The domain within your query sequence starts at position 23 and ends at position 215; the E-value for the LCM domain shown below is 3.6e-41.

GVRGTCEDASLCKRFAVSIGYWHDPYIEHLVRQSKERKAPEINRGYFARVHGVSQLIKAF
LRKTECHCQILNLGAGMDTTFWKLKDEGLLPNKYFEVDFPMIVTRKLLTIKSKPLLFRPI
MELHPEDTLQMDSHMLDSKRYAIIGADLRDLSELEEKLKKCNMNTQLPTLLITECVLVYM
TPEQSANLLKWAA

LCM

LCM
PFAM accession number:PF04072
Interpro abstract (IPR007213):

This entry includes a group of methyltransferases such as leucine carboxyl methyltransferase 1 (known as Ppm1 in yeast and LCMT1 in mammals), leucine carboxyl methyltransferase 2 (Ppm2/LCMT2) and O-methyltransferase TcmP.

Ppm1 regulates the activity of serine/threonine phosphatase 2A (PP2A) through methylation of the C-terminal leucine residue of the catalytic subunit of PP2A [(PUBMED:10600115), (PUBMED:11697862), (PUBMED:11060018)]. This affects the heteromultimeric composition of PP2A which in turn affects protein recognition and substrate specificity. Like many other methyltransferases Ppm1 uses S-adenosylmethionine (SAM) as the methyl donor. Ppm1 contains the common SAM-dependent methyltransferase core fold, with various insertions and additions creating a specific PP2A binding site [(PUBMED:14660564)]. Ppm2, a homologue of Ppm1, is a S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway, which is part of tRNA modification [(PUBMED:16642040)].

Streptomyces glaucescens TcmP is an O-methyltransferase that catalyses the methylation of the C-9 carboxy group of tetracenomycin E (TCM E) to yield TCM A2, which is then further processed to produce the antibiotic TCM C [(PUBMED:11009387)].

GO process:methylation (GO:0032259)
GO function:methyltransferase activity (GO:0008168)

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