ID A8WW80_CAEBR Unreviewed; 451 AA.
AC A8WW80;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Protein CBG04103 {ECO:0000313|EMBL:CAP24889.2};
GN ORFNames=CBG04103 {ECO:0000313|EMBL:CAP24889.2,
GN ECO:0000313|WormBase:CBG04103}, CBG_04103
GN {ECO:0000313|EMBL:CAP24889.2};
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:CAP24889.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP24889.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP24889.2,
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 C/M/P thioester hydrolase family.
CC {ECO:0000256|ARBA:ARBA00006538}.
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DR EMBL; HE600956; CAP24889.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WW80; -.
DR STRING; 6238.A8WW80; -.
DR ESTHER; caebr-A8WW80; Acyl-CoA_Thioesterase.
DR WormBase; CBG04103; CBP39671; WBGene00026843; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; A8WW80; -.
DR OMA; CHATRIY; -.
DR OrthoDB; 5356064at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.2240; Acyl-CoA thioester hydrolase/BAAT N-terminal domain; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR PANTHER; PTHR10824; ACYL-COENZYME A THIOESTERASE-RELATED; 1.
DR PANTHER; PTHR10824:SF10; PROTEIN CBG04103; 1.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008549}.
FT DOMAIN 14..134
FT /note="Acyl-CoA thioester hydrolase/bile acid-CoA amino
FT acid N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04775"
FT DOMAIN 197..428
FT /note="BAAT/Acyl-CoA thioester hydrolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08840"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
FT ACT_SITE 377
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
SQ SEQUENCE 451 AA; 51380 MW; 288860207DA750AC CRC64;
MSIHVDKPDS MQNELVEIQA LGLTPNQIYT FRMTLKHDYG THRSEATFKS DPAGRIDLKC
ASPLRGSYHD ADPMGLFLGM KPCEDFAYGG YLRCTPPIPF YYHLQLFNSV GTLIDETYIK
KHWMHPKLER IEMEDDGFCA TLFKPPGDGP FPAVLDLSGT GGGIHEHKGA MLASEGFVVL
CVAFFQYKYL PNKMEEVNME YFSKPIEYLA NLPYTLNVIG IQGVSFGATI VDLLATRHGD
KIKAVVSING PQVVSDYLYM QENGEPIPHL SHGQVTLEHC QFINGVMCSH RNFQIMTEKL
TPETEIPWSR IPTDVKIRVL GSVDDLCQPS VHATLYRQRR LKETGHDVEV RVQKYILEFI
QNQKKFVFQV EMVNGGHIME PPYFPHHELV YAKYQGFYCG YGGEVLLHAK SQEKTWANSI
KFFQRALGKT KHIEDWQRLE LILPPRGESK L
//