQE DKLPKLPLPD LKNTLRDLKK SLEPLYYADG YYKHPLDPVQ
IKGLTSALST FLGSDAALKL QAKLRTYYDN NDCYLDKLHL DINNHSSSRE IDDDILPRNP
FLILADDAVP DITQSARSAV LVHSALRFIS ALKQELLPPD TNNKDVPLSM VPYLNLFGTT
RCPVFQEGEV ENFDLDKPYT ASDLDNEDSF LSEDEYEDES DDQNKTKSFT QSRPTSSNSA
VSDDEDDIFT RHGITIDRHP DSKHILVISK GQYYTIEVLD DENKILYTEG RLSILFNQIL
TDSEESYSFK RSTALGSLTS HSFRNWKYAR KRLQKRYPQE LRLIDSALFV LVLDESTEQA
NEENTKRLFY GTSIIDNKGH QVGSCVSRWY DKLQLVVTKD ATAAVIWDSF TCDGSVVLRF
ISETFTEAVL RLAREVNAGD PQFSLWPNVM PSELAPKPAD FHPSSIVNKI DWSFSNILNT
HVHLSETKLA DLISKHDIVH RSISVGRRSA QRLGVKPDSM IQIALQIAHY SLYGKMAFGF
EPISTRGFKN SRSSFVNIQN QDLLELCQLF ISTSTDNQTK LDKFVQTCEK HSEKVRKAKL
GEGFEKHFNA LKYLYKFHSH FGIDFTEEDE KIASDVFNNT LIAPFSQPEL IVANCGTSAT
TQFGITPAIP QGFGIGYIIK DDQCDLTVTS QFRQGDRLIY MLNYVLNEFR SYWRVARETS
RNKTGIKISR SVDRLYQLDN ALNSVIDNSE GTPESAHRHH HSHHDHSQQK TGFFDLDAHL
DSSRSVSSTP SLSNIASRLA ELTVTRDSSR NHSSLALSVP TVNEKLNTGH QILQIHPNHV
DGSSGSEVST PNDSRPHSGF SSRRDSGASS TRPESKRQNV INSKFDIDFD RSRVGRKVST
YE
//
