ID A0A0D8Y5C4_DICVI Unreviewed; 386 AA.
AC A0A0D8Y5C4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00012352};
DE EC=2.3.1.176 {ECO:0000256|ARBA:ARBA00012352};
DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00032316};
GN ORFNames=DICVIV_01780 {ECO:0000313|EMBL:KJH52078.1};
OS Dictyocaulus viviparus (Bovine lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH52078.1, ECO:0000313|Proteomes:UP000053766};
RN [1] {ECO:0000313|EMBL:KJH52078.1, ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH52078.1,
RC ECO:0000313|Proteomes:UP000053766};
RA Mitreva M.;
RT "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX PubMed=26856411; DOI=10.1038/srep20316;
RA McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA Sternberg P.W., Gasser R.B., Mitreva M.;
RT "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT lungworm biology and support future intervention.";
RL Sci. Rep. 6:20316-20316(2016).
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; KN716171; KJH52078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8Y5C4; -.
DR STRING; 29172.A0A0D8Y5C4; -.
DR Proteomes; UP000053766; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd00829; SCP-x_thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000053766};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..116
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 254..344
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 386 AA; 42224 MW; FAA6D873FD2A234A CRC64;
MGKSKVFVIG VGMTKFCKPG SRDWDYPDMV KEAVSMALDD CSLKYSDIEQ ATVGYLFGGT
CCGQRALYEI GLTGIPIFNV NNACASGSSG VFLCKQIIES GNADCVLACG FEKMASGSLD
GQAGDGGDRV ISVDKHIQAR TKREHFAKIA WKNHLHSVHN PNSQFTKEFS LDQVINARKI
YDFMGLLECS PTSDGSAAIV ICSERFLERH PHLKPQAVEI VGMKLGTDLP SVFKENSNIK
MIGFDMIKKI STDLYRETGL TPNDVQVIEL HDCFAPNELI SYEALGLCDI GKGSTIVDRD
DNTYGGKWVI NPSGGLISKG HPIGATGVAQ VVELSNQLRG RCGKRQVPNC KLALQHNIGR
WLYFNTQTII SSTLCHLSHV IRLQIK
//
