ID   A8XQK3_CAEBR            Unreviewed;       560 AA.
AC   A8XQK3;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Protein CBG17205 {ECO:0000313|EMBL:CAP34928.2};
GN   ORFNames=CBG17205 {ECO:0000313|EMBL:CAP34928.2,
GN   ECO:0000313|WormBase:CBG17205}, CBG_17205
GN   {ECO:0000313|EMBL:CAP34928.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP34928.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP34928.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP34928.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; HE601483; CAP34928.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XQK3; -.
DR   STRING; 6238.A8XQK3; -.
DR   WormBase; CBG17205; CBP40923; WBGene00036912; -.
DR   eggNOG; KOG3718; Eukaryota.
DR   HOGENOM; CLU_013513_5_0_1; -.
DR   InParanoid; A8XQK3; -.
DR   OMA; DVWAKDY; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IBA:GO_Central.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
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:SF5; CARN_ACYLTRANSF DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          14..494
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   DOMAIN          500..546
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        308
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   560 AA;  63654 MW;  F4ADF06E3AE144A9 CRC64;
     MESTFSHQNS IPSLPLPGLK DTIEKYLKSL SPIDSKEELE HVTSLARGFG DSENGRKLQN
     FLELKSSSSK NWLEDWWYDA YTTNQDTLLT QNMGAIIPKS FMSNTSQIGM ASQIIHHLMN
     YWSRVRHEKI EITKSRGINW DMSQVYNLFN ACRTPAVSKD KIERYFCTES EGFCPSHIVV
     LYNGHIWKME TVQNGKILSV PEIRNILEII KSGSNRTDEN SIVKLTSLER DTWAKIRESM
     ICNSSRNRKM FEAIDSAVLC LTLANDFVEN DSELMKYSIF GSPLNAYMDK NLNIIVLKDG
     KACLQAEHGN VDAISLFAPC DFAADQFLDD SELSEKTLEN SSSTPTIEKI DFLLTGSVSS
     RIAEAEKQFF ALSSRINVNV YHYSNFGATF CKSRKLYADT IIQIALQMAY LKTHNKLAPI
     YETASTRKFY HGRTETVRSL TPDLAKYLEA CENSATNETI KTLFFDAYNS HNTLMDAARD
     GKGIDRHFLG LSFLGYNENG CFGYVVPMCK DGYGAFYRIN ASRFTFTLSN YFDDATNGDE
     FRENLEYSLD FIKNVIVTNE
//