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Database: UniProt
Entry: A0A0K0D174_ANGCA
LinkDB: A0A0K0D174_ANGCA
Original site: A0A0K0D174_ANGCA 
ID   A0A0K0D174_ANGCA        Unreviewed;       548 AA.
AC   A0A0K0D174;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetyl-CoA acetyltransferase, cytosolic {ECO:0000313|WBParaSite:ACAC_0000381901-mRNA-1};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000381901-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000381901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982}.
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DR   AlphaFoldDB; A0A0K0D174; -.
DR   STRING; 6313.A0A0K0D174; -.
DR   WBParaSite; ACAC_0000381901-mRNA-1; ACAC_0000381901-mRNA-1; ACAC_0000381901.
DR   Proteomes; UP000035642; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF156; ACETYL-COA ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   Pfam; PF00108; Thiolase_N; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 3.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035642}.
FT   DOMAIN          91..240
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          361..516
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
SQ   SEQUENCE   548 AA;  57674 MW;  A10D3CF20EEE3E0D CRC64;
     LFTALQEVFI VGSARTPIGS FRSQLASVPA PQLGSVAIKA ALERSGLKPD NVEEVFMGHV
     CQANVGQAPA RQAALGAGLN VSTIVTTVNK VVIGGGMESM SQVPFYLNRG ETTYGGMQLF
     DGIVKDGLTD AYDHCHMGNC GEKTAKDLAI SREEQDEYAI GSYTKSTSAW STGIMASEIV
     PVTVKTRKGT AVVDTDEEFK NFDPEKLKKL KTVFQKDGTI TAGNASTLND GAAAVLLASA
     EACKQYGCKP QAKILTFADA ATKPLDFSIA PVLVIPKMLQ NIGLKMTDID HWEVNEAFSV
     VAVAFIKQIG CDANKVNPHG GAVSIGHPIG MSGARLITHL VHTLKSGQKG CAAICNGGGG
     ATRTPIASFR GSFSSISAVE LASVAARTAL VRSGIEPSDI EETLVGSVLT ASCGQNIARQ
     LALSIGTPKS SQAVTINKVC SSSMKALAFA ALSIKSGYRK KVLVAGCENM SQVPFYLSRG
     EIPYGGTNIV DGVVRDGLED AMLKSHMGLC AEKSVKVKKW SFTDKFFFII SSKFLYSIVS
     MGGCSVVL
//
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