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Database: UniProt
Entry: E3LUT7_CAERE
LinkDB: E3LUT7_CAERE
Original site: E3LUT7_CAERE 
ID   E3LUT7_CAERE            Unreviewed;       744 AA.
AC   E3LUT7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=CRE-CPT-6 protein {ECO:0000313|EMBL:EFP11092.1};
GN   Name=Cre-cpt-6 {ECO:0000313|EMBL:EFP11092.1};
GN   ORFNames=CRE_31132 {ECO:0000313|EMBL:EFP11092.1}, FL81_18859
GN   {ECO:0000313|EMBL:POM28159.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFP11092.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|EMBL:EFP11092.1};
RG   The Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:POM28159.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM28159.1};
RX   PubMed=26114425; DOI=10.1371/journal.pgen.1005323;
RA   Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA   Ahearne T.E., Cutter A.D., Phillips P.C.;
RT   "Reproductive Mode and the Evolution of Genome Size and Structure in
RT   Caenorhabditis Nematodes.";
RL   PLoS Genet. 11:e1005323-e1005323(2015).
RN   [4] {ECO:0000313|EMBL:POM28159.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM28159.1};
RX   PubMed=26394399; DOI=10.1371/journal.pgen.1005497;
RA   Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA   Ahearne T.E., Cutter A.D., Phillips P.C.;
RT   "Correction: Reproductive Mode and the Evolution of Genome Size and
RT   Structure in Caenorhabditis Nematodes.";
RL   PLoS Genet. 11:e1005497-e1005497(2015).
RN   [5] {ECO:0000313|EMBL:POM28159.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM28159.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; DS268415; EFP11092.1; -; Genomic_DNA.
DR   EMBL; LFJK02001570; POM28159.1; -; Genomic_DNA.
DR   RefSeq; XP_003112571.1; XM_003112523.1.
DR   AlphaFoldDB; E3LUT7; -.
DR   STRING; 31234.E3LUT7; -.
DR   EnsemblMetazoa; CRE31132.1; CRE31132.1; WBGene00052163.
DR   GeneID; 9824610; -.
DR   KEGG; crq:GCK72_017932; -.
DR   CTD; 9824610; -.
DR   eggNOG; KOG3716; Eukaryota.
DR   HOGENOM; CLU_013513_2_0_1; -.
DR   OMA; WKLSTSH; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
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:SF99; CARN_ACYLTRANSF DOMAIN-CONTAINING PROTEIN; 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   ECO:0000256|RuleBase:RU003801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          149..733
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        445
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   744 AA;  84845 MW;  DCBA4ABE3D6017FE CRC64;
     MSSKKTVRPP YPLPTKFPTP LEQASYKTYN WFENRLWPVK PLPFVATTVA LAATLHYKYP
     ENAILDVLPK FSSEAAEIAK TALVSAIGTY AGVFTLRKLL KYFYFSYKGF LFDNPKKPSL
     KTKIWGIVRH ILSISPPILE SCDTLLPNLP VPALKDTISE YLDSMRHILS DQELETITKQ
     AQDFLENEGK TLQRYTNLYS LFTDNYVTSF WQKYAYLHGR YPLLINSSVA HCDLLKDKEA
     TRAHRAARVT WIEVMSHLAV NRQQYKPLGD GLVCTRHYKN MYAVTRVPGE EIDQLKLHGV
     QKHIVVVLRG KYYKIHVVDD KNNIYNIEQL TKIFHEMISR DEKEDGVIGK VAALTHDSRD
     SWCKNRKKYF LENETNFKIL QEIESAVFFL TLDEDDDYGY DPERPEVLNN FLSNTLSGDG
     ANRWVDKSLN YICSKNARCG GTTEHSIADG AEFDHIMENF VYVDLEILKY QSVEEQEKMA
     IIKNDEGKTL KLATPLNFEV PDEEMLTEIT RCYEAHQVSK NDLDLFALAF RDFGKGRIKK
     CGVSPDAFIQ MAIQLANYRD QGKFVLTYEP ASARFFANSR TETLRTVNDH SCAFVEAMLN
     ENESKDAKIA LLKKACENHV LRNKKCMVGQ GVDRHLFVLY ILSQGTGTPS PFLDNYISQK
     WKLSTSHVPN VTNQCDEDTD PNNTWLGACF GAVAADGYGI CYRFGGNHGI FANITSYRSA
     ANTDSTRFAK LLAESFHELS NLFV
//
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