The domain within your query sequence starts at position 243 and ends at position 360; the E-value for the Ketoacyl-synt_C domain shown below is 3.7e-38.

YATILNAGTNTDGSKEQGVTFPSGEVQEQLICSLYQPAGLAPESLEYIEAHGTGTKVGDP
QELNGITRSLCAFRQAPLLIGSTKSNMGHPEPASGLAALTKVLLSLEHGVWAPNLHFH

Ketoacyl-synt_C

Ketoacyl-synt_C
PFAM accession number:PF02801
Interpro abstract (IPR014031):

Beta-ketoacyl-ACP synthase EC 2.3.1.41 (KAS) [(PUBMED:3076376)] is the enzyme that catalyzes the condensation of malonyl-ACP with the growing fatty acid chain. It is found as a component of a number of enzymatic systems, including fatty acid synthetase (FAS), which catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH; the multi-functional 6-methysalicylic acid synthase (MSAS) from Penicillium patulum [(PUBMED:2209605)], which is involved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzyme systems; Emericella nidulans multifunctional protein Wa, which is involved in the biosynthesis of conidial green pigment; Rhizobium nodulation protein nodE, which probably acts as a beta-ketoacyl synthase in the synthesis of the nodulation Nod factor fatty acyl chain; and yeast mitochondrial protein CEM1. The condensation reaction is a two step process, first the acyl component of an activated acyl primer is transferred to a cysteine residue of the enzyme and is then condensed with an activated malonyl donor with the concomitant release of carbon dioxide.

This entry represents the C-terminal domain of beta-ketoacyl-ACP synthases. The active site is contained in a cleft betweeen N- and C-terminal domains, with residues from both domains contributing to substrate binding and catalysis [(PUBMED:11152607)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ketoacyl-synt_C