The domain within your query sequence starts at position 92 and ends at position 456; the E-value for the MCD domain shown below is 1.3e-120.

QGFGVDHGQVAEQSAGVLQLRQQAREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVR
FLVQLRADLLEAQALKLVEGPHVREMNGVLKSMLSEWFSSGFLNLERVTWHSPCEVLQKI
SECEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISNNIQGIVKEC
PPTETEERNRIAAAIFYSISLTQQGLQGVELGTFLIKRVVKELQKEFPQLGAFSSLSPIP
GFTKWLLGLLNVQGKEHGRNELFTDSECQEISAVTGNPVHESLKGFLSSGEWVKSEKLTQ
ALQGPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVMWRINWMADSSLKGLTSSCGLMV
NYRYY

MCD

 MCD
PFAM accession number:PF05292
Interpro abstract (IPR007956):

Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidised. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK) [ (PUBMED:12065578) ].

This entry represents the C-terminal catalytic domain of Malonyl-CoA decarboxylase [ (PUBMED:23791943) ].

GO process:fatty acid biosynthetic process (GO:0006633)
GO function:malonyl-CoA decarboxylase activity (GO:0050080)

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