ID A0A016TIH5_9BILA Unreviewed; 347 AA.
AC A0A016TIH5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Thiolase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0100.g3325 {ECO:0000313|EMBL:EYC02475.1};
GN Synonyms=Acey-B0303.3 {ECO:0000313|EMBL:EYC02475.1};
GN ORFNames=Y032_0100g3325 {ECO:0000313|EMBL:EYC02475.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC02475.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC02475.1}.
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DR EMBL; JARK01001436; EYC02475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016TIH5; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; 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; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 7..247
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 254..320
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 347 AA; 37529 MW; D1F3630FD5AD7EA8 CRC64;
MYPTYRTLVA RTHIPYKDID HIICGTVIQE CKTSNVAREA ALQAGIPDKI PCHTVTLACI
SSNVAMTTGM GMLATGNAKA IIAGGVELLS DVPIRYNRKA RKAMLGMQKA KAVADKLKIG
GDIVMNLLSP ELPAVAEFST GETMGHSGDR LAAAFNVSRK EQDEFALRSH TLAKAAAEAG
KLKDIIPVFL DGKKPQTVKA DNGIRISTME KMASLKPAFV KPHGTITAAN ASYLTDGASA
CLIMTEDFAL ANGYKPIAYL RDYQYVAQDP KDQLLLSPAY VIPKLLEKAG LGLNDISVFE
IHEAFAGQVL ANLNALDSDY FCKVFQFSSL YFALFIDIPN DLLYSSK
//
